Human Metabolome Database Version 2.5

Showing metabocard for NAD (HMDB00902)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2005-11-16 15:48:42

Update Date

2010-04-06 13:00:13

Accession Number

HMDB00902

Secondary Accession Numbers

Not Available

Common Name

NAD

Description

NAD (or Nicotinamide adenine dinucleotide) is used extensively in glycolysis and the citric acid cycle of cellular respiration. The reducing potential stored in NADH can be converted to ATP through the electron transport chain or used for anabolic metabolism. ATP "energy" is necessary for an organism to live. Green plants obtain ATP through photosynthesis, while other organisms obtain it by cellular respiration. (wikipedia). Nicotinamide adenine dinucleotide is a A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)

Synonyms

3-Carbamoyl-1-D-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate
3-Carbamoyl-1-beta-D-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt
Adenine-nicotinamide dinucleotide
CO-I
Codehydrase I
Codehydrogenase I
Coenzyme I
Cozymase
Cozymase I
Diphosphopyridine nucleotide
Endopride
NAD trihydrate
NAD-oxidized
Nicotinamide adenine dinucleotide
Nicotinamide dinucleotide
Nicotineamide adenine dinucleotide
Oxidized diphosphopyridine nucleotide
Pyridine nucleotide diphosphate
[(3S,2R,4R,5R)-5-(6-Aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl {[(3S,2R,4R,5R)-5-(3-carbamoylpyridyl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxyphosphoryl) hydrogen phosphate
[adenylate-32-P]-NAD
beta-Diphosphopyridine nucleotide
beta-NAD
beta-Nicotinamide adenine dinucleotide
beta-Nicotinamide adenine dinucleotide trihydrate
diphosphopyridine nucleotide oxidized
nicotinamide adenine dinucleotide oxidized
3-Carbamoyl-1-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate
3-Carbamoyl-1-beta-delta-ribofuranosylpyridinium hydroxide 5'-ester with adenosine 5'-pyrophosphate inner salt

Chemical IUPAC Name

[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-[[(2S,3S,4R,5R)-5-(5-carbamoylpyridin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-oxido-phosphoryl]oxy-phosphinic acid

Chemical Formula

C₂₁H₂₈N₇O₁₄P₂

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Nucleosides and Nucleoside conjugates
Class
Nucleotides
Sub Class
Nucleotide diphosphates
Family
Mammalian Metabolite
Species
cation secondary alcohol 1,2-diol primary amine primary aromatic amine primary carboxylic acid amide phosphoric acid ester aromatic compound heterocyclic compound
Biofunction
Component of Aminosugars metabolism Component of Androgen and estrogen metabolism Component of Arginine and proline metabolism Component of Ascorbate and aldarate metabolism Component of beta-Alanine metabolism Component of Bile acid biosynthesis Component of Butanoate metabolism Component of C21-Steroid hormone metabolism Component of Cysteine metabolism Component of D-Glutamine and D-glutamate metabolism Component of Fatty acid metabolism Component of Folate biosynthesis Component of Fructose and mannose metabolism Component of Galactose metabolism Component of Glutamate metabolism Component of Glutathione metabolism Component of Glycerolipid metabolism Component of Glycerophospholipid metabolism Component of Glycine, serine and threonine metabolism Component of Glyoxylate and dicarboxylate metabolism Component of Histidine metabolism Component of Inositol metabolism Component of Methane metabolism Component of Nicotinate and nicotinamide metabolism Component of Nitrogen metabolism Component of Nucleotide sugars metabolism Component of Phenylalanine metabolism Component of Porphyrin and chlorophyll metabolism Component of Propanoate metabolism Component of Prostaglandin and leukotriene metabolism Component of Purine metabolism Component of Pyruvate metabolism Component of Retinol metabolism Component of Starch and sucrose metabolism Component of Tryptophan metabolism Component of Tyrosine metabolism Component of Ubiquinone biosynthesis
Application
—
Source
Endogenous

Average Molecular Weight

664.433

Monoisotopic Molecular Weight

664.116943

Isomeric SMILES

NC(=O)C1=C[N+](=CC=C1)[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N2C=NC3=C2N=CN=C3N)[C@@H](O)[C@H]1O

Canonical SMILES

NC(=O)C1=C[N+](=CC=C1)C1OC(COP(O)(=O)OP(O)(=O)OCC2OC(C(O)C2O)N2C=NC3=C2N=CN=C3N)C(O)C1O

KEGG Compound ID

BioCyc ID

BiGG ID

Wikipedia Link

NuGOwiki Link

Metagene Link

METLIN ID

PubChem Compound

PubChem Substance

ChEBI ID

CAS Registry Number

53-84-9

InChI Identifier

InChI=1/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/p+1/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

Synthesis Reference

Hughes, N. A.; Kenner, G. W.; Todd, Alexander. Codehydrogenases. III. Synthesis of diphosphopyridine nucleotide (cozymase) and triphosphopyridine nucleotide. Journal of the Chemical Society (1957), 3733-8.

Melting Point (Experimental)

140.0-142.0 oC

Experimental Water Solubility

752.5 mg/mL [HMP experimental] Source: PhysProp

Predicted Water Solubility

1.81 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS

Physiological Charge

-1

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

-1.18 [Predicted by ALOGPS]; -3.68 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

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MOL File

Show

SDF File

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PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

Not Available

Experimental ¹H NMR Spectrum

Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image

Experimental ¹³C NMR Spectrum

Not Available

Experimental ¹³C HSQC Spectrum

Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image

Predicted ¹H NMR Spectrum

Show Image
Show Peaklist

Predicted ¹³C NMR Spectrum

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Show Peaklist

Mass Spectrum

Low Energy
Download File Show Experimental Conditions
Medium Energy
Download File Show Experimental Conditions
High Energy
Download File Show Experimental Conditions

Simplified TOCSY Spectrum

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Show Peaklist

BMRB Spectrum

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Cellular Location

Cytoplasm (Predicted from LogP)
endoplasmic reticulum
Extracellular
mitochondria
nucleus
peroxisome

Biofluid Location

Blood
Cellular Cytoplasm

Tissue Location

Tissue	References
Adrenal Gland	—
Brain	—
Epidermis	—
Fibroblasts	—
Liver	—
Platelet	—
Skeletal Muscle	—

Concentrations (Normal)

Biofluid	Blood
Value	24.00 (23.00-25.6) uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed ]

Biofluid	Cellular Cytoplasm
Value	88.7 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed ]

Concentrations (Abnormal)

Biofluid	Blood
Value	29.00 (25.00-33.00) uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Pellagra
Comments	Not Available
References	Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed ]

Associated Disorders

Condition	References
Pellagra	Creeke PI, Dibari F, Cheung E, van den Briel T, Kyroussis E, Seal AJ: Whole blood NAD and NADP concentrations are not depressed in subjects with clinical pellagra. J Nutr. 2007 Sep;137(9):2013-7. [PubMed ]

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Ammonia Recycling	SMP00009	map00910
Carnitine Synthesis	SMP00465
Citric Acid Cycle	SMP00057	map00020
Ethanol Degradation	SMP00449
Folate Metabolism	SMP00053	map00670
Gluconeogenesis	SMP00128	map00010
Glucose-Alanine Cycle	SMP00127
Glutamate Metabolism	SMP00072	map00250
Glycerol Phosphate Shuttle	SMP00124
Glycerolipid Metabolism	SMP00039	map00561
Glycine and Serine Metabolism	SMP00004	map00260
Glycolysis	SMP00040	map00010
Histidine Metabolism	SMP00044	map00340
Ketone Body Metabolism	SMP00071	map00072
Malate-Aspartate Shuttle	SMP00129
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids	SMP00482
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids	SMP00481
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids	SMP00480
Mitochondrial Electron Transport Chain	SMP00355	map00190
Nicotinate and Nicotinamide Metabolism	SMP00048	map00760
Plasmalogen Synthesis	SMP00479
Threonine and 2-Oxobutanoate Degradation	SMP00452
Transfer of Acetyl Groups into Mitochondria	SMP00466

General References

Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed ]
Ying W: NAD+ and NADH in cellular functions and cell death. Front Biosci. 2006 Sep 1;11:3129-48. [PubMed ]
Hamza A, Cho H, Tai HH, Zhan CG: Understanding human 15-hydroxyprostaglandin dehydrogenase binding with NAD+ and PGE2 by homology modeling, docking and molecular dynamics simulation. Bioorg Med Chem. 2005 Jul 15;13(14):4544-51. [PubMed ]
Begonja AJ, Gambaryan S, Geiger J, Aktas B, Pozgajova M, Nieswandt B, Walter U: Platelet NAD(P)H-oxidase-generated ROS production regulates alphaIIbbeta3-integrin activation independent of the NO/cGMP pathway. Blood. 2005 Oct 15;106(8):2757-60. Epub 2005 Jun 23. [PubMed ]
Bruzzone S, Moreschi I, Guida L, Usai C, Zocchi E, De Flora A: Extracellular NAD+ regulates intracellular calcium levels and induces activation of human granulocytes. Biochem J. 2006 Feb 1;393(Pt 3):697-704. [PubMed ]
Kim MY, Zhang T, Kraus WL: Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 2005 Sep 1;19(17):1951-67. [PubMed ]
Kunsman GW, Manno JE, Cockerham KR, Manno BR: A modification and validation of two urine ethanol procedures for use with the Monarch 2000 Chemistry System. J Anal Toxicol. 1991 May-Jun;15(3):130-5. [PubMed ]
Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed ]
Orczyk J, Morre DM, Morre DJ: Periodic fluctuations in oxygen consumption comparing HeLa (cancer) and CHO (non-cancer) cells and response to external NAD(P)+/NAD(P)H. Mol Cell Biochem. 2005 May;273(1-2):161-7. [PubMed ]
Krotz F, Sohn HY, Gloe T, Zahler S, Riexinger T, Schiele TM, Becker BF, Theisen K, Klauss V, Pohl U: NAD(P)H oxidase-dependent platelet superoxide anion release increases platelet recruitment. Blood. 2002 Aug 1;100(3):917-24. [PubMed ]
Wikipedia

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5275

Enzyme 1 Name

Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor

Enzyme 1 Synonyms

PDHE1-A type I

Enzyme 1 Gene Name

PDHA1

Enzyme 1 Protein Sequence

>Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor

MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS

Enzyme 1 Number of Residues

390

Enzyme 1 Molecular Weight

43296

Enzyme 1 Theoretical pI

8.14

Enzyme 1 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
metabolism physiological process
Component
—

Enzyme 1 General Function

Energy production and conversion

Enzyme 1 Specific Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)

Enzyme 1 Pathways

Butyrate Metabolism (map00650 )
Gluconeogenesis (map00010 )
Pyruvate Metabolism (map00620 )

Enzyme 1 Reactions

pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2

Enzyme 1 Pfam Domain Function

E1_dh (PF00676 )

Enzyme 1 Signals

1-16

Enzyme 1 Transmembrane Regions

Not Available

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

387009

Enzyme 1 UniProtKB/Swiss-Prot ID

P08559

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

ODPA_HUMAN Link Image

Enzyme 1 PDB ID

1NI4

Enzyme 1 PDB File

Show

Enzyme 1 3D Structure

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>1173 bp

ATGAGGAAGATGCTCGCCGCCGTCTCCCGCGTGCTGTCTGGCGCTTCTCAGAAGCCGGCA
AGCAGAGTGCTGGTAGCATCCCGTAATTTTGCAAATGATGCTACATTTGAAATTAAGAAA
TGTGACCTTCACCGGCTGGAAGAAGGCCCTCCTGTCACAACAGTGCTCACCAGGGAGGAT
GGGCTCAAATACTACAGGATGATGCAGACTGTACGCCGAATGGAGTTGAAAGCAGATCAG
CTGTATAAACAGAAAATTATTCGTGGTTTCTGTCACTTGTGTGATGGTCAGGAAGCTTGC
TGTGTGGGCCTGGAGGCCGGCATCAACCCCACAGACCATCTCATCACAGCCTACCGGGCT
CACGGCTTTACTTTCACCCGGGGCCTTTCCGTCCGAGAAATTCTCGCAGAGCTTACAGGA
CGAAAAGGAGGTTGTGCTAAAGGGAAAGGAGGATCGATGCACATGTATGCCAAGAACTTC
TACGGGGGCAATGGCATCGTGGGAGCGCAGGTGCCCCTGGGCGCTGGGATTGCTCTAGCC
TGTAAGTATAATGGAAAAGATGAGGTCTGCCTGACTTTATATGGCGATGGTGCTGCTAAC
CAGGGCCAGATATTCGAAGCTTACAACATGGCAGCTTTGTGGAAATTACCTTGTATTTTC
ATCTGTGAGAATAATCGCTATGGAATGGGAACGTCTGTTGAGAGAGCGGCAGCCAGCACT
GATTACTACAAGAGAGGCGATTTCATTCCTGGGCTGAGAGTGGATGGAATGGATATCCTG
TGCGTCCGAGAGGCAACAAGGTTTGCTGCTGCCTATTGTAGATCTGGGAAGGGGCCCATC
CTGATGGAGCTGCAGACTTACCGTTACCACGGACACAGTATGAGTGACCCTGGAGTCAGT
TACCGTACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGTGACCCTATTATGCTTCTC
AAGGACAGGATGGTGAACAGCAATCTTGCCAGTGTGGAAGAACTAAAGGAAATTGATGTG
GAAGTGAGGAAGGAGATTGAGGATGCTGCCCAGTTTGCCACGGCCGATCCTGAGCCACCT
TTGGAAGAGCTGGGCTACCACATCTACTCCAGCGACCCACCTTTTGAAGTTCGTGGTGCC
AATCAGTGGATCAAGTTTAAGTCAGTCAGTTAA

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

Xp22.2-p22.1

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Koike K, Urata Y, Matsuo S, Koike M: Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit. Gene. 1990 Sep 14;93(2):307-11. [PubMed ]
Ho L, Wexler ID, Liu TC, Thekkumkara TJ, Patel MS: Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5330-4. [PubMed ]
Dahl HH, Hunt SM, Hutchison WM, Brown GK: The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. 1987 May 25;262(15):7398-403. [PubMed ]
Maragos C, Hutchison WM, Hayasaka K, Brown GK, Dahl HH: Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex. J Biol Chem. 1989 Jul 25;264(21):12294-8. [PubMed ]
De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH: Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. 1988 Feb 5;263(4):1991-5. [PubMed ]
Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed ]
Harris EE, Hey J: X chromosome evidence for ancient human histories. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3320-4. [PubMed ]
Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed ]
Dahl HH, Brown GK, Brown RM, Hansen LL, Kerr DS, Wexler ID, Patel MS, De Meirleir L, Lissens W, Chun K, et al.: Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene. Hum Mutat. 1992;1(2):97-102. [PubMed ]
Hansen LL, Brown GK, Kirby DM, Dahl HH: Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis. 1991;14(2):140-51. [PubMed ]
De Meirleir L, Lissens W, Vamos E, Liebaers I: Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit. Hum Genet. 1992 Mar;88(6):649-52. [PubMed ]
Dahl HH, Hansen LL, Brown RM, Danks DM, Rogers JG, Brown GK: X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation. J Inherit Metab Dis. 1992;15(6):835-47. [PubMed ]
Matthews PM, Marchington DR, Squier M, Land J, Brown RM, Brown GK: Molecular genetic characterization of an X-linked form of Leigh's syndrome. Ann Neurol. 1993 Jun;33(6):652-5. [PubMed ]
Chun K, MacKay N, Petrova-Benedict R, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex. Hum Mol Genet. 1993 Apr;2(4):449-54. [PubMed ]
Matthews PM, Brown RM, Otero LJ, Marchington DR, LeGris M, Howes R, Meadows LS, Shevell M, Scriver CR, Brown GK: Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients. Brain. 1994 Jun;117 ( Pt 3):435-43. [PubMed ]
Hansen LL, Horn N, Dahl HH, Kruse TA: Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit. Hum Mol Genet. 1994 Jun;3(6):1021-2. [PubMed ]
Dahl HH, Brown GK: Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit. Hum Mutat. 1994;3(2):152-5. [PubMed ]
Awata H, Endo F, Tanoue A, Kitano A, Matsuda I: Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia. J Inherit Metab Dis. 1994;17(2):189-95. [PubMed ]
Chun K, MacKay N, Petrova-Benedict R, Federico A, Fois A, Cole DE, Robertson E, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex. Am J Hum Genet. 1995 Mar;56(3):558-69. [PubMed ]
Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, Lithgow T, Dahl HH: An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am J Hum Genet. 1995 Oct;57(4):772-80. [PubMed ]
Hemalatha SG, Kerr DS, Wexler ID, Lusk MM, Kaung M, Du Y, Kolli M, Schelper RL, Patel MS: Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit. Hum Mol Genet. 1995 Feb;4(2):315-8. [PubMed ]
Lissens W, De Meirleir L, Seneca S, Benelli C, Marsac C, Poll-The BT, Briones P, Ruitenbeek W, van Diggelen O, Chaigne D, Ramaekers V, Liebaers I: Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency. Hum Mutat. 1996;7(1):46-51. [PubMed ]
Tripatara A, Kerr DS, Lusk MM, Kolli M, Tan J, Patel MS: Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS). Hum Mutat. 1996;8(2):180-2. [PubMed ]
Otero LJ, Brown RM, Brown GK: Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity. Hum Mutat. 1998;12(2):114-21. [PubMed ]
Ito M, Huq AH, Naito E, Saijo T, Takeda E, Kuroda Y: Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein. J Inherit Metab Dis. 1992;15(6):848-56. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5279

Enzyme 2 Name

Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor

Enzyme 2 Synonyms

PDHE1-A type II

Enzyme 2 Gene Name

PDHA2

Enzyme 2 Protein Sequence

>Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor

MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS

Enzyme 2 Number of Residues

388

Enzyme 2 Molecular Weight

42934

Enzyme 2 Theoretical pI

8.56

Enzyme 2 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
metabolism physiological process
Component
—

Enzyme 2 General Function

Energy production and conversion

Enzyme 2 Specific Function

Enzyme 2 Pathways

Butyrate Metabolism (map00650 )
Gluconeogenesis (map00010 )
Pyruvate Metabolism (map00620 )

Enzyme 2 Reactions

pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2

Enzyme 2 Pfam Domain Function

E1_dh (PF00676 )

Enzyme 2 Signals

1-15

Enzyme 2 Transmembrane Regions

Not Available

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

190790

Enzyme 2 UniProtKB/Swiss-Prot ID

P29803

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

ODPAT_HUMAN Link Image

Enzyme 2 PDB ID

Not Available

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>1167 bp

ATGCTGGCCGCCTTCATCTCCCGCGTGTTGAGGCGAGTTGCCCAGAAATCAGCTCGCAGA
GTGCTGGTGGCATCCCGTAACTCCTCAAATGACGCTACATTTGAAATTAAGAAATGTGAT
CTTTATCTGTTGGAAGAGGGTCCCCCTGTCACTACAGTGCTCACTAGGGCGGAGGGGCTT
AAATACTACAGGATGATGCTGACTGTTCGCCGCATGGAATTGAAGGCAGATCAGCTGTAC
AAACAGAAATTCATTCGCGGTTTCTGTCACCTGTGCGATGGTCAGGAAGCTTGTTGCGTG
GGCCTTGAGGCCGGCATAAACCCCTCGGATCACGTCATTACATCCTATAGGGCTCATGGT
GTGTGCTATACTCGGGGACTTTCTGTCCGATCCATTCTCGCAGAGCTGACGGGAAGAAGA
GGAGGTTGTGCTAAAGGAAAAGGAGGATCGATGCATATGTATACCAAGAACTTCTATGGG
GGCAATGGCATCGTCGGTGCACAGGGCCCCCTGGGCGCTGGCATTGCTCTGGCCTGTAAA
TATAAAGGAAACGATGAGATCTGTTTGACTTTATATGGGGATGGCGCTGCGAATCAGGGG
CAGATAGCCGAAGCTTTCAATATGGCAGCTTTATGGAAATTACCTTGTGTTTTCATCTGT
GAGAATAACCTATATGGAATGGGAACATCTACTGAGAGAGCAGCAGCCAGCCCTGATTAC
TACAAGAGGGGCAATTTTATCCCTGGGCTAAAGGTCGATGGAATGGATGTTCTGTGTGTT
CGTGAGGCAACAAAATTTGCAGCTAACTACTGTAGATCTGGAAAGGGGCCCATACTGATG
GAGCTGCAAACCTACCGTTATCATGGACACAGTATGAGTGATCCTGGAGTCAGTTATCGT
ACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGGGATCCTATAATAATTCTCCAAGAT
AGAATGGTAAACAGCAAGCTCGCCACTGTGGAAGAATTAAAGGAAATTGGGGCTGAGGTG
AGGAAAGAAATTGATGATGCTGCCCAGTTTGCTACCACTGATCCTGAGCCACATTTGGAA
GAATTAGGCCATCACATCTACAGCAGTGATTCATCTTTTGAAGTTCGTGGTGCAAATCCA
TGGATCAAGTTTAAGTCCGTCAGTTAA

Enzyme 2 GenBank Gene ID

Enzyme 2 GeneCard ID

Enzyme 2 GenAtlas ID

Enzyme 2 HGNC ID

Enzyme 2 Chromosome Location

Enzyme 2 Locus

4q22-q23

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK: A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4. Genomics. 1990 Oct;8(2):225-32. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5280

Enzyme 3 Name

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial precursor

Enzyme 3 Synonyms

MMSDH
Malonate-semialdehyde dehydrogenase [acylating]

Enzyme 3 Gene Name

ALDH6A1

Enzyme 3 Protein Sequence

>Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial precursor

MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIH
NPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIA
KLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCA
GIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHG
QHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKEN
TLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLIT
PQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFG
PVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLP
MFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR

Enzyme 3 Number of Residues

535

Enzyme 3 Molecular Weight

57840

Enzyme 3 Theoretical pI

8.69

Enzyme 3 GO Classification

Function
catalytic activity methylmalonate-semialdehyde dehydrogenase (acylating) activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
amino acid and derivative metabolism amino acid metabolism branched chain family amino acid metabolism cellular metabolism metabolism physiological process valine metabolism
Component
—

Enzyme 3 General Function

Energy production and conversion

Enzyme 3 Specific Function

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA

Enzyme 3 Pathways

Propanoate Metabolism (map00640 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 3 Reactions

2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + CO2 + NADH

Enzyme 3 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 3 Signals

1-19

Enzyme 3 Transmembrane Regions

174-196

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

7160985

Enzyme 3 UniProtKB/Swiss-Prot ID

Q02252

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

MMSA_HUMAN Link Image

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>1608 bp

ATGGCGGCGCTATTGGCGGCGGCGGCAGTGCGAGCCCGGATCCTGCAGGTTTCTTCCAAG
GTGAAATCCAGTCCCACCTGGTATTCAGCATCTTCCTTCTCTTCTTCAGTGCCAACTGTA
AAGCTCTTCATTGGTGGGAAATTCGTTGAATCCAAAAGTGACAAATGGATCGATATCCAC
AACCCAGCCACCAATGAGGTCATTGGTCGGGTCCCTCAGGCCACCAAGGCAGAAATGGAT
GCAGCCATTGCTTCCTGCAAACGTGCTTTTCCTGCATGGGCAGACACTTCAGTATTAAGC
CGCCAGCAGGTCTTGCTCCGCTATCAACAACTTATTAAAGAAAACTTGAAAGAAATTGCC
AAGTTAATCACATTGGAACAAGGGAAGACCCTAGCTGATGCTGAAGGAGATGTATTTCGA
GGCCTTCAGGTGGTTGAGCATGCCTGTAGTGTGACATCCCTCATGATGGGAGAGACCATG
CCATCCATCACCAAAGACATGGACCTTTATTCCTACCGTCTGCCTCTGGGAGTGTGTGCA
GGCATTGCTCCATTCAATTTTCCTGCCATGATCCCCCTTTGGATGTTTCCCATGGCCATG
GTGTGTGGAAATACCTTCCTAATGAAACCATCTGAGCGAGTCCCTGGAGCAACTATGCTT
CTTGCTAAGTTGCTCCAGGATTCTGGTGCCCCTGATGGAACATTAAACATCATCCATGGA
CAGCATGAAGCTGTAAATTTTATTTGCGATCATCCGGACATCAAAGCAATCAGCTTTGTG
GGATCCAACAAGGCAGGAGAGTATATCTTCGAGAGAGGATCAAGACATGGCAAGAGGGTT
CAAGCCAATATGGGAGCCAAGAACCATGGGGTAGTCATGCCAGATGCCAATAAGGAAAAT
ACCCTGAACCAGCTGGTTGGGGCAGCATTTGGAGCTGCTGGTCAGCGCTGCATGGCTCTT
TCAACAGCAGTCCTTGTGGGAGAAGCCAAGAAGTGGCTGCCAGAGCTGGTGGAGCATGCC
AAAAACCTGAGAGTCAATGCAGGAGATCAGCCTGGAGCTGATCTTGGCCCTCTGATCACT
CCCCAGGCCAAAGAGCGAGTCTGTAATCTGATTGATAGTGGAACAAAGGAGGGAGCTTCC
ATCCTTCTTGATGGACGAAAAATTAAAGTGAAAGGCTATGAAAATGGCAACTTTGTTGGA
CCAACCATCATCTCGAATGTCAAGCCAAATATGACCTGTTACAAAGAGGAGATTTTTGGT
CCAGTTCTTGTGGTTCTGGAGACAGAAACATTGGATGAAGCCATCCAGATTGTAAATAAC
AACCCATATGGAAATGGAACTGCCATCTTCACCACCAATGGAGCCACTGCTCGGAAATAT
GCCCACTTGGTGGATGTTGGACAGGTGGGAGTGAATGTCCCCATTCCAGTGCCTTTGCCA
ATGTTCTCATTCACCGGCTCTCGATCCTCCTTCAGGGGAGACACCAATTTCTATGGCAAA
CAGGGCATCCAATTCTACACTCAGTTAAAGACCATTACTTCTCAGTGGAAAGAAGAAGAT
GCTACTCTTTCCTCACCTGCTGTTGTCATGCCTACCATGGGCCGTTAG

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

14q24.3

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Chambliss KL, Gray RG, Rylance G, Pollitt RJ, Gibson KM: Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency. J Inherit Metab Dis. 2000 Jul;23(5):497-504. [PubMed ]
Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA: CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J Biol Chem. 1992 Sep 25;267(27):19724-9. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5283

Enzyme 4 Name

Dihydrolipoyl dehydrogenase, mitochondrial precursor

Enzyme 4 Synonyms

Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein

Enzyme 4 Gene Name

DLD

Enzyme 4 Protein Sequence

>Dihydrolipoyl dehydrogenase, mitochondrial precursor

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGTDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF

Enzyme 4 Number of Residues

509

Enzyme 4 Molecular Weight

54151

Enzyme 4 Theoretical pI

7.76

Enzyme 4 GO Classification

Function
FAD binding adenyl nucleotide binding binding catalytic activity dihydrolipoyl dehydrogenase activity disulfide oxidoreductase activity electron transporter activity nucleotide binding oxidoreductase activity purine nucleotide binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
cell cytoplasm intracellular

Enzyme 4 General Function

Energy production and conversion

Enzyme 4 Specific Function

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes

Enzyme 4 Pathways

Citrate Cycle (map00020 )
Gluconeogenesis (map00010 )
Glycine, Serine and Threonine Metabolism (map00260 )
Pyruvate Metabolism (map00620 )

Enzyme 4 Reactions

protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+

Enzyme 4 Pfam Domain Function

Pyr_redox (PF00070 )
Pyr_redox_2 (PF07992 )
Pyr_redox_dim (PF02852 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

307137

Enzyme 4 UniProtKB/Swiss-Prot ID

P09622

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

DLDH_HUMAN Link Image

Enzyme 4 PDB ID

Not Available

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>1530 bp

ATGCAGAGCTGGAGTCGTGTGTACTGCTCCTTGGCCAAGAGAGGCCATTTCAATCGAATA
TCTCATGGCCTACAGGGACTTTCTGCAGTGCCTCTGAGAACTTACGCAGATCAGCCGATT
GATGCTGATGTAACAGTTATAGGTTCTGGTCCTGGAGGATATGTTGCTGCTATTAAAGCT
GCCCAGTTAGGCTTCAAGACAGTCTGCATTGAGAAAAATGAAACACTTGGTGGAACATGC
TTGAATGTTGGTTGTATTCCTTCTAAGGCTTTATTGAACAACTCTCATTATTACCATATG
GCCCATGGAACAGATTTTGCATCTAGAGGAATTGAAATGTCCGAAGTTCGCTTGAATTTA
GACAAGATGATGGAGCAGAAGAGTACTGCAGTAAAAGCTTTAACAGGTGGAATTGCCCAC
TTATTCAAACAGAATAAGGTTGTTCATGTCAATGGATATGGAAAGATAACTGGCAAAAAT
CAAGTCACTGCTACGAAAGCTGATGGCGGCACTCAGGTTATTGATACAAAGAACATTCTT
ATAGCCACGGGTTCAGAAGTTACTCCTTTTCCTGGAATCACGATAGATGAAGATACAATA
GTGTCATCTACAGGTGCTTTATCTTTAAAAAAAGTTCCAGAAAAGATGGTTGTTATTGGT
GCAGGAGTAATAGGTGTAGAATTGGGTTCAGTTTGGCAAAGACTTGGTGCAGATGTGACA
GCAGTTGAATTTTTAGGTCATGTAGGTGGAGTTGGAATTGATATGGAGATATCTAAAAAC
TTTCAACGCATCCTTCAAAAACAGGGGTTTAAATTTAAATTGAATACAAAGGTTACTGGT
GCTACCAAGAAGTCAGATGGAAAAATTGATGTTTCTATTGAAGCTGCTTCTGGTGGTAAA
GCTGAAGTTATCACTTGTGATGTACTCTTGGTTTGCATTGGCCGACGACCCTTTACTAAG
AATTTGGGACTAGAAGAGCTGGGAATTGAACTAGATCCTAGAGGTAGAATTCCAGTCAAT
ACCAGATTTCAAACTAAAATTCCAAATATCTATGCCATTGGTGATGTAGTTGCTGGTCCA
ATGCTGGCTCACAAAGCAGAGGATGAAGGCATTATCTGTGTTGAAGGAATGGCTGGTGGT
GCTGTGCACATTGACTACAATTGTGTGCCATCAGTGATTTACACACACCCTGAAGTTGCT
TGGGTTGGCAAATCAGAAGAGCAGTTGAAAGAAGAGGGTATTGAGTACAAAGTTGGGAAA
TTCCCATTTGCTGCTAACAGCAGAGCTAAGACAAATGCTGACACAGATGGCATGGTGAAG
ATCCTTGGGCAGAAATCGACAGACAGAGTACTGGGAGCACATATTCTTGGACCAGGTGCT
GGAGAAATGGTAAATGAAGCTGCTCTTGCTTTGGAATATGGAGCATCCTGTGAAGATATA
GCTAGAGTCTGTCATGCACATCCGACCTTATCAGAAGCTTTTAGAGAAGCAAATCTTGCT
GCGTCATTTGGCAAATCAATCAACTTTTGA

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

7q31-q32

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8. [PubMed ]
Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. [PubMed ]
Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. [PubMed ]
Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
Johanning GL, Morris JI, Madhusudhan KT, Samols D, Patel MS: Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10964-8. [PubMed ]
Liu TC, Kim H, Arizmendi C, Kitano A, Patel MS: Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5186-90. [PubMed ]
Hong YS, Kerr DS, Craigen WJ, Tan J, Pan Y, Lusk M, Patel MS: Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency. Hum Mol Genet. 1996 Dec;5(12):1925-30. [PubMed ]
Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON: Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5284

Enzyme 5 Name

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor

Enzyme 5 Synonyms

Pyruvate dehydrogenase complex E2 subunit
PDCE2
E2
Dihydrolipoamide S- acetyltransferase component of pyruvate dehydrogenase complex
PDC- E2
70 kDa mitochondrial autoantigen of primary biliary cirrhosis
PBC
M2 antigen complex 70 kDa subunit

Enzyme 5 Gene Name

DLAT

Enzyme 5 Protein Sequence

>Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor

MSPHCSTTYLRTLGRTTMFWKTTEGRDGKMAVQEFSEFGLLLQLLGSPGRRYYSLPPHQK
VPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEG
TRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGS
SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLA
KILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTP
QPLAPTPSTPCPATPAGPKGRVFVDPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFV
PSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVN
MGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSV
AVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGI
KNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLA
EFRKYLEKPITMLL

Enzyme 5 Number of Residues

614

Enzyme 5 Molecular Weight

65782

Enzyme 5 Theoretical pI

5.95

Enzyme 5 GO Classification

Function
S-acetyltransferase activity acetyltransferase activity acyltransferase activity binding catalytic activity dihydrolipoyllysine-residue acetyltransferase activity protein binding transferase activity transferase activity, transferring acyl groups transferase activity, transferring groups other than amino-acyl groups
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
protein complex pyruvate dehydrogenase complex

Enzyme 5 General Function

Energy production and conversion

Enzyme 5 Specific Function

Enzyme 5 Pathways

Gluconeogenesis (map00010 )
Pyruvate Metabolism (map00620 )

Enzyme 5 Reactions

acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine

Enzyme 5 Pfam Domain Function

2-oxoacid_dh (PF00198 )
Biotin_lipoyl (PF00364 )
E3_binding (PF02817 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

35360

Enzyme 5 UniProtKB/Swiss-Prot ID

P10515

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

ODP2_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>1848 bp

CGAGTGACCTCGCGATCTGGCCCGGCTCCCGCTCGTCGCAACAGCGTGACTACAGGGTAT
GGCGGGGTCCGGGCACTGTGCGGCTGGACCCCCAGTTCTGGGGCCACGCCGCGGAACCGC
TTACTGCTGCAGCTTTTGGGGTCGCCCGGCCGCCGCTATTACAGTCTTCCCCCGCATCAG
AAGGTTCCATTGCCTTCTCTTTCCCCCACAATGCAGGCAGGCACCATAGCCCGTTGGAAA
AAAAAAGAGGGGGACAAAATCAATGAAGGTGACCTAATTGCAGAGGTTGAAACTGATAAA
GCCACTGTTGGATTTGAGAGCCTGGAGGAGTGTTATATGGCAAAGATACTTGTTGCTGAA
GGTACCAGGGATGTTCCCATCGGAGCGATCATCTGTATCACAGTTGGCAAGCCTGAGGAT
ATTGAGGCCTTTAAAAATTATACACTGGATTCCTCAGCAGCACCTACCCCACAAGCGGCC
CCAGCACCAACCCCTGCTGCCACTGCTTCGCCACCTACACCTTCTGCTCAGGCTCCTGGT
AGCTCATATCCCCCTCACATGCAGGTACTTCTTCCTGCCCTCTCTCCCACCATGACCATG
GGCACAGTTCAGAGATGGGAAAAAAAAGTGGGTGAGAAGCTAAGTGAAGGAGACTTACTG
GCAGAGATAGAAACTGACAAAGCCACTATAGGTTTTGAAGTACAGGAAGAAGGTTATCTG
GCAAAAATCCTGGTCCCTGAAGGCACAAGAGATGTCCCTCTAGGAACCCCACTCTGTATC
ATTGTAGAAAAAGAGGCAGATATATCAGCATTTGCTGACTATAGGCCAACCGAAGTAACA
GATTTAAAACCACAAGTGCCACCACCTACCCCACCCCCGGTGGCCGCTGTTCCTCCAACT
CCCCAGCCTTTAGCTCCTACACCTTCAGCACCCTGCCCAGCTACTCCTGCTGGACCAAAG
GGAAGGGTGTTTGTTAGCCCTCTTGCAAAGAAGTTGGCAGTAGAGAAAGGGATTGATCTT
ACACAAGTAAAAGGGACAGGACCAGATGGTAGAATCACCAAGAAGGATATCGACTCTTTT
GTGCCTAGTAAAGTTGCTCCTGCTCCGGCAGCTGTTGTGCCTCCCACAGGTCCTGGAATG
GCACCAGTTCCTACAGGTGTCTTCACAGATATCCCAATCAGCAACATTCGTCGGGTTATT
GCACAGCGATTAATGCAATCAAAGCAAACCATACCTCATTATTACCTTTCTATCGATGTA
AATATGGGAGAAGTTTTGTTGGTACGGAAAGAACTTAATAAGATATTAGAAGGGAGAAGC
AAAATTTCTGTCAATGACTTCATCATAAAAGCTTCAGCTTTGGCATGTTTAAAAGTTCCC
GAAGCAAATTCTTCTTGGATGGACACAGTTATAAGACAAAATCATGTTGTTGATGTCAGT
GTTGCGGTCAGTACTCCTGCAGGACTCATCACACCTATTGTGTTTAATGCACATATAAAA
GGAGTGGAAACCATTGCTAATGATGTTGTTTCTTTAGCAACCAAAGCAAGAGAGGGTAAA
CTACAGCCACATGAATTCCAGGGTGGCACTTTTACGATCTCCAATTTAGGAATGTTTGGA
ATTAAGAATTTCTCTGCTATTATTAACCCACCTCAAGCATGTATTTTGGCAATTGGTGCT
TCAGAGGATAAACTGGTCCCTGCAGATAATGAAAAAGGGTTTGATGTGGCTAGCATGATG
TCTGTTACACTCAGTTGTGATCACCGGGTGGTGGATGGAGCAGTTGGAGCCCAGTGGCTT
GCTGAGTTTAGAAAGTACCTTGAAAAACCTATCACTATGTTGTTGTAA

Enzyme 5 GenBank Gene ID

Enzyme 5 GeneCard ID

Enzyme 5 GenAtlas ID

Enzyme 5 HGNC ID

Enzyme 5 Chromosome Location

Enzyme 5 Locus

11q23.1

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Coppel RL, McNeilage LJ, Surh CD, Van de Water J, Spithill TW, Whittingham S, Gershwin ME: Primary structure of the human M2 mitochondrial autoantigen of primary biliary cirrhosis: dihydrolipoamide acetyltransferase. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7317-21. [PubMed ]
Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS: Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 1988 Nov 21;240(1-2):45-8. [PubMed ]
Howard MJ, Fuller C, Broadhurst RW, Perham RN, Tang JG, Quinn J, Diamond AG, Yeaman SJ: Three-dimensional structure of the major autoantigen in primary biliary cirrhosis. Gastroenterology. 1998 Jul;115(1):139-46. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5303

Enzyme 6 Name

Aldo-keto reductase family 1 member C4

Enzyme 6 Synonyms

Chlordecone reductase
CDR
3-alpha-hydroxysteroid dehydrogenase type I
3-alpha-HSD1
Dihydrodiol dehydrogenase 4
DD4
HAKRA

Enzyme 6 Gene Name

AKR1C4

Enzyme 6 Protein Sequence

>Aldo-keto reductase family 1 member C4

MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPM
ALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKP
GLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN
RNYRYVVMDFLMDHPDYPFSDEY

Enzyme 6 Number of Residues

323

Enzyme 6 Molecular Weight

37095

Enzyme 6 Theoretical pI

7.19

Enzyme 6 GO Classification

Function
catalytic activity oxidoreductase activity
Process
—
Component
—

Enzyme 6 General Function

Not Available

Enzyme 6 Specific Function

Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3alpha,17beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route

Enzyme 6 Pathways

Androgen and Estrogen Metabolism (map00150 )
Bile Acid Biosynthesis (map00120 )
C21 Steroid Hormone Metabolism (map00140 )

Enzyme 6 Reactions

chlordecone alcohol + NADP+ = chlordecone + NADPH + H+

Enzyme 6 Pfam Domain Function

Aldo_ket_red (PF00248 )

Enzyme 6 Signals

None

Enzyme 6 Transmembrane Regions

None

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

4261710

Enzyme 6 UniProtKB/Swiss-Prot ID

P17516

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

AK1C4_HUMAN Link Image

Enzyme 6 PDB ID

Not Available

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>972 bp

ATGGATCCCAAATATCAGCGTGTAGAGCTAAATGATGGTCATTTCATGCCCGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGGAACAGAGCTGTAGAGGTCACCAAATTA
GCAATAGAAGCTGGCTTCCGCCATATTGATTCTGCTTATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCACTTTCTTTCAACCACAGATGGTCCAACCAGCCTTGGAA
AGCTCACTGAAAAAACTTCAACTGGACTATGTTGACCTCTATCTTCTTCATTTCCCAATG
GCTCTCAAGCCAGGTGAGACGCCACTACCAAAAGATGAAAATGGAAAAGTAATATTCGAC
ACAGTGGATCTCTCTGCCACATGGGAGGTCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCAAACTTCAACTGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCTTACCTCAACCAGAGC
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCCACAGTGCTCTGGGA
ACCCAACGACATAAACTATGGGTGGACCCAAACTCCCCAGTTCTTTTGGAGGACCCAGTT
CTTTGTGCCTTAGCAAAGAAACACAAACGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGGATCAGAGAGAAC
ATCCAGGTTTTTGAATTCCAGTTGACATCAGAGGATATGAAAGTTCTAGATGGTCTAAAC
AGAAATTATCGATATGTTGTCATGGATTTTCTTATGGACCATCCTGATTATCCATTTTCA
GATGAATATTAG

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

10p15-p14

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed ]
Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed ]
Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed ]
Kume T, Iwasa H, Shiraishi H, Yokoi T, Nagashima K, Otsuka M, Terada T, Takagi T, Hara A, Kamataki T: Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver. Pharmacogenetics. 1999 Dec;9(6):763-71. [PubMed ]
Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed ]
Dufort I, Labrie F, Luu-The V: Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J Clin Endocrinol Metab. 2001 Feb;86(2):841-6. [PubMed ]
Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990 Jan 30;29(4):1080-7. [PubMed ]
Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed ]
Binstock JM, Iyer RB, Hamby CV, Fried VA, Schwartz IS, Weinstein BI, Southren AL: Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase. Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5307

Enzyme 7 Name

15-hydroxyprostaglandin dehydrogenase [NAD+]

Enzyme 7 Synonyms

PGDH
Prostaglandin dehydrogenase 1

Enzyme 7 Gene Name

HPGD

Enzyme 7 Protein Sequence

>15-hydroxyprostaglandin dehydrogenase [NAD+]

MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLF
IQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLD
YMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNA
ICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNG
AIMKITTSKGIHFQDYDTTPFQAKTQ

Enzyme 7 Number of Residues

266

Enzyme 7 Molecular Weight

28978

Enzyme 7 Theoretical pI

5.65

Enzyme 7 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 7 General Function

Lipid transport and metabolism

Enzyme 7 Specific Function

Inactivation of prostaglandins

Enzyme 7 Pathways

Not Available

Enzyme 7 Reactions

(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD+ = (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH + H+

Enzyme 7 Pfam Domain Function

adh_short (PF00106 )

Enzyme 7 Signals

None

Enzyme 7 Transmembrane Regions

None

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

1203984

Enzyme 7 UniProtKB/Swiss-Prot ID

P15428

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

PGDH_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>801 bp

ATGCACGTGAACGGCAAAGTGGCGCTGGTGACCGGCGCGGCTCAGGGCATAGGCAGAGCC
TTTGCAGAGGCGCTGCTGCTTAAGGGCGCCAAGGTAGCGCTGGTGGATTGGAATCTTGAA
GCAGGTGTACAGTGTAAAGCTGCCCTGCATGAGCAATTTGAACCTCAGAAGACTCTGTTC
ATCCAGTGCGATGTGGCTGACCAGCAACAACTGAGAGACACTTTTAGAAAAGTTGTAGAC
CACTTTGGAAGACTGGACATTTTGGTCAATAATGCTGGAGTGAATAATGAGAAAAACTGG
GAAAAAACTCTGCAAATTAATTTGGTTTCTGTTATCAGTGGAACCTATCTTGGTTTGGAT
TACATGAGTAAGCAAAATGGAGGTGAAGGCGGCATCATTATCAATATGTCATCTTTAGCA
GGACTCATGCCCGTTGCACAGCAGCCGGTTTATTGTGCTTCAAAGCATGGCATAGTTGGA
TTCACACGCTCAGCAGCGTTGGCTGCTAATCTTATGAACAGTGGTGTGAGACTGAATGCC
ATTTGTCCAGGCTTTGTTAACACAGCCATCCTTGAATCAATTGAAAAAGAAGAAAACATG
GGACAATATATAGAATATAAGGATCATATCAAGGATATGATTAAATACTATGGAATTTTG
GACCCACCATTGATTGCCAATGGATTGATAACACTCATTGAAGATGATGCTTTAAATGGT
GCTATTATGAAGATCACAACTTCTAAGGGAATTCATTTTCAAGACTATGATACAACTCCA
TTTCAAGCAAAAACCCAATGA

Enzyme 7 GenBank Gene ID

Enzyme 7 GeneCard ID

Enzyme 7 GenAtlas ID

Enzyme 7 HGNC ID

Enzyme 7 Chromosome Location

Enzyme 7 Locus

4q34-q35

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Krook M, Marekov L, Jornvall H: Purification and structural characterization of placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry. 1990 Jan 23;29(3):738-43. [PubMed ]
Ensor CM, Yang JY, Okita RT, Tai HH: Cloning and sequence analysis of the cDNA for human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase. J Biol Chem. 1990 Sep 5;265(25):14888-91. [PubMed ]
Ensor CM, Tai HH: Site-directed mutagenesis of the conserved tyrosine 151 of human placental NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem Biophys Res Commun. 1991 Apr 30;176(2):840-5. [PubMed ]
Krook M, Ghosh D, Duax W, Jornvall H: Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase). FEBS Lett. 1993 May 10;322(2):139-42. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

5319

Enzyme 8 Name

Tyrosinase precursor

Enzyme 8 Synonyms

Monophenol monooxygenase
Tumor rejection antigen AB
SK29-AB
LB24-AB

Enzyme 8 Gene Name

TYR

Enzyme 8 Protein Sequence

>Tyrosinase precursor

MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILL
SNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVR
RNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMH
YYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRD
AEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRN
PGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQS
SMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGH
NRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLG
AAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL

Enzyme 8 Number of Residues

529

Enzyme 8 Molecular Weight

60394

Enzyme 8 Theoretical pI

6.05

Enzyme 8 GO Classification

Function
catalytic activity oxidoreductase activity
Process
metabolism physiological process
Component
—

Enzyme 8 General Function

Not Available

Enzyme 8 Specific Function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone

Enzyme 8 Pathways

Riboflavin Metabolism (map00740 )
Stilbene, coumarine and lignin biosynthesis (map00940 )
Tyrosine Metabolism (map00350 )

Enzyme 8 Reactions

L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O

Enzyme 8 Pfam Domain Function

Tyrosinase (PF00264 )

Enzyme 8 Signals

1-18

Enzyme 8 Transmembrane Regions

477-497

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

340037

Enzyme 8 UniProtKB/Swiss-Prot ID

P14679

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

TYRO_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>1590 bp

ATGCTCCTGGCTGTTTTGTACTGCCTGCTGTGGAGTTTCCAGACCTCCGCTGGCCATTTC
CCTAGAGCCTGTGTCTCCTCTAAGAACCTGATGGAGAAGGAATGCTGTCCACCGTGGAGC
GGGGACAGGAGTCCCTGTGGCCAGCTTTCAGGCAGAGGTTCCTGTCAGAATATCCTTCTG
TCCAATGCACCACTTGGGCCTCAATTTCCCTTCACAGGGGTGGATGACCGGGAGTCGTGG
CCTTCCGTCTTTTATAATAGGACCTGCCAGTGCTCTGGCAACTTCATGGGATTCAACTGT
GGAAACTGCAAGTTTGGCTTTTGGGGACCAAACTGCACAGAGAGACGACTCTTGGTGAGA
AGAAACATCTTCGATTTGAGTGCCCCAGAGAAGGACAAATTTTTTGCCTACCTCACTTTA
GCAAAGCATACCATCAGCTCAGACTATGTCATCCCCATAGGGACCTATGGCCAAATGAAA
AATGGATCAACACCCATGTTTAACGACATCAATATTTATGACCTCTTTGTCTGGATGCAT
TATTATGTGTCAATGGATGCACTGCTTGGGGGATCTGAAATCTGGAGAGACATTGATTTT
GCCCATGAAGCACCAGCTTTTCTGCCTTGGCATAGACTCTTCTTGTTGCGGTGGGAACAA
GAAATCCAGAAGCTGACAGGAGATGAAAACTTCACTATTCCATATTGGGACTGGCGGGAT
GCAGAAAAGTGTGACATTTGCACAGATGAGTACATGGGAGGTCAGCACCCCACAAATCCT
AACTTACTCAGCCCAGCATCATTCTTCTCCTCTTGGCAGATTGTCTGTAGCCGATTGGAG
GAGTACAACAGCCATCAGTCTTTATGCAATGGAACGCCCGAGGGACCTTTACGGCGTAAT
CCTGGAAACCATGACAAATCCAGAACCCCAAGGCTCCCCTCTTCAGCTGATGTAGAATTT
TGCCTGAGTTTGACCCAATATGAATCTGGTTCCATGGATAAAGCTGCCAATTTCAGCTTT
AGAAATACACTGGAAGGATTTGCTAGTCCACTTACTGGGATAGCGGATGCCTCTCAAAGC
AGCATGCACAATGCCTTGCACATCTATATGAATGGAACAATGTCCCAGGTACAGGGATCT
GCCAACGATCCTATCTTCCTTCTTCACCATGCATTTGTTGACAGTATTTTTGAGCAGTGG
CTCCGAAGGCACCGTCCTCTTCAAGAAGTTTATCCAGAAGCCAATGCACCCATTGGACAT
AACCGGGAATCCTACATGGTTCCTTTTATACCACTGTACAGAAATGGTGATTTCTTTATT
TCATCCAAAGATCTGGGCTATGACTATAGCTATCTACAAGATTCAGACCCAGACTCTTTT
CAAGACTACATTAAGTCCTATTTGGAACAAGCGAGTCGGATCTGGTCATGGCTCCTTGGG
GCGGCGATGGTAGGGGCCGTCCTCACTGCCCTGCTGGCAGGGCTTGTGAGCTTGCTGTGT
CGTCACAAGAGAAAGCAGCTTCCTGAAGAAAAGCAGCCACTCCTCATGGAGAAAGAGGAT
TACCACAGCTTGTATCAGAGCCATTTATAA

Enzyme 8 GenBank Gene ID

M27160

Enzyme 8 GeneCard ID

TYR

Enzyme 8 GenAtlas ID

TYR

Enzyme 8 HGNC ID

HGNC:12442 Link Image

Enzyme 8 Chromosome Location

Enzyme 8 Locus

11q14-q21

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Giebel LB, Strunk KM, Spritz RA: Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. Genomics. 1991 Mar;9(3):435-45. [PubMed ]
Kwon BS, Haq AK, Pomerantz SH, Halaban R: Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7473-7. [PubMed ]
Bouchard B, Fuller BB, Vijayasaradhi S, Houghton AN: Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA. J Exp Med. 1989 Jun 1;169(6):2029-42. [PubMed ]
Chintamaneni CD, Halaban R, Kobayashi Y, Witkop CJ Jr, Kwon BS: A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5272-6. [PubMed ]
Brichard V, Van Pel A, Wolfel T, Wolfel C, De Plaen E, Lethe B, Coulie P, Boon T: The tyrosinase gene codes for an antigen recognized by autologous cytolytic T lymphocytes on HLA-A2 melanomas. J Exp Med. 1993 Aug 1;178(2):489-95. [PubMed ]
Martinez-Arias R, Comas D, Andres A, Abello MT, Domingo-Roura X, Bertranpetit J: The tyrosinase gene in gorillas and the albinism of 'Snowflake'. Pigment Cell Res. 2000 Dec;13(6):467-70. [PubMed ]
Kikuchi H, Miura H, Yamamoto H, Takeuchi T, Dei T, Watanabe M: Characteristic sequences in the upstream region of the human tyrosinase gene. Biochim Biophys Acta. 1989 Dec 22;1009(3):283-6. [PubMed ]
Takeda A, Tomita Y, Okinaga S, Tagami H, Shibahara S: Functional analysis of the cDNA encoding human tyrosinase precursor. Biochem Biophys Res Commun. 1989 Aug 15;162(3):984-90. [PubMed ]
Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed ]
Oetting WS, King RA: Molecular basis of type I (tyrosinase-related) oculocutaneous albinism: mutations and polymorphisms of the human tyrosinase gene. Hum Mutat. 1993;2(1):1-6. [PubMed ]
Oetting WS, King RA: Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. Hum Mutat. 1999;13(2):99-115. [PubMed ]
Spritz RA, Strunk KM, Giebel LB, King RA: Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism. N Engl J Med. 1990 Jun 14;322(24):1724-8. [PubMed ]
Giebel LB, Strunk KM, King RA, Hanifin JM, Spritz RA: A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism. Proc Natl Acad Sci U S A. 1990 May;87(9):3255-8. [PubMed ]
Giebel LB, Tripathi RK, Strunk KM, Hanifin JM, Jackson CE, King RA, Spritz RA: Tyrosinase gene mutations associated with type IB ("yellow") oculocutaneous albinism. Am J Hum Genet. 1991 Jun;48(6):1159-67. [PubMed ]
Tripathi RK, Strunk KM, Giebel LB, Weleber RG, Spritz RA: Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions. Am J Med Genet. 1992 Jul 15;43(5):865-71. [PubMed ]
Spritz RA, Strunk KM, Hsieh CL, Sekhon GS, Francke U: Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. Am J Hum Genet. 1991 Feb;48(2):318-24. [PubMed ]
Giebel LB, Tripathi RK, King RA, Spritz RA: A tyrosinase gene missense mutation in temperature-sensitive type I oculocutaneous albinism. A human homologue to the Siamese cat and the Himalayan mouse. J Clin Invest. 1991 Mar;87(3):1119-22. [PubMed ]
King RA, Mentink MM, Oetting WS: Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism. Mol Biol Med. 1991 Feb;8(1):19-29. [PubMed ]
Oetting WS, King RA: Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism. Hum Genet. 1992 Nov;90(3):258-62. [PubMed ]
Tripathi RK, Bundey S, Musarella MA, Droetto S, Strunk KM, Holmes SA, Spritz RA: Mutations of the tyrosinase gene in Indo-Pakistani patients with type I (tyrosinase-deficient) oculocutaneous albinism (OCA). Am J Hum Genet. 1993 Dec;53(6):1173-9. [PubMed ]
Gershoni-Baruch R, Rosenmann A, Droetto S, Holmes S, Tripathi RK, Spritz RA: Mutations of the tyrosinase gene in patients with oculocutaneous albinism from various ethnic groups in Israel. Am J Hum Genet. 1994 Apr;54(4):586-94. [PubMed ]
Breimer LH, Winder AF, Jay B, Jay M: Initiation codon mutation of the tyrosinase gene as a cause of human albinism. Clin Chim Acta. 1994 Jun;227(1-2):17-22. [PubMed ]
Summers CG, Oetting WS, King RA: Diagnosis of oculocutaneous albinism with molecular analysis. Am J Ophthalmol. 1996 Jun;121(6):724-6. [PubMed ]
Morell R, Spritz RA, Ho L, Pierpont J, Guo W, Friedman TB, Asher JH Jr: Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and autosomal recessive ocular albinism (AROA). Hum Mol Genet. 1997 May;6(5):659-64. [PubMed ]
Spritz RA, Oh J, Fukai K, Holmes SA, Ho L, Chitayat D, France TD, Musarella MA, Orlow SJ, Schnur RE, Weleber RG, Levin AV: Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous albinism (OCA1). Hum Mutat. 1997;10(2):171-4. [PubMed ]
Passmore LA, Kaesmann-Kellner B, Weber BH: Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population. Hum Genet. 1999 Sep;105(3):200-10. [PubMed ]
Tsai CH, Tsai FJ, Wu JY, Lin SP, Chang JG, Yang CF, Lee CC: Insertion/deletion mutations of type I oculocutaneous albinism in chinese patients from Taiwan. Hum Mutat. 1999 Dec;14(6):542. [PubMed ]
Camand O, Marchant D, Boutboul S, Pequignot M, Odent S, Dollfus H, Sutherland J, Levin A, Menasche M, Marsac C, Dufier JL, Heon E, Abitbol M: Mutation analysis of the tyrosinase gene in oculocutaneous albinism. Hum Mutat. 2001 Apr;17(4):352. [PubMed ]
Nakamura E, Miyamura Y, Matsunaga J, Kano Y, Dakeishi-Hara M, Tanita M, Kono M, Tomita Y: A novel mutation of the tyrosinase gene causing oculocutaneous albinism type 1 (OCA1). J Dermatol Sci. 2002 Feb;28(2):102-5. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

5320

Enzyme 9 Name

Aldose reductase

Enzyme 9 Synonyms

AR
Aldehyde reductase

Enzyme 9 Gene Name

AKR1B1

Enzyme 9 Protein Sequence

>Aldose reductase

MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQ
EKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGK
EFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKP
AVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAK
HNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCA
LLSCTSHKDYPFHEEF

Enzyme 9 Number of Residues

316

Enzyme 9 Molecular Weight

35854

Enzyme 9 Theoretical pI

6.99

Enzyme 9 GO Classification

Function
catalytic activity oxidoreductase activity
Process
—
Component
—

Enzyme 9 General Function

Not Available

Enzyme 9 Specific Function

Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies

Enzyme 9 Pathways

Fructose and Mannose Metabolism (map00051 )
Galactose Metabolism (map00052 )
Glycerolipid Metabolism (map00561 )
Pyruvate Metabolism (map00620 )

Enzyme 9 Reactions

alditol + NAD(P)+ = aldose + NAD(P)H + H+

Enzyme 9 Pfam Domain Function

Aldo_ket_red (PF00248 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

None

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

178487

Enzyme 9 UniProtKB/Swiss-Prot ID

P15121

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

ALDR_HUMAN Link Image

Enzyme 9 PDB ID

1T40

Enzyme 9 PDB File

Show

Enzyme 9 3D Structure

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>951 bp

ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC
TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC
CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG
GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG
TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG
AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG
GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC
ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC
AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT
GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC
CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG
GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG
CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG
ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA
CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC
TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA

Enzyme 9 GenBank Gene ID

Enzyme 9 GeneCard ID

Enzyme 9 GenAtlas ID

Enzyme 9 HGNC ID

Enzyme 9 Chromosome Location

Enzyme 9 Locus

7q35

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed ]
Chung S, LaMendola J: Cloning and sequence determination of human placental aldose reductase gene. J Biol Chem. 1989 Sep 5;264(25):14775-7. [PubMed ]
Graham A, Hedge PJ, Powell SJ, Riley J, Brown L, Gammack A, Carey F, Markham AF: Nucleotide sequence of cDNA for human aldose reductase. Nucleic Acids Res. 1989 Oct 25;17(20):8368. [PubMed ]
Grundmann U, Bohn H, Obermeier R, Amann E: Cloning and prokaryotic expression of a biologically active human placental aldose reductase. DNA Cell Biol. 1990 Apr;9(3):149-57. [PubMed ]
Nishimura C, Matsuura Y, Kokai Y, Akera T, Carper D, Morjana N, Lyons C, Flynn TG: Cloning and expression of human aldose reductase. J Biol Chem. 1990 Jun 15;265(17):9788-92. [PubMed ]
Graham A, Brown L, Hedge PJ, Gammack AJ, Markham AF: Structure of the human aldose reductase gene. J Biol Chem. 1991 Apr 15;266(11):6872-7. [PubMed ]
Ko BC, Ruepp B, Bohren KM, Gabbay KH, Chung SS: Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene. J Biol Chem. 1997 Jun 27;272(26):16431-7. [PubMed ]
Ferraretto A, Negri A, Giuliani A, De Grada L, Fuhrman Conti AM, Ronchi S: Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. Biochim Biophys Acta. 1993 Feb 17;1175(3):283-8. [PubMed ]
Morjana NA, Lyons C, Flynn TG: Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. J Biol Chem. 1989 Feb 15;264(5):2912-9. [PubMed ]
Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK: Identification of the reactive cysteine residue in human placenta aldose reductase. Biochim Biophys Acta. 1993 Aug 7;1164(3):268-72. [PubMed ]
Jaquinod M, Potier N, Klarskov K, Reymann JM, Sorokine O, Kieffer S, Barth P, Andriantomanga V, Biellmann JF, Van Dorsselaer A: Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. Eur J Biochem. 1993 Dec 15;218(3):893-903. [PubMed ]
Tarle I, Borhani DW, Wilson DK, Quiocho FA, Petrash JM: Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. J Biol Chem. 1993 Dec 5;268(34):25687-93. [PubMed ]
Wilson DK, Bohren KM, Gabbay KH, Quiocho FA: An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science. 1992 Jul 3;257(5066):81-4. [PubMed ]
Borhani DW, Harter TM, Petrash JM: The crystal structure of the aldose reductase.NADPH binary complex. J Biol Chem. 1992 Dec 5;267(34):24841-7. [PubMed ]
Wilson DK, Tarle I, Petrash JM, Quiocho FA: Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9847-51. [PubMed ]
Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH: The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 1997 Dec 23;36(51):16134-40. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

5335

Enzyme 10 Name

Short-chain specific acyl-CoA dehydrogenase, mitochondrial precursor

Enzyme 10 Synonyms

SCAD
Butyryl-CoA dehydrogenase

Enzyme 10 Gene Name

ACADS

Enzyme 10 Protein Sequence

>Short-chain specific acyl-CoA dehydrogenase, mitochondrial precursor

MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQV
DKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNN
SLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLN
GTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTAN
LIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAF
GAPLTKLQVIQFKLADMALALESARLLTWRAAMLKDNKKPFIKEAAMAKLAASEAATAIS
HQAIQILGGMGYVTEMPAERHYRDARITEIYEGTSEIQRLVIAGHLLRSYRS

Enzyme 10 Number of Residues

412

Enzyme 10 Molecular Weight

44298

Enzyme 10 Theoretical pI

8.12

Enzyme 10 GO Classification

Function
acyl-CoA dehydrogenase activity catalytic activity oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 10 General Function

Lipid transport and metabolism

Enzyme 10 Specific Function

Butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor

Enzyme 10 Pathways

Butyrate Metabolism (map00650 )
Fatty Acid Metabolism (map00071 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 10 Reactions

butanoyl-CoA + acceptor = 2-butenoyl-CoA + reduced acceptor

Enzyme 10 Pfam Domain Function

Acyl-CoA_dh_1 (PF00441 )
Acyl-CoA_dh_M (PF02770 )
Acyl-CoA_dh_N (PF02771 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

None

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

337928

Enzyme 10 UniProtKB/Swiss-Prot ID

P16219

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

ACADS_HUMAN Link Image

Enzyme 10 PDB ID

1JQI

Enzyme 10 PDB File

Show

Enzyme 10 3D Structure

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>1239 bp

ATGGCCGCCGCGCTGCTCGCCCGGGCCTCGGGCCCTGCCCGCAGAGCTCTCTGTCCTAGG
GCCTGGCGGCAGTTACACACCATCTACCAGTCTGTGGAACTGCCCGAGACACACCAGATG
TTGCTCCAGACATGCCGGGACTTTGCCGAGAAGGAGTTGTTTCCCATTGCAGCCCAGGTG
GATAAGGAACATCTCTTCCCAGCGGCTCAGGTGAAGAAGATGGGCGGGCTTGGGCTTCTG
GCCATGGACGTGCCCGAGGAGCTTGGCGGTGCTGGCCTCGATTACCTGGCCTACGCCATC
GCCATGGAGGAGATCAGCCGTGGCTGCGCCTCCACCGGAGTCATCATGAGTGTCAACAAC
TCTCTCTACCTGGGGCCCATCTTGAAGTTTGGCTCCAAGGAGCAGAAGCAGGCGTGGGTC
ACGCCTTTCACCAGTGGTGACAAAATTGGCTGCTTTGCCCTCAGCGAACCAGGGAACGGC
AGTGATGCAGGAGCTGCGTCCACCACCGCCCGGGCCGAGGGCGACTCATGGGTTCTGAAT
GGAACCAAAGCCTGGATCACCAATGCCTGGGAGGCTTCGGCTGCCGTGGTCTTTGCCAGC
ACGGACAGAGCCCTGCAAAACAAGGGCATCAGTGCCTTCCTGGTCCCCATGCCAACGCCT
GGGCTCACGTTGGGGAAGAAAGAAGACAAGCTGGGCATCCGGGGCTCATCCACGGCCAAC
CTCATCTTTGAGGACTGTCGCATCCCCAAGGACAGCATCCTGGGGGAGCCAGGGATGGGC
TTCAAGATAGCCATGCAAACCCTGGACATGGGCCGCATCGGCATCGCCTCCCAGGCCCTG
GGCATTGCCCAGACCGCCCTCGATTGTGCTGTGAACTACGCTGAGAATCGCATGGCCTTC
GGGGCGCCCCTCACCAAGCTCCAGGTCATCCAGTTCAAGTTGGCAGACATGGCCCTGGCC
CTGGAGAGTGCCCGGCTGCTGACCTGGCGCGCTGCCATGCTGAAGGATAACAAGAAGCCT
TTCATCAAGGAGGCAGCCATGGCCAAGCTGGCCGCCTCGGAGGCCGCGACCGCCATCAGC
CACCAGGCCATCCAGATCCTGGGCGGCATGGGCTACGTGACAGAGATGCCGGCAGAGCGG
CACTACCGCGACGCCCGCATCACTGAGATCTACGAGGGCACCAGCGAAATCCAGCGGCTG
GTGATCGCCGGGCATCTGCTCAGGAGCTACCGGAGCTGA

Enzyme 10 GenBank Gene ID

M26393

Enzyme 10 GeneCard ID

ACADS

Enzyme 10 GenAtlas ID

ACADS

Enzyme 10 HGNC ID

HGNC:90

Enzyme 10 Chromosome Location

Enzyme 10 Locus

12q22-qter

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Naito E, Ozasa H, Ikeda Y, Tanaka K: Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1989 May;83(5):1605-13. [PubMed ]
Corydon MJ, Andresen BS, Bross P, Kjeldsen M, Andreasen PH, Eiberg H, Kolvraa S, Gregersen N: Structural organization of the human short-chain acyl-CoA dehydrogenase gene. Mamm Genome. 1997 Dec;8(12):922-6. [PubMed ]
Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
Naito E, Indo Y, Tanaka K: Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J Clin Invest. 1990 May;85(5):1575-82. [PubMed ]
Gregersen N, Winter VS, Corydon MJ, Corydon TJ, Rinaldo P, Ribes A, Martinez G, Bennett MJ, Vianey-Saban C, Bhala A, Hale DE, Lehnert W, Kmoch S, Roig M, Riudor E, Eiberg H, Andresen BS, Bross P, Bolund LA, Kolvraa S: Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet. 1998 Apr;7(4):619-27. [PubMed ]
Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N: Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

5349

Enzyme 11 Name

NADH-ubiquinone oxidoreductase chain 1

Enzyme 11 Synonyms

NADH dehydrogenase subunit 1

Enzyme 11 Gene Name

MT-ND1

Enzyme 11 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 1

MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEP
LKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSG
WASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWP
LAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTT
IFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLAL
LMWYVSMPITISSIPPQT

Enzyme 11 Number of Residues

318

Enzyme 11 Molecular Weight

35661

Enzyme 11 Theoretical pI

6.53

Enzyme 11 GO Classification

Function
—
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
cell membrane

Enzyme 11 General Function

Energy production and conversion

Enzyme 11 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 11 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 11 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 11 Pfam Domain Function

NADHdh (PF00146 )

Enzyme 11 Signals

1-18

Enzyme 11 Transmembrane Regions

68-90
100-122
135-157
172-191
222-244
254-273
293-315

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

Not Available

Enzyme 11 UniProtKB/Swiss-Prot ID

P03886

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

NU1M_HUMAN Link Image

Enzyme 11 PDB ID

Not Available

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

Not Available

Enzyme 11 GenBank Gene ID

V00662

Enzyme 11 GeneCard ID

MT-ND1

Enzyme 11 GenAtlas ID

MT-ND1

Enzyme 11 HGNC ID

HGNC:7455

Enzyme 11 Chromosome Location

Enzyme 11 Locus

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Howell N, Bindoff LA, McCullough DA, Kubacka I, Poulton J, Mackey D, Taylor L, Turnbull DM: Leber hereditary optic neuropathy: identification of the same mitochondrial ND1 mutation in six pedigrees. Am J Hum Genet. 1991 Nov;49(5):939-50. [PubMed ]
Huoponen K, Vilkki J, Aula P, Nikoskelainen EK, Savontaus ML: A new mtDNA mutation associated with Leber hereditary optic neuroretinopathy. Am J Hum Genet. 1991 Jun;48(6):1147-53. [PubMed ]
Howell N, Kubacka I, Xu M, McCullough DA: Leber hereditary optic neuropathy: involvement of the mitochondrial ND1 gene and evidence for an intragenic suppressor mutation. Am J Hum Genet. 1991 May;48(5):935-42. [PubMed ]
Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed ]
Majander A, Huoponen K, Savontaus ML, Nikoskelainen E, Wikstrom M: Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 1991 Nov 4;292(1-2):289-92. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Johns DR, Neufeld MJ, Park RD: An ND-6 mitochondrial DNA mutation associated with Leber hereditary optic neuropathy. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1551-7. [PubMed ]
Shoffner JM, Brown MD, Torroni A, Lott MT, Cabell MF, Mirra SS, Beal MF, Yang CC, Gearing M, Salvo R, et al.: Mitochondrial DNA variants observed in Alzheimer disease and Parkinson disease patients. Genomics. 1993 Jul;17(1):171-84. [PubMed ]
Jaksch M, Hofmann S, Kaufhold P, Obermaier-Kusser B, Zierz S, Gerbitz KD: A novel combination of mitochondrial tRNA and ND1 gene mutations in a syndrome with MELAS, cardiomyopathy, and diabetes mellitus. Hum Mutat. 1996;7(4):358-60. [PubMed ]
Nakagawa Y, Ikegami H, Yamato E, Takekawa K, Fujisawa T, Hamada Y, Ueda H, Uchigata Y, Miki T, Kumahara Y, et al.: A new mitochondrial DNA mutation associated with non-insulin-dependent diabetes mellitus. Biochem Biophys Res Commun. 1995 Apr 17;209(2):664-8. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

5351

Enzyme 12 Name

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Enzyme 12 Synonyms

E- NPP 1
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
NPPase]

Enzyme 12 Gene Name

ENPP1

Enzyme 12 Protein Sequence

>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED

Enzyme 12 Number of Residues

925

Enzyme 12 Molecular Weight

104925

Enzyme 12 Theoretical pI

7.14

Enzyme 12 GO Classification

Function
binding catalytic activity endonuclease activity hydrolase activity hydrolase activity, acting on ester bonds nuclease activity nucleic acid binding
Process
cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleotide metabolism physiological process
Component
—

Enzyme 12 General Function

Not Available

Enzyme 12 Specific Function

Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity

Enzyme 12 Pathways

Nicotinate and Nicotinamide Metabolism (map00760 )
Pantothenate and CoA Biosynthesis (map00770 )
Purine Metabolism (map00230 )
Riboflavin Metabolism (map00740 )
Starch and Sucrose Metabolism (map00500 )

Enzyme 12 Reactions

A dinucleotide + H2O = 2 mononucleotides

Enzyme 12 Pfam Domain Function

Phosphodiest (PF01663 )
Somatomedin_B (PF01033 )

Enzyme 12 Signals

None

Enzyme 12 Transmembrane Regions

77-97

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

189650

Enzyme 12 UniProtKB/Swiss-Prot ID

P22413

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

ENPP1_HUMAN Link Image

Enzyme 12 PDB ID

Not Available

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

>2622 bp

ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA

Enzyme 12 GenBank Gene ID

M57736

Enzyme 12 GeneCard ID

ENPP1

Enzyme 12 GenAtlas ID

ENPP1

Enzyme 12 HGNC ID

HGNC:3356

Enzyme 12 Chromosome Location

Enzyme 12 Locus

6q22-q23

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed ]
Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed ]
Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed ]
Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed ]
Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed ]
Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed ]

Enzyme 12 Metabolite References

Not Available

Enzyme 13 [top]

Enzyme 13 ID

5352

Enzyme 13 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial precursor

Enzyme 13 Synonyms

NADH-ubiquinone oxidoreductase 49 kDa subunit
Complex I-49kD
CI-49kD

Enzyme 13 Gene Name

NDUFS2

Enzyme 13 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial precursor

MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGAVMYPSKETAH
WKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVMELSGEMVRKCDPHIGLLHRGT
EKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIRPPPRAQWIRVLFGEITRL
LNHIMAVTTHALDLGAMTPFFWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGL
MDDIYQFSKNFSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQW
DLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNKMPPGEIKVDD
AKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPY
RCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEVDR

Enzyme 13 Number of Residues

463

Enzyme 13 Molecular Weight

52546

Enzyme 13 Theoretical pI

7.61

Enzyme 13 GO Classification

Function
catalytic activity electron transporter activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 13 General Function

Energy production and conversion

Enzyme 13 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 13 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 13 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 13 Pfam Domain Function

Complex1_49kDa (PF00346 )

Enzyme 13 Signals

1-15

Enzyme 13 Transmembrane Regions

Not Available

Enzyme 13 Essentiality

Not Available

Enzyme 13 GenBank ID Protein

3540239

Enzyme 13 UniProtKB/Swiss-Prot ID

O75306

Enzyme 13 UniProtKB/Swiss-Prot Entry Name

NDUS2_HUMAN Link Image

Enzyme 13 PDB ID

Not Available

Enzyme 13 Cellular Location

Not Available

Enzyme 13 Gene Sequence

>1392 bp

ATGGCGGCGCTGAGGGCTTTGTGCGGCTTCCGGGGCGTCGCGGCCCAGGTGCTGCGGCCT
GGGGCTGGAGGCCGATTGCCGATTCAGCCCAGCAGAGGTGTTCGGCAGTGGCAGCCAGAT
GTGGAATGGGCACAGCAGTTTGGGGGAGCTGTTATGTACCCAAGCAAAGAAACAGCCCAC
TGGAAGCCTCCACCTTGGAATGATGTGGACCCTCCAAAGGACACAATTGTGAAGAACATT
ACCCTGAACTTTGGGCCCCAACACCCAGCAGCGCATGGTGTCCTGCGACTAGTGATGGAA
TTGAGTGGGGAGATGGTGCGGAAGTGTGATCCTCACATCGGGCTCCTGCACCGAGGCACT
GAGAAGCTCATTGAATACAAGACCTATCTTCAGGCCCTTCCATACTTTGACCGGCTAGAC
TATGTGTCCATGATGTGTAACGAACAGGCCTATTCTCTAGCTGTGGAGAAGTTGCTAAAC
ATCCGGCCTCCTCCTCGGGCACAGTGGATCCGAGTGCTGTTTGGAGAAATCACACGTTTG
TTGAACCACATCATGGCTGTGACCACACATGCCCTGGACCTTGGGGCCATGACCCCTTTC
TTCTGGCTGTTTGAAGAAAGGGAGAAGATGTTTGAGTTCTACGAGCGAGTGTCTGGAGCC
CGAATGCATGCTGCTTATATCCGGCCAGGAGGAGTGCACCAGGACCTACCCCTTGGGCTT
ATGGATGACATTTATCAGTTTTCTAAGAACTTCTCTCTTCGGCTTGATGAGTTGGAGGAG
TTGCTGACCAACAATAGGATCTGGCGAAATCGGACAATTGACATTGGGGTTGTAACAGCA
GAAGAAGCACTTAACTATGGTTTTAGTGGAGTGATGCTTCGGGGCTCAGGCATCCAGTGG
GACCTGCGGAAGACCCAGCCCTATGATGTTTACGACCAGGTTGAGTTTGATGTTCCTGTT
GGTTCTCGAGGGGACTGCTATGATAGGTACCTGTGCCGGGTGGAGGAGATGCGCCAGTCC
CTGAGAATTATCGCACAGTGTCTAAACAAGATGCCTCCTGGGGAGATCAAGGTTGATGAT
GCCAAAGTGTCTCCACCTAAGCGAGCAGAGATGAAGACTTCCATGGAGTCACTGATTCAT
CACTTTAAGTTGTATACTGAGGGCTACCAAGTTCCTCCAGGAGCCACATATACTGCCATT
GAGGCTCCCAAGGGAGAGTTTGGGGTGTACCTGGTGTCTGATGGCAGCAGCCGCCCTTAT
CGATGCAAGATCAAGGCTCCTGGTTTTGCCCATCTGGCTGGTTTGGACAAGATGTCTAAG
GGACACATGTTGGCAGATGTCGTTGCCATCATAGGTACCCAAGATATTGTATTTGGAGAA
GTAGATCGGTGA

Enzyme 13 GenBank Gene ID

AF013160

Enzyme 13 GeneCard ID

NDUFS2

Enzyme 13 GenAtlas ID

NDUFS2

Enzyme 13 HGNC ID

HGNC:7708

Enzyme 13 Chromosome Location

Enzyme 13 Locus

1q23

Enzyme 13 SNPs

SNPJam Report Link Image

Enzyme 13 General References

Procaccio V, de Sury R, Martinez P, Depetris D, Rabilloud T, Soularue P, Lunardi J, Issartel J: Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria. Mamm Genome. 1998 Jun;9(6):482-4. [PubMed ]
Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J: cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed. Biochem Biophys Res Commun. 1998 Jun 29;247(3):751-8. [PubMed ]

Enzyme 13 Metabolite References

Not Available

Enzyme 14 [top]

Enzyme 14 ID

5356

Enzyme 14 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

Enzyme 14 Synonyms

NADH-ubiquinone oxidoreductase subunit B17.2
Complex I-B17.2
CI-B17.2
CIB17.2
13 kDa differentiation- associated protein

Enzyme 14 Gene Name

NDUFA12

Enzyme 14 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12

MELVQVLKRGLQQITGHGGLRGYLRVFFRTNDAKVGTLVGEDKYGNKYYEDNKQFFGRHR
WVVYTTEMNGKNTFWDVDGSMVPPEWHRWLHSMTDDPPTTKPLTARKFIWTNHKFNVTGT
PEQYVPYSTTRKKIQEWIPPSTPYK

Enzyme 14 Number of Residues

145

Enzyme 14 Molecular Weight

17115

Enzyme 14 Theoretical pI

10.10

Enzyme 14 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity electron transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
cell membrane mitochondrial inner membrane organelle inner membrane organelle membrane

Enzyme 14 General Function

Energy production and conversion

Enzyme 14 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 14 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 14 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 14 Pfam Domain Function

NDUFA12 (PF05071 )

Enzyme 14 Signals

None

Enzyme 14 Transmembrane Regions

None

Enzyme 14 Essentiality

Not Available

Enzyme 14 GenBank ID Protein

9651637

Enzyme 14 UniProtKB/Swiss-Prot ID

Q9UI09

Enzyme 14 UniProtKB/Swiss-Prot Entry Name

NDUAC_HUMAN Link Image

Enzyme 14 PDB ID

Not Available

Enzyme 14 Cellular Location

Not Available

Enzyme 14 Gene Sequence

>438 bp

ATGGAGTTAGTGCAGGTCCTGAAACGCGGGCTGCAGCAGATCACCGGCCACGGCGGTCTC
CGAGGCTATCTACGGGTTTTTTTCAGGACAAATGATGCGAAGGTTGGTACATTAGTGGGG
GAAGACAAATATGGAAACAAATACTATGAAGACAACAAGCAATTTTTTGGCCGTCACCGA
TGGGTTGTATATACTACTGAAATGAATGGCAAAAACACATTCTGGGATGTGGATGGAAGC
ATGGTGCCTCCTGAATGGCATCGTTGGCTTCACAGTATGACTGATGATCCTCCAACAACA
AAACCACTTACTGCTCGTAAATTCATTTGGACGAACCATAAATTCAACGTGACTGGCACC
CCAGAACAATATGTACCTTATTCTACCACTAGAAAGAAGATTCAGGAGTGGATCCCACCT
TCAACACCTTACAAGTAA

Enzyme 14 GenBank Gene ID

AF217092

Enzyme 14 GeneCard ID

NDUFA12

Enzyme 14 GenAtlas ID

NDUFA12

Enzyme 14 HGNC ID

HGNC:23987 Link Image

Enzyme 14 Chromosome Location

Enzyme 14 Locus

12q22

Enzyme 14 SNPs

SNPJam Report Link Image

Enzyme 14 General References

Triepels R, Smeitink J, Loeffen J, Smeets R, Trijbels F, van den Heuvel L: Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and mutational analysis of 19 genes of the HP fraction in complex I-deficient-patients. Hum Genet. 2000 Apr;106(4):385-91. [PubMed ]
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

Enzyme 14 Metabolite References

Not Available

Enzyme 15 [top]

Enzyme 15 ID

5357

Enzyme 15 Name

NADH-cytochrome b5 reductase 3

Enzyme 15 Synonyms

Cytochrome b5 reductase
B5R
Diaphorase-1[Contains: NADH-cytochrome b5 reductase 3 membrane-bound form
NADH-cytochrome b5 reductase 3 soluble form]

Enzyme 15 Gene Name

CYB5R3

Enzyme 15 Protein Sequence

>NADH-cytochrome b5 reductase 3

MGAQLSTLGHMVLFPVWFLYSLLMKLFQRSTPAITLESPDIKYPLRLIDREIISHDTRRF
RFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFKDTHPK
FPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIRPDKKSNPIIRTVKSVGMIAG
GTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLD
RAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFV
F

Enzyme 15 Number of Residues

301

Enzyme 15 Molecular Weight

34235

Enzyme 15 Theoretical pI

7.68

Enzyme 15 GO Classification

Function
FAD binding NAD binding adenyl nucleotide binding binding catalytic activity coenzyme binding cofactor binding cytochrome-b5 reductase activity electron transporter activity nucleotide binding oxidoreductase activity purine nucleotide binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 15 General Function

Coenzyme transport and metabolism

Enzyme 15 Specific Function

Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction

Enzyme 15 Pathways

Aminosugars metabolism (map00530 )

Enzyme 15 Reactions

NADH + H+ + 2 ferricytochrome b5 = NAD+ + 2 ferrocytochrome b5

Enzyme 15 Pfam Domain Function

FAD_binding_6 (PF00970 )
NAD_binding_1 (PF00175 )

Enzyme 15 Signals

1-33

Enzyme 15 Transmembrane Regions

Not Available

Enzyme 15 Essentiality

Not Available

Enzyme 15 GenBank ID Protein

553600

Enzyme 15 UniProtKB/Swiss-Prot ID

P00387

Enzyme 15 UniProtKB/Swiss-Prot Entry Name

NB5R3_HUMAN Link Image

Enzyme 15 PDB ID

1UMK

Enzyme 15 PDB File

Show

Enzyme 15 3D Structure

Enzyme 15 Cellular Location

Not Available

Enzyme 15 Gene Sequence

>906 bp

ATGGGGGCCCAGCTCAGCACGTTGGGCCATATGGTCCTCTTCCCAGTCTGGTTCCTGTAC
AGTCTGCTCATGAAGCTGTTCCAGGGCTCCACGCCAGCCATCACCCTCGAGAGCCCGGAC
ATCAAGTACCCGCTGCGGCTCATCGACCGGGAGATCATCAGCCATGACACCCGGCGCTTC
CGCTTTGCCCTGCCGCCACCCCAGCACATCCTGGGCCTCCCTGTCGGCCAGCACATCTAC
CTCTCGGCTCGAATTGATGGAAACCTGGTCGTCCGGCCCTATACACCAATCTCCAGCGAT
GATGACAAGGGCTTCGTGGACCTGGTCATCAAGGTTTACTTCAAGGACACCCATCCCAAG
TTTCCCGCTGGAGGGAAGATGTCTCAGTACCTGGAGAGCATGCAGATTGGAGACACCATT
GAGTTCCGGGGCCCCAGTGGGCTGCTGGTCTACCAGGGCAAAGGGAAGTTCGCCATCCGA
CCTGACAAAAAGTCCAACCCTATCATCAGGACAGTGAAGTCTGTGGGCATGATCGCGGGA
GGGACAGGCATCACCCCGATGCTGCAGGTGATCCGCGCCATCATGAAGGACCCTGATGAC
CACACTGTGTGCCACCTGCTCTTTGCCAACCAGACCGAGAAGGACATCCTGCTGCGACCT
GAGCTGGAGGAACTCAGGAACAAACATTCTGCACGCTTCAAGCTCTGGTACACGCTGGAC
AGAGCCCCTGAAGCCTGGGACTACGGCCAGGGCTTCGTGAATGAGGAGATGATCCGGGAC
CACCTTCCACCCCCAGAGGAGGAGCCGCTGGTGCTGATGTGTGGCCCCCCACCCATGATC
CAGTACGCCTGCCTTCCCAACCTGGACCACGTGGGCCACCCCACGGAGCGCTGCTTCGTC
TTCTGA

Enzyme 15 GenBank Gene ID

M28713

Enzyme 15 GeneCard ID

CYB5R3

Enzyme 15 GenAtlas ID

CYB5R3

Enzyme 15 HGNC ID

HGNC:2873

Enzyme 15 Chromosome Location

Enzyme 15 Locus

22q13.31-qter|22q13.2-q13.31

Enzyme 15 SNPs

SNPJam Report Link Image

Enzyme 15 General References

Tomatsu S, Kobayashi Y, Fukumaki Y, Yubisui T, Orii T, Sakaki Y: The organization and the complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene. Gene. 1989 Aug 15;80(2):353-61. [PubMed ]
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
Yubisui T, Naitoh Y, Zenno S, Tamura M, Takeshita M, Sakaki Y: Molecular cloning of cDNAs of human liver and placenta NADH-cytochrome b5 reductase. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3609-13. [PubMed ]
Murakami K, Yubisui T, Takeshita M, Miyata T: The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases. J Biochem. 1989 Feb;105(2):312-7. [PubMed ]
Yubisui T, Miyata T, Iwanaga S, Tamura M, Takeshita M: Complete amino acid sequence of NADH-cytochrome b5 reductase purified from human erythrocytes. J Biochem (Tokyo). 1986 Feb;99(2):407-22. [PubMed ]
Yubisui T, Miyata T, Iwanaga S, Tamura M, Yoshida S, Takeshita M, Nakajima H: Amino acid sequence of NADH-cytochrome b5 reductase of human erythrocytes. J Biochem (Tokyo). 1984 Aug;96(2):579-82. [PubMed ]
Bulbarelli A, Valentini A, DeSilvestris M, Cappellini MD, Borgese N: An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humans. Blood. 1998 Jul 1;92(1):310-9. [PubMed ]
Shirabe K, Yubisui T, Nishino T, Takeshita M: Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential. J Biol Chem. 1991 Apr 25;266(12):7531-6. [PubMed ]
Yubisui T, Shirabe K, Takeshita M, Kobayashi Y, Fukumaki Y, Sakaki Y, Takano T: Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase. J Biol Chem. 1991 Jan 5;266(1):66-70. [PubMed ]
Katsube T, Sakamoto N, Kobayashi Y, Seki R, Hirano M, Tanishima K, Tomoda A, Takazakura E, Yubisui T, Takeshita M, et al.: Exonic point mutations in NADH-cytochrome B5 reductase genes of homozygotes for hereditary methemoglobinemia, types I and III: putative mechanisms of tissue-dependent enzyme deficiency. Am J Hum Genet. 1991 Apr;48(4):799-808. [PubMed ]
Shirabe K, Yubisui T, Borgese N, Tang CY, Hultquist DE, Takeshita M: Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J Biol Chem. 1992 Oct 5;267(28):20416-21. [PubMed ]
Shirabe K, Fujimoto Y, Yubisui T, Takeshita M: An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme. J Biol Chem. 1994 Feb 25;269(8):5952-7. [PubMed ]
Vieira LM, Kaplan JC, Kahn A, Leroux A: Four new mutations in the NADH-cytochrome b5 reductase gene from patients with recessive congenital methemoglobinemia type II. Blood. 1995 Apr 15;85(8):2254-62. [PubMed ]
Jenkins MM, Prchal JT: A high-frequency polymorphism of NADH-cytochrome b5 reductase in African-Americans. Hum Genet. 1997 Feb;99(2):248-50. [PubMed ]
Wu YS, Huang CH, Wan Y, Huang QJ, Zhu ZY: Identification of a novel point mutation (Leu72Pro) in the NADH-cytochrome b5 reductase gene of a patient with hereditary methaemoglobinaemia type I. Br J Haematol. 1998 Jul;102(2):575-7. [PubMed ]
Higasa K, Manabe JI, Yubisui T, Sumimoto H, Pung-Amritt P, Tanphaichitr VS, Fukumaki Y: Molecular basis of hereditary methaemoglobinaemia, types I and II: two novel mutations in the NADH-cytochrome b5 reductase gene. Br J Haematol. 1998 Dec;103(4):922-30. [PubMed ]
Wang Y, Wu YS, Zheng PZ, Yang WX, Fang GA, Tang YC, Xie F, Lan FH, Zhu ZY: A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia. Blood. 2000 May 15;95(10):3250-5. [PubMed ]

Enzyme 15 Metabolite References

Not Available

Enzyme 16 [top]

Enzyme 16 ID

5359

Enzyme 16 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

Enzyme 16 Synonyms

NADH-ubiquinone oxidoreductase MWFE subunit
Complex I-MWFE
CI-MWFE

Enzyme 16 Gene Name

NDUFA1

Enzyme 16 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1

MWFEILPGLSVMGVCLLIPGLATAYIHRFTNGGKEKRVAHFGYHWSLMERDRRISGVDRY
YVSKGLENID

Enzyme 16 Number of Residues

Enzyme 16 Molecular Weight

8073

Enzyme 16 Theoretical pI

9.12

Enzyme 16 GO Classification

Not Available

Enzyme 16 General Function

Not Available

Enzyme 16 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 16 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 16 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 16 Pfam Domain Function

Not Available

Enzyme 16 Signals

1-24

Enzyme 16 Transmembrane Regions

Not Available

Enzyme 16 Essentiality

Not Available

Enzyme 16 GenBank ID Protein

2274974

Enzyme 16 UniProtKB/Swiss-Prot ID

O15239

Enzyme 16 UniProtKB/Swiss-Prot Entry Name

NDUA1_HUMAN Link Image

Enzyme 16 PDB ID

Not Available

Enzyme 16 Cellular Location

Not Available

Enzyme 16 Gene Sequence

>213 bp

ATGTGGTTCGAGATTCTCCCCGGACTCTCCGTCATGGGCGTGTGCTTGTTGATTCCAGGA
CTGGCTACTGCGTACATCCACAGGTTCACTAACGGGGGCAAGGAAAAAAGGGTTGCTCAT
TTTGGGTATCACTGGAGTCTGATGGAAAGAGATAGGCGCATCTCTGGAGTTGATCGTTAC
TATGTGTCAAAGGGTTTGGAGAACATTGATTAA

Enzyme 16 GenBank Gene ID

X81900

Enzyme 16 GeneCard ID

NDUFA1

Enzyme 16 GenAtlas ID

NDUFA1

Enzyme 16 HGNC ID

HGNC:7683

Enzyme 16 Chromosome Location

Enzyme 16 Locus

Xq24

Enzyme 16 SNPs

SNPJam Report Link Image

Enzyme 16 General References

Zhuchenko O, Wehnert M, Bailey J, Sun ZS, Lee CC: Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I. Genomics. 1996 Nov 1;37(3):281-8. [PubMed ]
Frattini A, Faranda S, Bagnasco L, Patrosso C, Nulli P, Zucchi I, Vezzoni P: Identification of a new member (ZNF183) of the Ring finger gene family in Xq24-25. Gene. 1997 Jun 19;192(2):291-8. [PubMed ]

Enzyme 16 Metabolite References

Not Available

Enzyme 17 [top]

Enzyme 17 ID

5360

Enzyme 17 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2

Enzyme 17 Synonyms

NADH-ubiquinone oxidoreductase MLRQ subunit homolog
NUOMS

Enzyme 17 Gene Name

NDUFA4L2

Enzyme 17 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2

MAGASLGARFYRQIKRHPGIIPMIGLICLGMGSAALYLLRLALRSPDVCWDRKNNPEPWN
RLSPNDQYKFLAVSTDYKKLKKDRPDF

Enzyme 17 Number of Residues

Enzyme 17 Molecular Weight

9966

Enzyme 17 Theoretical pI

10.46

Enzyme 17 GO Classification

Not Available

Enzyme 17 General Function

Not Available

Enzyme 17 Specific Function

Not Available

Enzyme 17 Pathways

Not Available

Enzyme 17 Reactions

Not Available

Enzyme 17 Pfam Domain Function

Not Available

Enzyme 17 Signals

1-35

Enzyme 17 Transmembrane Regions

Not Available

Enzyme 17 Essentiality

Not Available

Enzyme 17 GenBank ID Protein

8895095

Enzyme 17 UniProtKB/Swiss-Prot ID

Q9NRX3

Enzyme 17 UniProtKB/Swiss-Prot Entry Name

NUA4L_HUMAN Link Image

Enzyme 17 PDB ID

Not Available

Enzyme 17 Cellular Location

Not Available

Enzyme 17 Gene Sequence

>264 bp

ATGGCAGGAGCCAGTCTTGGGGCCCGCTTCTACCGGCAGATCAAAAGACATCCGGGGATC
ATCCCGATGATCGGCTTAATCTGCCTGGGCATGGGCAGCGCTGCGCTTTACTTGCTGCGA
CTCGCCCTTCGCAGCCCCGACGTCTGCTGGGACAGAAAGAACAACCCGGAGCCCTGGAAC
CGCCTGAGCCCCAATGACCAATACAAGTTCCTTGCAGTTTCCACTGACTATAAGAAGCTG
AAGAAGGACCGGCCAGACTTCTAA

Enzyme 17 GenBank Gene ID

AF164796

Enzyme 17 GeneCard ID

NDUFA4L2

Enzyme 17 GenAtlas ID

NDUFA4L2

Enzyme 17 HGNC ID

HGNC:29836 Link Image

Enzyme 17 Chromosome Location

Enzyme 17 Locus

12q13.3

Enzyme 17 SNPs

SNPJam Report Link Image

Enzyme 17 General References

Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

Enzyme 17 Metabolite References

Not Available

Enzyme 18 [top]

Enzyme 18 ID

5361

Enzyme 18 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

Enzyme 18 Synonyms

NADH-ubiquinone oxidoreductase B9 subunit
Complex I-B9
CI-B9

Enzyme 18 Gene Name

NDUFA3

Enzyme 18 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3

MAARVGAFLKNAWDKEPVLVVSFVVGGLAVILPPLSPYFKYSVMINKATPYNYPVPVRDD
GNMPDVPSHPQDPQGPSLEWLKKL

Enzyme 18 Number of Residues

Enzyme 18 Molecular Weight

9279

Enzyme 18 Theoretical pI

8.92

Enzyme 18 GO Classification

Not Available

Enzyme 18 General Function

Not Available

Enzyme 18 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 18 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 18 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 18 Pfam Domain Function

Not Available

Enzyme 18 Signals

1-29

Enzyme 18 Transmembrane Regions

Not Available

Enzyme 18 Essentiality

Not Available

Enzyme 18 GenBank ID Protein

4164444

Enzyme 18 UniProtKB/Swiss-Prot ID

O95167

Enzyme 18 UniProtKB/Swiss-Prot Entry Name

NDUA3_HUMAN Link Image

Enzyme 18 PDB ID

Not Available

Enzyme 18 Cellular Location

Not Available

Enzyme 18 Gene Sequence

>255 bp

ATGGCTGCGAGAGTCGGCGCCTTCCTCAAGAATGCCTGGGACAAGGAGCCAGTGCTGGTC
GTGTCCTTCGTCGTCGGGGGCCTCGCTGTAATTCTGCCCCCATTGAGCCCCTACTTCAAG
TACTCCGTCATGATCAACAAGGCCACGCCCTACAACTACCCAGTGCCCGTCCGTGATGAT
GGGAACATGCCCGACGTGCCCAGCCACCCCCAGGACCCTCAGGGCCCCAGCCTGGAGTGG
CTGAAGAAACTGTGA

Enzyme 18 GenBank Gene ID

AF044955

Enzyme 18 GeneCard ID

NDUFA3

Enzyme 18 GenAtlas ID

NDUFA3

Enzyme 18 HGNC ID

HGNC:7686

Enzyme 18 Chromosome Location

Enzyme 18 Locus

19q13.42

Enzyme 18 SNPs

SNPJam Report Link Image

Enzyme 18 General References

Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

Enzyme 18 Metabolite References

Not Available

Enzyme 19 [top]

Enzyme 19 ID

5364

Enzyme 19 Name

NADH-ubiquinone oxidoreductase chain 4L

Enzyme 19 Synonyms

NADH dehydrogenase subunit 4L

Enzyme 19 Gene Name

MT-ND4L

Enzyme 19 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 4L

MPLIYMNIMLAFTISLLGMLVYRSHLMSSLLCLEGMMLSLFIMATLMTLNTHSLLANIVP
IAMLVFAACEAAVGLALLVSISNTYGLDYVHNLNLLQC

Enzyme 19 Number of Residues

Enzyme 19 Molecular Weight

10741

Enzyme 19 Theoretical pI

6.20

Enzyme 19 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 19 General Function

Not Available

Enzyme 19 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 19 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 19 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 19 Pfam Domain Function

Oxidored_q2 (PF00420 )

Enzyme 19 Signals

1-18

Enzyme 19 Transmembrane Regions

26-48
58-80

Enzyme 19 Essentiality

Not Available

Enzyme 19 GenBank ID Protein

Not Available

Enzyme 19 UniProtKB/Swiss-Prot ID

P03901

Enzyme 19 UniProtKB/Swiss-Prot Entry Name

NU4LM_HUMAN Link Image

Enzyme 19 PDB ID

Not Available

Enzyme 19 Cellular Location

Not Available

Enzyme 19 Gene Sequence

Not Available

Enzyme 19 GenBank Gene ID

J01415

Enzyme 19 GeneCard ID

MT-ND4L

Enzyme 19 GenAtlas ID

MT-ND4L

Enzyme 19 HGNC ID

HGNC:7460

Enzyme 19 Chromosome Location

Enzyme 19 Locus

Enzyme 19 SNPs

SNPJam Report Link Image

Enzyme 19 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
Arnason U, Xu X, Gullberg A: Comparison between the complete mitochondrial DNA sequences of Homo and the common chimpanzee based on nonchimeric sequences. J Mol Evol. 1996 Feb;42(2):145-52. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Brown MD, Torroni A, Reckord CL, Wallace DC: Phylogenetic analysis of Leber's hereditary optic neuropathy mitochondrial DNA's indicates multiple independent occurrences of the common mutations. Hum Mutat. 1995;6(4):311-25. [PubMed ]
Polyak K, Li Y, Zhu H, Lengauer C, Willson JK, Markowitz SD, Trush MA, Kinzler KW, Vogelstein B: Somatic mutations of the mitochondrial genome in human colorectal tumours. Nat Genet. 1998 Nov;20(3):291-3. [PubMed ]

Enzyme 19 Metabolite References

Not Available

Enzyme 20 [top]

Enzyme 20 ID

5365

Enzyme 20 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

Enzyme 20 Synonyms

NADH-ubiquinone oxidoreductase subunit B14.7
Complex I-B14.7
CI-B14.7

Enzyme 20 Gene Name

NDUFA11

Enzyme 20 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11

MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYT
FTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARTHNYGIGAAACVYFGI
AASLVKMGRLEGWEVFAKPKV

Enzyme 20 Number of Residues

141

Enzyme 20 Molecular Weight

14852

Enzyme 20 Theoretical pI

8.89

Enzyme 20 GO Classification

Not Available

Enzyme 20 General Function

Not Available

Enzyme 20 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 20 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 20 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 20 Pfam Domain Function

Not Available

Enzyme 20 Signals

None

Enzyme 20 Transmembrane Regions

21-43 58-80

Enzyme 20 Essentiality

Not Available

Enzyme 20 GenBank ID Protein

28170654

Enzyme 20 UniProtKB/Swiss-Prot ID

Q86Y39

Enzyme 20 UniProtKB/Swiss-Prot Entry Name

NDUAB_HUMAN Link Image

Enzyme 20 PDB ID

Not Available

Enzyme 20 Cellular Location

Not Available

Enzyme 20 Gene Sequence

>426 bp

ATGGCGCCGAAGGTTTTTCGTCAGTACTGGGATATCCCCGATGGCACCGATTGCCACCGC
AAAGCCTACAGCACCACCAGTATTGCCAGCGTCGCTGGCCTGACCGCCGCTGCCTACAGA
GTCACACTCAATCCTCCGGGCACCTTCCTTGAAGGAGTGGCTAAGGTTGGACAATACACG
TTCACTGCAGCTGCTGTCGGGGCCGTGTTTGGCCTCACCACCTGCATCAGCGCCCATGTC
CGCGAGAAGCCCGACGACCCCCTGAACTACTTCCTCGGTGGCTGCGCCGGAGGCCTGACT
CTGGGAGCACGCACGCACAACTACGGGATTGGCGCCGCCGCCTGCGTGTACTTTGGCATA
GCGGCCTCCCTGGTCAAGATGGGCCGGCTGGAGGGCTGGGAGGTGTTTGCAAAACCCAAG
GTGTGA

Enzyme 20 GenBank Gene ID

AJ539081

Enzyme 20 GeneCard ID

NDUFA11

Enzyme 20 GenAtlas ID

NDUFA11

Enzyme 20 HGNC ID

HGNC:20371 Link Image

Enzyme 20 Chromosome Location

Enzyme 20 Locus

19p13.3

Enzyme 20 SNPs

SNPJam Report Link Image

Enzyme 20 General References

Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]

Enzyme 20 Metabolite References

Not Available

Enzyme 21 [top]

Enzyme 21 ID

5367

Enzyme 21 Name

Lathosterol oxidase

Enzyme 21 Synonyms

Lathosterol 5-desaturase
Delta(7-sterol 5-desaturase
C-5 sterol desaturase
Sterol-C5- desaturase

Enzyme 21 Gene Name

SC5DL

Enzyme 21 Protein Sequence

>Lathosterol oxidase

MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE

Enzyme 21 Number of Residues

299

Enzyme 21 Molecular Weight

35301

Enzyme 21 Theoretical pI

8.24

Enzyme 21 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 21 General Function

Lipid transport and metabolism

Enzyme 21 Specific Function

Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol

Enzyme 21 Pathways

Not Available

Enzyme 21 Reactions

Not Available

Enzyme 21 Pfam Domain Function

Sterol_desat (PF01598 )

Enzyme 21 Signals

None

Enzyme 21 Transmembrane Regions

32-52 79-99 117-137 186-206

Enzyme 21 Essentiality

Not Available

Enzyme 21 GenBank ID Protein

1906796

Enzyme 21 UniProtKB/Swiss-Prot ID

O75845

Enzyme 21 UniProtKB/Swiss-Prot Entry Name

SC5D_HUMAN Link Image

Enzyme 21 PDB ID

Not Available

Enzyme 21 Cellular Location

Not Available

Enzyme 21 Gene Sequence

>711 bp

ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA

Enzyme 21 GenBank Gene ID

D85181

Enzyme 21 GeneCard ID

SC5DL

Enzyme 21 GenAtlas ID

SC5DL

Enzyme 21 HGNC ID

HGNC:10547 Link Image

Enzyme 21 Chromosome Location

Enzyme 21 Locus

11q23.3

Enzyme 21 SNPs

SNPJam Report Link Image

Enzyme 21 General References

Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed ]
Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed ]
Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed ]
Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed ]
Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed ]

Enzyme 21 Metabolite References

Not Available

Enzyme 22 [top]

Enzyme 22 ID

5369

Enzyme 22 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial precursor

Enzyme 22 Synonyms

NADH-ubiquinone oxidoreductase 18 kDa subunit
Complex I-18 kDa
CI-18 kDa
Complex I-AQDQ
CI- AQDQ

Enzyme 22 Gene Name

NDUFS4

Enzyme 22 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial precursor

MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLD
ITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADP
LSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK

Enzyme 22 Number of Residues

175

Enzyme 22 Molecular Weight

20108

Enzyme 22 Theoretical pI

11.02

Enzyme 22 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 22 General Function

Not Available

Enzyme 22 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 22 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 22 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 22 Pfam Domain Function

ETC_C1_NDUFA4 (PF04800 )

Enzyme 22 Signals

1-34

Enzyme 22 Transmembrane Regions

Not Available

Enzyme 22 Essentiality

Not Available

Enzyme 22 GenBank ID Protein

2655053

Enzyme 22 UniProtKB/Swiss-Prot ID

O43181

Enzyme 22 UniProtKB/Swiss-Prot Entry Name

NDUS4_HUMAN Link Image

Enzyme 22 PDB ID

Not Available

Enzyme 22 Cellular Location

Not Available

Enzyme 22 Gene Sequence

>528 bp

ATGGCGGCGGTCTCAATGTCAGTGGTACTGAGGCAGACGTTGTGGCGGAGAAGGGCAGTG
GCTGTAGCTGCCCTTTCCGTTTCCAGGGTTCCGACCAGGTCGTTGAGGACTTCCACATGG
AGATTGGCACAGGACCAGACTCAAGACACACAACTCATAACAGTTGATGAAAAATTGGAT
ATCACTACTTTAACTGGCGTTCCAGAAGAGCATATAAAAACTAGAAAAGTCAGGATCTTT
GTTCCTGCTCGCAATAACATGCAGTCTGGAGTAAACAACACAAAGAAATGGAAGATGGAG
TTTGATACCAGGGAGCGATGGGAAAATCCTTTGATGGGTTGGGCATCAACGGCTGATCCC
TTATCCAACATGGTTCTAACCTTCAGTACTAAAGAAGATGCAGTTTCCTTTGCAGAAAAA
AATGGATGGAGCTATGACATTGAAGAGAGGAAGGTTCCAAAACCCAAGTCCAAGTCTTAT
GGTGCAAACTTTTCTTGGAACAAAAGAACAAGAGTATCCACAAAATAG

Enzyme 22 GenBank Gene ID

AF020351

Enzyme 22 GeneCard ID

NDUFS4

Enzyme 22 GenAtlas ID

NDUFS4

Enzyme 22 HGNC ID

HGNC:7711

Enzyme 22 Chromosome Location

Enzyme 22 Locus

5q11.1

Enzyme 22 SNPs

SNPJam Report Link Image

Enzyme 22 General References

van den Heuvel L, Ruitenbeek W, Smeets R, Gelman-Kohan Z, Elpeleg O, Loeffen J, Trijbels F, Mariman E, de Bruijn D, Smeitink J: Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am J Hum Genet. 1998 Feb;62(2):262-8. [PubMed ]

Enzyme 22 Metabolite References

Not Available

Enzyme 23 [top]

Enzyme 23 ID

5370

Enzyme 23 Name

Ribosyldihydronicotinamide dehydrogenase [quinone]

Enzyme 23 Synonyms

NRH dehydrogenase [quinone] 2
Quinone reductase 2
QR2
NRH:quinone oxidoreductase 2

Enzyme 23 Gene Name

NQO2

Enzyme 23 Protein Sequence

>Ribosyldihydronicotinamide dehydrogenase [quinone]

MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNFEPRATDKDITGTL
SNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRV
LCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFC
GFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ

Enzyme 23 Number of Residues

231

Enzyme 23 Molecular Weight

25953

Enzyme 23 Theoretical pI

6.24

Enzyme 23 GO Classification

Function
NAD(P)H dehydrogenase (quinone) activity catalytic activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 23 General Function

Not Available

Enzyme 23 Specific Function

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis

Enzyme 23 Pathways

Not Available

Enzyme 23 Reactions

Not Available

Enzyme 23 Pfam Domain Function

Flavodoxin_2 (PF02525 )

Enzyme 23 Signals

None

Enzyme 23 Transmembrane Regions

None

Enzyme 23 Essentiality

Not Available

Enzyme 23 GenBank ID Protein

190818

Enzyme 23 UniProtKB/Swiss-Prot ID

P16083

Enzyme 23 UniProtKB/Swiss-Prot Entry Name

NQO2_HUMAN Link Image

Enzyme 23 PDB ID

1SG0

Enzyme 23 PDB File

Show

Enzyme 23 3D Structure

Enzyme 23 Cellular Location

Not Available

Enzyme 23 Gene Sequence

>696 bp

ATGGCAGGTAAGAAAGTACTCATTGTCTATGCACACCAGGAACCCAAGTCTTTCAACGGA
TCCTTGAAGAATGTGGCTGTAGATGAACTGAGCAGGCAGGGCTGCACCGTCACAGTGTCT
GATTTGTATGCCATGAACTTTGAGCCGAGGGCCACAGACAAAGATATCACTGGTACTCTT
TCTAATCCTGAGGTTTTCAATTATGGAGTGGAAACCCACGAAGCCTACAAGCAAAGGTCT
CTGGCTAGCGACATCACTGATGAGCAGAAAAAGGTTCGGGAGGCTGACCTAGTGATATTT
CAGTTCCCGCTGTACTGGTTCAGCGTGCCGGCCATCCTGAAGGGCTGGATGGATAGGGTG
CTGTGCCAGGGCTTTGCCTTTGACATCCCAGGATTCTACGATTCCGGTTTGCTCCAGGGT
AAACTAGCGCTCCTTTCCGTAACCACGGGAGGCACGGCCGAGATGTACACGAAGACAGGA
GTCAATGGAGATTCTCGATACTTCCTGTGGCCACTCCAGCATGGCACATTACACTTCTGT
GGATTTAAAGTCCTTGCCCCTCAGATCAGCTTTGCTCCTGAAATTGCATCCGAAGAAGAA
AGAAAGGGGATGGTGGCTGCGTGGTCCCAGAGGCTGCAGACCATCTGGAAGGAAGAGCCC
ATCCCCTGCACAGCCCACTGGCACTTCGGGCAATAA

Enzyme 23 GenBank Gene ID

J02888

Enzyme 23 GeneCard ID

NQO2

Enzyme 23 GenAtlas ID

NQO2

Enzyme 23 HGNC ID

HGNC:7856

Enzyme 23 Chromosome Location

Enzyme 23 Locus

6pter-q12

Enzyme 23 SNPs

SNPJam Report Link Image

Enzyme 23 General References

Jaiswal AK, Burnett P, Adesnik M, McBride OW: Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6. Biochemistry. 1990 Feb 20;29(7):1899-906. [PubMed ]
Jaiswal AK: Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J Biol Chem. 1994 May 20;269(20):14502-8. [PubMed ]
Wu K, Knox R, Sun XZ, Joseph P, Jaiswal AK, Zhang D, Deng PS, Chen S: Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch Biochem Biophys. 1997 Nov 15;347(2):221-8. [PubMed ]
Zhao Q, Yang XL, Holtzclaw WD, Talalay P: Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase) Proc Natl Acad Sci U S A. 1997 Mar 4;94(5):1669-74. [PubMed ]
Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM: Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry. 1999 Aug 3;38(31):9881-6. [PubMed ]

Enzyme 23 Metabolite References

Not Available

Enzyme 24 [top]

Enzyme 24 ID

5371

Enzyme 24 Name

NADH-ubiquinone oxidoreductase chain 5

Enzyme 24 Synonyms

NADH dehydrogenase subunit 5

Enzyme 24 Gene Name

MT-ND5

Enzyme 24 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 5

MTMHTTMTTLTLTSLIPPILTTLVNPNKKNSYPHYVKSIVASTFIISLFPTTMFMCLDQE
VIISNWHWATTQTTQLSLSFKLDYFSMMFIPVALFVTWSIMEFSLWYMNSDPNINQFFKY
LLIFLITMLILVTANNLFQLFIGWEGVGIMSFLLISWWYARADANTAAIQAILYNRIGDI
GFILALAWFILHSNSWDPQQMALLNANPSLTPLLGLLLAAAGKSAQLGLHPWLPSAMEGP
TPVSALLHSSTMVVAGIFLLIRFHPLAENSPLIQTLTLCLGAITTLFAAVCALTQNDIKK
IVAFSTSSQLGLMMVTIGINQPHLAFLHICTHAFFKAMLFMCSGSIIHNLNNEQDIRKMG
GLLKTMPLTSTSLTIGSLALAGMPFLTGFYSKDHIIETANMSYTNAWALSITLIATSLTS
AYSTRMILLTLTGQPRFPTLTNINENNPTLLNPIKRLAAGSLFAGFLITNNISPASPFQT
TIPLYLKLTALAVTFLGLLTALDLNYLTNKLKMKSPLCTFYFSNMLGFYPSITHRTIPYL
GLLTSQNLPLLLLDLTWLEKLLPKTISQHQISTSIITSTQKGMIKLYFLSFFFPLILTLL
LIT

Enzyme 24 Number of Residues

603

Enzyme 24 Molecular Weight

67027

Enzyme 24 Theoretical pI

9.32

Enzyme 24 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 24 General Function

Energy production and conversion

Enzyme 24 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 24 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 24 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 24 Pfam Domain Function

NADH5_C (PF06455 )
Oxidored_q1 (PF00361 )
Oxidored_q1_N (PF00662 )

Enzyme 24 Signals

1-21

Enzyme 24 Transmembrane Regions

35-57
85-107
120-137
141-160
172-191
211-233
245-267
272-294
301-320
325-347
368-387
407-429
450-472
482-504
583-602

Enzyme 24 Essentiality

Not Available

Enzyme 24 GenBank ID Protein

Not Available

Enzyme 24 UniProtKB/Swiss-Prot ID

P03915

Enzyme 24 UniProtKB/Swiss-Prot Entry Name

NU5M_HUMAN Link Image

Enzyme 24 PDB ID

Not Available

Enzyme 24 Cellular Location

Not Available

Enzyme 24 Gene Sequence

Not Available

Enzyme 24 GenBank Gene ID

J01415

Enzyme 24 GeneCard ID

MT-ND5

Enzyme 24 GenAtlas ID

MT-ND5

Enzyme 24 HGNC ID

HGNC:7461

Enzyme 24 Chromosome Location

Enzyme 24 Locus

Enzyme 24 SNPs

SNPJam Report Link Image

Enzyme 24 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
Maca-Meyer N, Gonzalez AM, Larruga JM, Flores C, Cabrera VM: Major genomic mitochondrial lineages delineate early human expansions. BMC Genet. 2001;2:13. Epub 2001 Aug 13. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Brown WM, Prager EM, Wang A, Wilson AC: Mitochondrial DNA sequences of primates: tempo and mode of evolution. J Mol Evol. 1982;18(4):225-39. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Brown MD, Voljavec AS, Lott MT, Torroni A, Yang CC, Wallace DC: Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics. 1992 Jan;130(1):163-73. [PubMed ]
Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed ]
Howell N, Halvorson S, Burns J, McCullough DA, Paulton J: When does bilateral optic atrophy become Leber hereditary optic neuropathy? Am J Hum Genet. 1993 Oct;53(4):959-63. [PubMed ]
Rieder MJ, Taylor SL, Tobe VO, Nickerson DA: Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 1998 Feb 15;26(4):967-73. [PubMed ]

Enzyme 24 Metabolite References

Not Available

Enzyme 25 [top]

Enzyme 25 ID

5372

Enzyme 25 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial precursor

Enzyme 25 Synonyms

NADH-ubiquinone oxidoreductase 30 kDa subunit
Complex I-30kD
CI-30kD

Enzyme 25 Gene Name

NDUFS3

Enzyme 25 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial precursor

MAAAAVARLWWRGILGASALTRGTGRPSVLLLPVRRESAGADTRPTVRPRNDVAHKQLSA
FGEYVAEILPKYVQQVQVSCFNELEVCIHPDGVIPVLTFLRDHTNAQFKSLVDLTAVDVP
TRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESAVSVFKAANWYEREIWDMFGVFFAN
HPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWE
AFPVYRQPPESLKLEAGDKKPDAK

Enzyme 25 Number of Residues

264

Enzyme 25 Molecular Weight

30242

Enzyme 25 Theoretical pI

7.62

Enzyme 25 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity catalytic activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 25 General Function

Energy production and conversion

Enzyme 25 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 25 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 25 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 25 Pfam Domain Function

Complex1_30kDa (PF00329 )

Enzyme 25 Signals

1-25

Enzyme 25 Transmembrane Regions

Not Available

Enzyme 25 Essentiality

Not Available

Enzyme 25 GenBank ID Protein

3337441

Enzyme 25 UniProtKB/Swiss-Prot ID

O75489

Enzyme 25 UniProtKB/Swiss-Prot Entry Name

NDUS3_HUMAN Link Image

Enzyme 25 PDB ID

Not Available

Enzyme 25 Cellular Location

Not Available

Enzyme 25 Gene Sequence

>795 bp

ATGGCGGCGGCGGCGGTAGCCAGGCTGTGGTGGCGCGGGATCTTGGGGGCCTCGGCGCTG
ACCAGGGGGACTGGGCGACCCTCCGTTCTGTTGCTGCCGGTGAGGCGGGAGAGCGCCGGG
GCCGACACGCGCCCCACTGTCAGACCACGGAATGATGTGGCCCACAAGCAGCTCTCAGCT
TTTGGAGAGTATGTGGCTGAAATCTTGCCCAAGTATGTCCAACAAGTTCAGGTGTCCTGC
TTCAATGAGTTAGAGGTCTGTATCCATCCTGATGGCGTCATCCCAGTGCTGACTTTCCTC
AGGGATCACACCAATGCACAGTTCAAATCTCTGGTTGACTTGACAGCAGTGGACGTCCCA
ACTCGGCAAAACCGTTTTGAGATTGTCTACAACCTGTTGTCTCTGCGCTTCAACTCACGG
ATCCGTGTGAAGACCTACACAGATGAGCTGACGCCCATTGAGTCTGCTGTCTCTGTGTTC
AAGGCAGCCAACTGGTATGAAAGGGAGATCTGGGACATGTTTGGAGTCTTCTTTGCTAAC
CACCCTGATCTAAGAAGGATCCTGACAGATTATGGCTTCGAGGGACATCCTTTCCGGAAA
GACTTTCCTCTATCTGGCTATGTTGAGTTACGTTATGATGATGAAGTGAAGCGGGTGGTG
GCAGAGCCGGTGGAGTTGGCCCAAGAGTTCCGCAAATTTGACCTGAACAGCCCCTGGGAG
GCTTTCCCAGTCTATCGCCAACCCCCGGAGAGTCTCAAGCTTGAAGCCGGAGACAAGAAG
CCTGATGCCAAGTAG

Enzyme 25 GenBank Gene ID

AF067139

Enzyme 25 GeneCard ID

NDUFS3

Enzyme 25 GenAtlas ID

NDUFS3

Enzyme 25 HGNC ID

HGNC:7710

Enzyme 25 Chromosome Location

Enzyme 25 Locus

11p11.11

Enzyme 25 SNPs

SNPJam Report Link Image

Enzyme 25 General References

Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J: cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed. Biochem Biophys Res Commun. 1998 Jun 29;247(3):751-8. [PubMed ]
Procaccio V, Lescuyer P, Bourges I, Beugnot R, Duborjal H, Depetris D, Mousson B, Montfort MF, Smeets H, De Coo R, Issartel JP: Human NDUFS3 gene coding for the 30-kDa subunit of mitochondrial complex I: genomic organization and expression. Mamm Genome. 2000 Sep;11(9):808-10. [PubMed ]
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

Enzyme 25 Metabolite References

Not Available

Enzyme 26 [top]

Enzyme 26 ID

5373

Enzyme 26 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

Enzyme 26 Synonyms

NADH-ubiquinone oxidoreductase 15 kDa subunit
Complex I-15 kDa
CI-15 kDa

Enzyme 26 Gene Name

NDUFS5

Enzyme 26 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

MPFLDIQKRFGLNIDRWLTIQSGEQPYKMAGRCHAFEKEWIECAHGIGYTRAEKECKIEY
DDFVECLLRQKTMRRAGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP

Enzyme 26 Number of Residues

106

Enzyme 26 Molecular Weight

12518

Enzyme 26 Theoretical pI

9.54

Enzyme 26 GO Classification

Not Available

Enzyme 26 General Function

Not Available

Enzyme 26 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 26 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 26 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 26 Pfam Domain Function

Not Available

Enzyme 26 Signals

None

Enzyme 26 Transmembrane Regions

None

Enzyme 26 Essentiality

Not Available

Enzyme 26 GenBank ID Protein

2911482

Enzyme 26 UniProtKB/Swiss-Prot ID

O43920

Enzyme 26 UniProtKB/Swiss-Prot Entry Name

NDUS5_HUMAN Link Image

Enzyme 26 PDB ID

Not Available

Enzyme 26 Cellular Location

Not Available

Enzyme 26 Gene Sequence

>321 bp

ATGCCTTTCTTGGACATCCAGAAAAGGTTCGGCCTTAACATAGATCGATGGTTGACAATC
CAGAGTGGTGAACAGCCCTACAAGATGGCTGGTCGATGCCATGCTTTTGAAAAAGAATGG
ATAGAATGTGCACATGGAATCGGTTATACTCGGGCAGAGAAAGAGTGCAAGATAGAATAT
GATGATTTCGTAGAGTGTTTGCTTCGGCAGAAAACGATGAGACGTGCAGGTACCATCAGG
AAGCAGCGGGATAAGCTGATAAAGGAAGGAAAGTACACCCCTCCACCTCACCACATTGGC
AAGGGGGAGCCTCGGCCCTGA

Enzyme 26 GenBank Gene ID

AF047434

Enzyme 26 GeneCard ID

NDUFS5

Enzyme 26 GenAtlas ID

NDUFS5

Enzyme 26 HGNC ID

HGNC:7712

Enzyme 26 Chromosome Location

Enzyme 26 Locus

1p34.2-p33

Enzyme 26 SNPs

SNPJam Report Link Image

Enzyme 26 General References

Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z: Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8175-80. [PubMed ]
Loeffen J, Smeets R, Smeitink J, Triepels R, Sengers R, Trijbels F, van den Heuvel L: The human NADH: ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA cloning, chromosomal localization, tissue distribution and the absence of mutations in isolated complex I-deficient patients. J Inherit Metab Dis. 1999 Feb;22(1):19-28. [PubMed ]

Enzyme 26 Metabolite References

Not Available

Enzyme 27 [top]

Enzyme 27 ID

5374

Enzyme 27 Name

NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial precursor

Enzyme 27 Synonyms

NADH-ubiquinone oxidoreductase 24 kDa subunit

Enzyme 27 Gene Name

NDUFV2

Enzyme 27 Protein Sequence

>NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial precursor

MFFSAALRARAAGLTAHWGRHVRNLHKTVMQNGAGGALFVHRDTPENNPDTPFDFTPENY
KRIEAIVKNYPEGHKAAAVLPVLDLAQRQNGWLPISAMNKVAEVLQVPPMRVYEVATFYT
MYNRKPVGKYHIQVCTTTPCMLRNSDSILEAIQKKLGIKVGETTPDKLFTLIEVECLGAC
VNAPMVQINDNYYEDLTAKDIEEIIDELKAGKIPKPGPRSGRFSCEPAGGLTSLTEPPKG
PGFGVQAGL

Enzyme 27 Number of Residues

249

Enzyme 27 Molecular Weight

27392

Enzyme 27 Theoretical pI

8.21

Enzyme 27 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 27 General Function

Energy production and conversion

Enzyme 27 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 27 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 27 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 27 Pfam Domain Function

Complex1_24kDa (PF01257 )

Enzyme 27 Signals

1-11

Enzyme 27 Transmembrane Regions

Not Available

Enzyme 27 Essentiality

Not Available

Enzyme 27 GenBank ID Protein

188852

Enzyme 27 UniProtKB/Swiss-Prot ID

P19404

Enzyme 27 UniProtKB/Swiss-Prot Entry Name

NDUV2_HUMAN Link Image

Enzyme 27 PDB ID

Not Available

Enzyme 27 Cellular Location

Not Available

Enzyme 27 Gene Sequence

>750 bp

ATGTTCTTCTCCGCGGCGCTCCGGGCCCGGGCGGCTGGCCTCACCGCCCACTGGGGAAGA
CATGTAAGGAATTTGCATAAGACAGCTATGCAAAATGGAGCTGGAGGAGCTTTATTTGTG
CACAGAGATACTCCTGAGAATAACCCTGATACTCCATTTGATTTCACACCAGAAAACTAT
AAGAGGATAGAGGCAATTGTAAAAAACTATCCAGAAGGCCATAAAGCAGCAGCTGTTCTT
CCAGTCCTGGATTTAGCCCAAAGGCAGAATGGGTGGTTGCCCATCTCTGCTATGAACAAG
GTTGCAGAAGTTTTACAAGTACCTCCAATGAGAGTATATGAAGTAGCAACTTTTTATACA
ATGTATAATCGAAAGCCAGTTGGAAAGTATCACATTCAGGTCTGCACTACTACACCCTGC
ATGCTTCGAAACTCTGACAGCATACTGGAGGCCATTCAGAAAAAGCTTGGAATAAAGGTT
GGGGAGACTACACCTGACAAACTTTTCACTCTTATAGAAGTGGAATGTTTAGGGGCCTGT
GTGAACGCACCAATGGTTCAAATAAATGACAATTACTATGAGGATTTGACAGCTAAGGAT
ATTGAAGAAATTATTGATGAGCTCAAGGCTGGCAAAATCCCAAAACCAGGGCCAAGGAGT
GGACGCTTCTCTTGTGAGCCAGCTGGAGGTCTTACCTCTTTGACTGAACCACCCAAGGGA
CCTGGATTTGGTGTACAAGCAGGCCTTTAA

Enzyme 27 GenBank Gene ID

M22538

Enzyme 27 GeneCard ID

NDUFV2

Enzyme 27 GenAtlas ID

NDUFV2

Enzyme 27 HGNC ID

HGNC:7717

Enzyme 27 Chromosome Location

Enzyme 27 Locus

18p11.31-p11.2

Enzyme 27 SNPs

SNPJam Report Link Image

Enzyme 27 General References

Pilkington SJ, Walker JE: Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit. Biochemistry. 1989 Apr 18;28(8):3257-64. [PubMed ]

Enzyme 27 Metabolite References

Not Available

Enzyme 28 [top]

Enzyme 28 ID

5376

Enzyme 28 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial precursor

Enzyme 28 Synonyms

NADH-ubiquinone oxidoreductase 42 kDa subunit
Complex I-42kD
CI-42kD

Enzyme 28 Gene Name

NDUFA10

Enzyme 28 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial precursor

MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVI
TVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDD
PRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIR
KQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENA
YKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQD
KFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK

Enzyme 28 Number of Residues

355

Enzyme 28 Molecular Weight

40751

Enzyme 28 Theoretical pI

8.68

Enzyme 28 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity nucleotide binding oxidoreductase activity phosphotransferase activity, alcohol group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism physiological process
Component
—

Enzyme 28 General Function

Nucleotide transport and metabolism

Enzyme 28 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 28 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 28 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 28 Pfam Domain Function

dNK (PF01712 )

Enzyme 28 Signals

1-20

Enzyme 28 Transmembrane Regions

Not Available

Enzyme 28 Essentiality

Not Available

Enzyme 28 GenBank ID Protein

4191348

Enzyme 28 UniProtKB/Swiss-Prot ID

O95299

Enzyme 28 UniProtKB/Swiss-Prot Entry Name

NDUAA_HUMAN Link Image

Enzyme 28 PDB ID

Not Available

Enzyme 28 Cellular Location

Not Available

Enzyme 28 Gene Sequence

>1068 bp

ATGGCCTTGCGGCTCCTGAAGCTGGCAGCGACGTCCGCGTCCGCCCGGGTCGTGGCGGCG
GGCGCCCAGCGCGTGAGAGGAATTCATAGCAGTGTGCAGTGCAAGCTGCGCTATGGAATG
TGGCATTTCCTACTTGGGGATAAAGCAAGCAAAAGACTGACAGAACGCAGCAGAGTGATA
ACTGTAGATGGCAATATATGTACTGGAAAAGGCAAACTTGCAAAAGAAATAGCAGAGAAA
CTAGGCTTCAAGCACTTTCCTGAAGCGGGGATTCATTATCCAGACAGTACCACAGGAGAT
GGGAAGCCCCTCGCCACCGACTATAATGGCAACTGTAGTTTGGAGAAATTTTACGATGAT
CCGAGAAGCAATGATGGCAACAGTTACCGCCTGCAGTCCTGGTTGTACAGCAGTCGCCTG
CTGCAGTACTCAGATGCCTTGGAGCACTTGCTGACCACAGGACAAGGTGTTGTGTTGGAG
CGCTCCATCTTCAGTGACTTTGTGTTCCTGGAGGCGATGTACAACCAGGGATTCATCCGA
AAGCAGTGTGTGGACCACTACAACGAGGTGAAGAGCGTCACCATCTGCGATTACCTGCCC
CCCCACCTGGTGATTTACATCGATGTGCCCGTTCCAGAGGTCCAGAGGCGGATTCAGAAG
AAAGGAGATCCACATGAAATGAAGATCACCTCTGCCTATCTACAGGACATTGAGAATGCC
TATAAGAAAACCTTTCTCCCTGAGATGAGTGAAAAATGTGAGGTTTTACAGTATTCTGCA
AGGGAAGCTCAAGATTCAAAAAAGGTGGTAGAGGACATTGAATACCTGAAGTTCGATAAA
GGGCCGTGGCTCAAGCAGGACAATCGCACTTTATACCACCTGCGATTACTGGTTCAGGAT
AAGTTTGAGGTGCTGAATTACACAAGCATTCCTATCTTTCTCCCGGAAGTCACCATTGGA
GCTCATCAGACTGACCGTGTCTTACATCAGTTCAGAGAGCTGCCGGGCCGCAAGTACAGC
CCTGGGTACAACACCGAGGTGGGAGACAAGTGGATCTGGCTGAAGTGA

Enzyme 28 GenBank Gene ID

AF087661

Enzyme 28 GeneCard ID

NDUFA10

Enzyme 28 GenAtlas ID

NDUFA10

Enzyme 28 HGNC ID

HGNC:7684

Enzyme 28 Chromosome Location

Enzyme 28 Locus

2q37.3

Enzyme 28 SNPs

SNPJam Report Link Image

Enzyme 28 General References

Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]

Enzyme 28 Metabolite References

Not Available

Enzyme 29 [top]

Enzyme 29 ID

5377

Enzyme 29 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

Enzyme 29 Synonyms

NADH-ubiquinone oxidoreductase B14 subunit
Complex I-B14
CI-B14

Enzyme 29 Gene Name

NDUFA6

Enzyme 29 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6

MAGSGVRQATSTASTFVKPIFSRDMNEAKRRVRELYRAWYREVPNTVHQFQLDITVKMGR
DKVREMFMKNAHVTDPRVVDLLVIKGKIELEETIKVWKQRTHVMRFFHETEAPRPKDFLS
KFYVGHDP

Enzyme 29 Number of Residues

128

Enzyme 29 Molecular Weight

15137

Enzyme 29 Theoretical pI

10.64

Enzyme 29 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
cell membrane mitochondrial inner membrane organelle inner membrane organelle membrane

Enzyme 29 General Function

Not Available

Enzyme 29 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 29 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 29 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 29 Pfam Domain Function

Complex1_LYR (PF05347 )

Enzyme 29 Signals

None

Enzyme 29 Transmembrane Regions

None

Enzyme 29 Essentiality

Not Available

Enzyme 29 GenBank ID Protein

2909856

Enzyme 29 UniProtKB/Swiss-Prot ID

P56556

Enzyme 29 UniProtKB/Swiss-Prot Entry Name

NDUA6_HUMAN Link Image

Enzyme 29 PDB ID

Not Available

Enzyme 29 Cellular Location

Not Available

Enzyme 29 Gene Sequence

>387 bp

ATGGCGGGGAGCGGCGTCCGCCAAGCTACTTCTACCGCCAGCACCTTCGTGAAGCCCATT
TTCAGTCGGGACATGAACGAGGCCAAGCGGAGGGTGCGCGAGCTCTACCGCGCCTGGTAT
CGGGAGGTGCCGAACACTGTGCACCAATTCCAGCTGGACATCACTGTGAAAATGGGACGG
GATAAAGTCCGAGAAATGTTTATGAAGAATGCCCATGTCACAGACCCCAGGGTGGTTGAT
CTTCTGGTCATTAAGGGAAAGATCGAACTGGAAGAAACAATTAAAGTATGGAAGCAGCGG
ACACATGTTATGCGGTTCTTCCATGAAACAGAAGCGCCAAGGCCAAAGGATTTCCTATCC
AAGTTCTATGTTGGCCACGATCCATGA

Enzyme 29 GenBank Gene ID

AF047182

Enzyme 29 GeneCard ID

NDUFA6

Enzyme 29 GenAtlas ID

NDUFA6

Enzyme 29 HGNC ID

HGNC:7690

Enzyme 29 Chromosome Location

Enzyme 29 Locus

22q13.2-q13.31

Enzyme 29 SNPs

SNPJam Report Link Image

Enzyme 29 General References

Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed ]
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

Enzyme 29 Metabolite References

Not Available

Enzyme 30 [top]

Enzyme 30 ID

5381

Enzyme 30 Name

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

Enzyme 30 Synonyms

NADH-ubiquinone oxidoreductase B15 subunit
Complex I-B15
CI-B15

Enzyme 30 Gene Name

NDUFB4

Enzyme 30 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4

MSFPKYKPSSLRTLPETLDPAEYNISPETRRAQAERLAIRAQLKREYLLQYNDPNRRGLI
ENPALLRWAYARTINVYPNFRPTPKNSLMGALCGFGPLIFIYYIIKTERDRKEKLIQEGK
LDRTFHLSY

Enzyme 30 Number of Residues

129

Enzyme 30 Molecular Weight

15209

Enzyme 30 Theoretical pI

10.24

Enzyme 30 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
intracellular membrane-bound organelle membrane-bound organelle mitochondrion organelle

Enzyme 30 General Function

Not Available

Enzyme 30 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 30 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 30 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 30 Pfam Domain Function

NDUF_B4 (PF07225 )

Enzyme 30 Signals

None

Enzyme 30 Transmembrane Regions

88-105

Enzyme 30 Essentiality

Not Available

Enzyme 30 GenBank ID Protein

4164446

Enzyme 30 UniProtKB/Swiss-Prot ID

O95168

Enzyme 30 UniProtKB/Swiss-Prot Entry Name

NDUB4_HUMAN Link Image

Enzyme 30 PDB ID

Not Available

Enzyme 30 Cellular Location

Not Available

Enzyme 30 Gene Sequence

>390 bp

ATGTCGTTCCCAAAGTATAAGCCGTCGAGCCTGCGCACTCTGCCTGAGACCCTCGACCCA
GCCGAATACAACATATCTCCGGAAACCCGGCGGGCGCAAGCCGAGCGGTTGGCCATAAGA
GCCCAGCTGAAACGAGAGTACCTGCTTCAGTACAACGATCCCAACCGCCGAGGGCTCATC
GAAAATCCTGCCTTGCTTCGTTGGGCCTATGCAAGAACAATAAATGTCTATCCTAATTTC
AGACCCACTCCTAAAAACTCACTCATGGGAGCTCTGTGTGGATTTGGGCCCCTCATCTTC
ATTTATTATATTATCAAAACTGAGAGGGATAGGAAAGAAAAACTTATCCAGGAAGGAAAA
TTGGATCGAACATTTCACCTCTCATATTAA

Enzyme 30 GenBank Gene ID

AF044957

Enzyme 30 GeneCard ID

NDUFB4

Enzyme 30 GenAtlas ID

NDUFB4

Enzyme 30 HGNC ID

HGNC:7699

Enzyme 30 Chromosome Location

Enzyme 30 Locus

3q13.33

Enzyme 30 SNPs

SNPJam Report Link Image

Enzyme 30 General References

Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]

Enzyme 30 Metabolite References

Not Available

Enzyme 31 [top]

Enzyme 31 ID

5384

Enzyme 31 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial precursor

Enzyme 31 Synonyms

NADH-ubiquinone oxidoreductase 23 kDa subunit
Complex I-23kD
CI-23kD
TYKY subunit

Enzyme 31 Gene Name

NDUFS8

Enzyme 31 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial precursor

MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLL
WTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAI
CPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEE
LLYNKEKLLNNGDKWEAEIAANIQADYLYR

Enzyme 31 Number of Residues

210

Enzyme 31 Molecular Weight

23705

Enzyme 31 Theoretical pI

6.27

Enzyme 31 GO Classification

Function
binding catalytic activity cation binding electron transporter activity ion binding iron ion binding oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH transition metal ion binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 31 General Function

Energy production and conversion

Enzyme 31 Specific Function

May donate electrons to ubiquinone

Enzyme 31 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 31 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 31 Pfam Domain Function

Fer4 (PF00037 )

Enzyme 31 Signals

1-19

Enzyme 31 Transmembrane Regions

Not Available

Enzyme 31 Essentiality

Not Available

Enzyme 31 GenBank ID Protein

1935056

Enzyme 31 UniProtKB/Swiss-Prot ID

O00217

Enzyme 31 UniProtKB/Swiss-Prot Entry Name

NDUS8_HUMAN Link Image

Enzyme 31 PDB ID

Not Available

Enzyme 31 Cellular Location

Not Available

Enzyme 31 Gene Sequence

>633 bp

ATGCGCTGCCTGACCACGCCTATGCTGCTGCGGGCCCTGGCCCAGGCTGCACGTGCAGGA
CCTCCTGGTGGCCGGAGCCTCCACAGCAGTGCAGTGGCAGCCACCTACAAGTATGTGAAC
ATGCAGGATCCCGAGATGGACATGAAGTCAGTGACTGACCGGGCAGCCCGCACCCTGCTG
TGGACTGAGCTCTTCCGAGGCCTGGGCATGACCCTGAGCTACCTGTTCCGGGAACCGGCC
ACCATCAACTACCCGTTCGAGAAGGGCCCGCTGAGCCCTCGCTTCCGTGGGGAGCATGCG
CTGCGCCGGTACCCATCCGGGGAGGAGCGTTGCATTGCCTGCAAGCTCTGCGAGGCCATC
TGCCCCGCCCAGGCCATCACCATCGAGGCTGAGCCAAGAGCTGATGGCAGCCGCCGGACC
ACCCGCTATGACATCGACATGACCAAGTGCATCTACTGCGGCTTCTGCCAGGAGGCCTGT
CCCGTGGATGCCATCGTCGAGGGCCCCAACTTTGAGTTCTCCACGGAGACCCATGAGGAG
CTGCTGTACAACAAGGAGAAGTTGCTCAACAACGGGGACAAGTGGGAGGCCGAGATCGCC
GCCAACATCCAGGCTGACTACTTGTATCGGTGA

Enzyme 31 GenBank Gene ID

U65579

Enzyme 31 GeneCard ID

NDUFS8

Enzyme 31 GenAtlas ID

NDUFS8

Enzyme 31 HGNC ID

HGNC:7715

Enzyme 31 Chromosome Location

Enzyme 31 Locus

11q13

Enzyme 31 SNPs

SNPJam Report Link Image

Enzyme 31 General References

Procaccio V, Depetris D, Soularue P, Mattei MG, Lunardi J, Issartel JP: cDNA sequence and chromosomal localization of the NDUFS8 human gene coding for the 23 kDa subunit of the mitochondrial complex I. Biochim Biophys Acta. 1997 Mar 20;1351(1-2):37-41. [PubMed ]
de Sury R, Martinez P, Procaccio V, Lunardi J, Issartel JP: Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase. Gene. 1998 Jul 17;215(1):1-10. [PubMed ]
Loeffen J, Smeitink J, Triepels R, Smeets R, Schuelke M, Sengers R, Trijbels F, Hamel B, Mullaart R, van den Heuvel L: The first nuclear-encoded complex I mutation in a patient with Leigh syndrome. Am J Hum Genet. 1998 Dec;63(6):1598-608. [PubMed ]

Enzyme 31 Metabolite References

Not Available

Enzyme 32 [top]

Enzyme 32 ID

5386

Enzyme 32 Name

NADH-ubiquinone oxidoreductase chain 2

Enzyme 32 Synonyms

NADH dehydrogenase subunit 2

Enzyme 32 Gene Name

MT-ND2

Enzyme 32 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 2

MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYF
LTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQ
GTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILA
YSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWL
TPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYST
SITLLPMSNNVKMKWQFEHTKPTPFLPTLIALTTLLLPISPFMLMIL

Enzyme 32 Number of Residues

347

Enzyme 32 Molecular Weight

38962

Enzyme 32 Theoretical pI

10.30

Enzyme 32 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 32 General Function

Energy production and conversion

Enzyme 32 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 32 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 32 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 32 Pfam Domain Function

NADH_dehy_S2_C (PF06444 )
Oxidored_q1 (PF00361 )

Enzyme 32 Signals

1-33

Enzyme 32 Transmembrane Regions

59-81
93-115
149-171
178-195
200-219
239-261
276-298
324-346

Enzyme 32 Essentiality

Not Available

Enzyme 32 GenBank ID Protein

Not Available

Enzyme 32 UniProtKB/Swiss-Prot ID

P03891

Enzyme 32 UniProtKB/Swiss-Prot Entry Name

NU2M_HUMAN Link Image

Enzyme 32 PDB ID

Not Available

Enzyme 32 Cellular Location

Not Available

Enzyme 32 Gene Sequence

Not Available

Enzyme 32 GenBank Gene ID

J01415

Enzyme 32 GeneCard ID

MT-ND2

Enzyme 32 GenAtlas ID

MT-ND2

Enzyme 32 HGNC ID

HGNC:7456

Enzyme 32 Chromosome Location

Enzyme 32 Locus

Enzyme 32 SNPs

SNPJam Report Link Image

Enzyme 32 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Sanger F, Coulson AR, Barrell BG, Smith AJ, Roe BA: Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J Mol Biol. 1980 Oct 25;143(2):161-78. [PubMed ]
Wise CA, Sraml M, Easteal S: Departure from neutrality at the mitochondrial NADH dehydrogenase subunit 2 gene in humans, but not in chimpanzees. Genetics. 1998 Jan;148(1):409-21. [PubMed ]
Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Johns DR, Berman J: Alternative, simultaneous complex I mitochondrial DNA mutations in Leber's hereditary optic neuropathy. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1324-30. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Brown MD, Voljavec AS, Lott MT, Torroni A, Yang CC, Wallace DC: Mitochondrial DNA complex I and III mutations associated with Leber's hereditary optic neuropathy. Genetics. 1992 Jan;130(1):163-73. [PubMed ]
Lin FH, Lin R, Wisniewski HM, Hwang YW, Grundke-Iqbal I, Healy-Louie G, Iqbal K: Detection of point mutations in codon 331 of mitochondrial NADH dehydrogenase subunit 2 in Alzheimer's brains. Biochem Biophys Res Commun. 1992 Jan 15;182(1):238-46. [PubMed ]
Rieder MJ, Taylor SL, Tobe VO, Nickerson DA: Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. Nucleic Acids Res. 1998 Feb 15;26(4):967-73. [PubMed ]

Enzyme 32 Metabolite References

Not Available

Enzyme 33 [top]

Enzyme 33 ID

5388

Enzyme 33 Name

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor

Enzyme 33 Synonyms

P5C dehydrogenase
Aldehyde dehydrogenase 4A1

Enzyme 33 Gene Name

ALDH4A1

Enzyme 33 Protein Sequence

>Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor

MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ

Enzyme 33 Number of Residues

563

Enzyme 33 Molecular Weight

61720

Enzyme 33 Theoretical pI

8.20

Enzyme 33 GO Classification

Function
1-pyrroline-5-carboxylate dehydrogenase activity catalytic activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
amino acid and derivative metabolism amino acid metabolism cellular metabolism glutamine family amino acid metabolism metabolism physiological process proline biosynthesis proline metabolism
Component
membrane-enclosed lumen mitochondrial lumen mitochondrial matrix organelle lumen

Enzyme 33 General Function

Energy production and conversion

Enzyme 33 Specific Function

Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes

Enzyme 33 Pathways

Arginine and Proline Metabolism (map00330 )
Glutamate Metabolism (map00251 )

Enzyme 33 Reactions

1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH + H+

Enzyme 33 Pfam Domain Function

Aldedh (PF00171 )

Enzyme 33 Signals

1-19

Enzyme 33 Transmembrane Regions

Not Available

Enzyme 33 Essentiality

Not Available

Enzyme 33 GenBank ID Protein

1353250

Enzyme 33 UniProtKB/Swiss-Prot ID

P30038

Enzyme 33 UniProtKB/Swiss-Prot Entry Name

AL4A1_HUMAN Link Image

Enzyme 33 PDB ID

Not Available

Enzyme 33 Cellular Location

Not Available

Enzyme 33 Gene Sequence

>1692 bp

ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGATGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATGGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAAAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCGCGCTCCTCGCCCAGCCTCACCATCCTGGCTGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAC
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA

Enzyme 33 GenBank Gene ID

U24267

Enzyme 33 GeneCard ID

ALDH4A1

Enzyme 33 GenAtlas ID

ALDH4A1

Enzyme 33 HGNC ID

HGNC:406

Enzyme 33 Chromosome Location

Enzyme 33 Locus

1p36

Enzyme 33 SNPs

SNPJam Report Link Image

Enzyme 33 General References

Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed ]
Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed ]
Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed ]

Enzyme 33 Metabolite References

Not Available

Enzyme 34 [top]

Enzyme 34 ID

5389

Enzyme 34 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

Enzyme 34 Synonyms

NADH-ubiquinone oxidoreductase subunit B14.5a
Complex I-B14.5a
CI-B14.5a

Enzyme 34 Gene Name

NDUFA7

Enzyme 34 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7

MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGR
RESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL

Enzyme 34 Number of Residues

113

Enzyme 34 Molecular Weight

12552

Enzyme 34 Theoretical pI

10.80

Enzyme 34 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
cell membrane mitochondrial inner membrane organelle inner membrane organelle membrane

Enzyme 34 General Function

Not Available

Enzyme 34 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 34 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 34 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 34 Pfam Domain Function

CI-B14_5a (PF07347 )

Enzyme 34 Signals

None

Enzyme 34 Transmembrane Regions

None

Enzyme 34 Essentiality

Not Available

Enzyme 34 GenBank ID Protein

4164452

Enzyme 34 UniProtKB/Swiss-Prot ID

O95182

Enzyme 34 UniProtKB/Swiss-Prot Entry Name

NDUA7_HUMAN Link Image

Enzyme 34 PDB ID

Not Available

Enzyme 34 Cellular Location

Not Available

Enzyme 34 Gene Sequence

>342 bp

ATGGCGTCCGCCACCCGTCTCATCCAGCGGCTGCGGAACTGGGCGTCCGGGCATGACCTG
CAGGGGAAGCTGCAGCTACGCTACCAGGAGATCTCCAAGCGAACTCAGCCTCCTCCCAAG
CTCCCTGTGGGTCCTAGCCACAAGCTCTCCAACAATTACTATTGCACTCGCGATGGCCGC
CGGGAATCTGTGCCCCCTTCCATCATCATGTCGTCGCAGAAGGCGCTGGTGTCAGGCAAG
CCAGCAGAGAGCTCTGCTGTAGCTGCCACTGAGAAGAAGGCGGTGACTCCAGCTCCTCCC
ATAAAGAGGTGGGAGCTGTCCTCGGACCAGCCTTACCTGTGA

Enzyme 34 GenBank Gene ID

AF050637

Enzyme 34 GeneCard ID

NDUFA7

Enzyme 34 GenAtlas ID

NDUFA7

Enzyme 34 HGNC ID

HGNC:7691

Enzyme 34 Chromosome Location

Enzyme 34 Locus

19p13.2

Enzyme 34 SNPs

SNPJam Report Link Image

Enzyme 34 General References

Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

Enzyme 34 Metabolite References

Not Available

Enzyme 35 [top]

Enzyme 35 ID

5391

Enzyme 35 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

Enzyme 35 Synonyms

NADH-ubiquinone oxidoreductase B8 subunit
Complex I-B8
CI-B8

Enzyme 35 Gene Name

NDUFA2

Enzyme 35 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSD
VQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA

Enzyme 35 Number of Residues

Enzyme 35 Molecular Weight

10922

Enzyme 35 Theoretical pI

10.11

Enzyme 35 GO Classification

Not Available

Enzyme 35 General Function

Not Available

Enzyme 35 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 35 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 35 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 35 Pfam Domain Function

L51_S25_CI-B8 (PF05047 )

Enzyme 35 Signals

None

Enzyme 35 Transmembrane Regions

None

Enzyme 35 Essentiality

Not Available

Enzyme 35 GenBank ID Protein

2909862

Enzyme 35 UniProtKB/Swiss-Prot ID

O43678

Enzyme 35 UniProtKB/Swiss-Prot Entry Name

NDUA2_HUMAN Link Image

Enzyme 35 PDB ID

1S3A

Enzyme 35 PDB File

Show

Enzyme 35 3D Structure

Enzyme 35 Cellular Location

Not Available

Enzyme 35 Gene Sequence

>300 bp

ATGGCGGCGGCCGCAGCAAGTCGAGGAGTCGGGGCAAAGCTGGGCCTGCGTGAGATTCGC
ATCCACTTATGTCAGCGCTCGCCCGGCAGCCAGGGCGTCAGGGACTTCATTGAGAAACGC
TACGTGGAGCTGAAGAAGGCGAATCCCGACCTACCCATCCTAATCCGCGAATGCTCCGAT
GTGCAGCCCAAGCTCTGGGCCCGCTACGCATTTGGCCAAGAGACGAATGTCCCTTTGAAC
AACTTCAGTGCTGATCAGGTAACCAGAGCCCTGGAGAACGTTCTAAGTGGTAAAGCCTGA

Enzyme 35 GenBank Gene ID

AF047185

Enzyme 35 GeneCard ID

NDUFA2

Enzyme 35 GenAtlas ID

NDUFA2

Enzyme 35 HGNC ID

HGNC:7685

Enzyme 35 Chromosome Location

Enzyme 35 Locus

5q31

Enzyme 35 SNPs

SNPJam Report Link Image

Enzyme 35 General References

Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]

Enzyme 35 Metabolite References

Not Available

Enzyme 36 [top]

Enzyme 36 ID

5394

Enzyme 36 Name

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor

Enzyme 36 Synonyms

Complex I-75kD
CI-75kD

Enzyme 36 Gene Name

NDUFS1

Enzyme 36 Protein Sequence

>NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial precursor

MLRIPVRKALVGLSKSPKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQI
PRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFL
LANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCT
RCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTA
RPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQ
RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGKDVAAIAGGLVDAEALVALKDLLNR
VDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRK
SWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSA
LQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKN
PPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTE
GRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIE
GANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQA
VEEPSIC

Enzyme 36 Number of Residues

727

Enzyme 36 Molecular Weight

79468

Enzyme 36 Theoretical pI

6.11

Enzyme 36 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity binding catalytic activity cation binding cation transporter activity electron transporter activity hydrogen ion transporter activity ion binding ion transporter activity iron ion binding monovalent inorganic cation transporter activity oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH transition metal ion binding transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 36 General Function

Energy production and conversion

Enzyme 36 Specific Function

This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized

Enzyme 36 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 36 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 36 Pfam Domain Function

DUF1982 (PF09326 )
Fer2 (PF00111 )
Molybdopterin (PF00384 )

Enzyme 36 Signals

None

Enzyme 36 Transmembrane Regions

None

Enzyme 36 Essentiality

Not Available

Enzyme 36 GenBank ID Protein

38079

Enzyme 36 UniProtKB/Swiss-Prot ID

P28331

Enzyme 36 UniProtKB/Swiss-Prot Entry Name

NDUS1_HUMAN Link Image

Enzyme 36 PDB ID

Not Available

Enzyme 36 Cellular Location

Not Available

Enzyme 36 Gene Sequence

>2184 bp

ATGTTAAGGATACCTGTAAGAAGGGCCTTAGTAGGCCTTTCTAAGTCTCCTAAAGGATGT
GTTCGAACAACTGCCACAGCAGCAAGCAACTTGATTGAAGTATTTGTTGATGGTCAGTCT
GTCATGGTGGAACCGGGAACGACCGTCCTCCAAGCTTGTGAGAAGGTTGGCATGCAGATC
CCTCGATTCTGTTATCATGAAAGGTTGTCTGTTGCTGGAAACTGCAGGATGTGCCTTGTT
GAAATTGAGAAAGCCCCTAAGGTTGTAGCTGCTTGTGCCATGCCAGTAATGAAGGGTTGG
AATATCCTAACAAACTCAGAAAAATCCAAAAAGGCCAGGGAAGGTGTGATGGAGTTCTTA
TTAGCAAATCACCCATTGGACTGTCCTATTTGTGACCAGGGAGGTGAATGTGATCTGCAG
GACCAGTCCATGATGTTTGGAAATGATAGGAGCCGATTTTTAGAGGGGAAGCGTGCTGTG
GAAGACAAGAACATTGGGCCATTGGTAAAGACCATCATGACAAGATGTATACAGTGTACT
CGCTGCATCAGGTTTGCAAGTGAGATTGCAGGAGTAGATGATTTGGGAACAACAGGCAGA
GGAAATGATATGCAAGTTGGCACATACATTGAAAAGATGTTCATGTCTGAACTGTCTGGG
AATATCATTGATATCTGCCCTGTAGGTGCCCTAACCTCTAAGCCCTATGCCTTTACTGCC
CGGCCTTGGGAAACAAGAAAGACAGAATCCATTGATGTAATGGATGCGGTTGGAAGTAAT
ATTGTGGTTAGCACAAGAACTGGAGAAGTGATGAGGATTTTGCCACGTATGCATGAGGAC
ATCAATGAAGAGTGGATCTCTGATAAAACCAGATTTGCCTATGATGGGCTAAAACGTCAA
AGACTTACCGAGCCAATGGTCAGAAATGAAAAAGGGCTTTTAACCTATACTTCTTGGGAG
GATGCTCTCTCTCGCGTAGCTGGAATGTTGCAGAGTTTTCAAGGCAAAGATGTGGCAGCA
ATTGCAGGTGGCTTGGTGGATGCTGAAGCCCTGGTAGCTCTCAAAGATTTGCTTAATAGA
GTGGACTCTGACACCTTATGCACTGAAGAGGTCTTCCCCACTGCAGGAGCTGGCACAGAT
TTGCGTTCCAATTATCTTCTTAATACTACAATTGCTGGTGTGGAAGAGGCAGATGTTGTT
CTTCTGGTTGGTACAAACCCACGTTTTGAGGCACCACTGTTTAATGCATGGATTCGAAAG
AGCTGGCTGCATAATGACTTAAAAGTGGCCCTTATAGGCAGTCCAGTGGACCTCACTTAC
ACATATGACCACCTGGGAGACTCCCCCAAAATTCTTCAAGACATTGCTTCGGGAAGCCAT
CCATTTAGCCAGGTCCTAAAGGAAGCTAAAAAACCAATGGTGGTTTTAGGCAGTTCTGCA
CTCCAAAGAAATGATGGAGCAGCAATTCTTGCAGCTGTTTCTAGCATTGCACAAAAGATT
CGGATGACTAGTGGTGTTACTGGTGATTGGAAAGTTATGAATATCCTTCATAGGATTGCA
AGTCAAGTAGCTGCTTTGGACCTTGGCTATAAGCCTGGGGTGGAAGCAATTCGGAAGAAC
CCTCCCAAGGTGCTGTTTCTCCTGGGAGCAGATGGAGGTTGTATCACACGACAGGATTTG
CCAAAGGATTGTTTCATTATTTATCAAGGACATCATGGTGATGTTGGGGCTCCCATAGCT
GATGTTATTCTCCCAGGAGCTGCTTACACAGAGAAGTCTGCTACATATGTCAACACTGAG
GGTAGAGCTCAGCAGACTAAGGTAGCAGTGACACCTCCTGGCTTGGCAAGAGAAGACTGG
AAAATTATAAGAGCACTCTCTGAGATTGCTGGAATGACTCTTCCATATGATACTCTGGAT
CAAGTAAGGAACAGATTGGAAGAATTCTCTCCTAATCTTGTTCGATATGATGATATTGAA
GGGGCTAATTACTTCCAGCAAGCAAATGAGCTCTCAAAGCTAGTGAACCAGCAGCTTCTT
GCTGACCCACTTGTTCCACCTCAGCTAACTCTAAAAGACTTCTACATGACAGATTCGATT
AGCAGAGCCTCACAGACAATGGCCAAATGTGTCAAAGCTGTCACAGAGGGTGCCCAGGCA
GTAGAGGAACCATCCATATGCTGA

Enzyme 36 GenBank Gene ID

X61100

Enzyme 36 GeneCard ID

NDUFS1

Enzyme 36 GenAtlas ID

NDUFS1

Enzyme 36 HGNC ID

HGNC:7707

Enzyme 36 Chromosome Location

Enzyme 36 Locus

2q33-q34

Enzyme 36 SNPs

SNPJam Report Link Image

Enzyme 36 General References

Chow W, Ragan I, Robinson BH: Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase. Eur J Biochem. 1991 Nov 1;201(3):547-50. [PubMed ]

Enzyme 36 Metabolite References

Not Available

Enzyme 37 [top]

Enzyme 37 ID

5395

Enzyme 37 Name

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial precursor

Enzyme 37 Synonyms

NADH-ubiquinone oxidoreductase SGDH subunit
Complex I-SGDH
CI-SGDH

Enzyme 37 Gene Name

NDUFB5

Enzyme 37 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial precursor

MAAMSLLRRVSVTAVAALSGRPLGTRLGFGGFLTRGFPKAAAPVRHSGDHGKRLFVIRPS
RFYDRRFLKLLRFYIALTGIPVAIFITLVNVFIGQAELAEIPEGYVPEHWEYYKHPISRW
IARNFYDSPEKIYERTMAVLQIEAEKAELRVKELEVRKLMHVRGDGPWYYYETIDKELID
HSPKATPDN

Enzyme 37 Number of Residues

189

Enzyme 37 Molecular Weight

21751

Enzyme 37 Theoretical pI

10.02

Enzyme 37 GO Classification

Not Available

Enzyme 37 General Function

Not Available

Enzyme 37 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 37 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 37 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 37 Pfam Domain Function

Not Available

Enzyme 37 Signals

1-16

Enzyme 37 Transmembrane Regions

70-92

Enzyme 37 Essentiality

Not Available

Enzyme 37 GenBank ID Protein

2909854

Enzyme 37 UniProtKB/Swiss-Prot ID

O43674

Enzyme 37 UniProtKB/Swiss-Prot Entry Name

NDUB5_HUMAN Link Image

Enzyme 37 PDB ID

Not Available

Enzyme 37 Cellular Location

Not Available

Enzyme 37 Gene Sequence

>570 bp

ATGGCGGCCATGAGTTTGTTGCGGCGGGTTTCGGTTACTGCGGTGGCAGCTCTGTCTGGC
CGGCCCCTTGGCACTCGCCTCGGATTTGGGGGCTTCCTCACTCGTGGCTTTCCGAAGGCT
GCTGCTCCTGTTCGACACAGTGGAGACCATGGGAAAAGACTATTTGTCATCAGACCTTCT
AGATTCTATGACAGGCGTTTTTTGAAGTTATTGAGATTCTACATTGCATTGACTGGGATT
CCAGTAGCAATTTTCATAACTCTGGTGAATGTATTCATTGGTCAAGCTGAACTAGCAGAA
ATTCCAGAAGGCTATGTCCCAGAACACTGGGAATATTATAAGCATCCCATATCAAGATGG
ATTGCCCGTAATTTCTATGATAGTCCTGAAAAGATATATGAAAGAACAATGGCCGTCCTT
CAGATTGAAGCTGAAAAGGCTGAATTACGGGTAAAGGAGCTGGAAGTGCGAAAATTGATG
CATGTGAGAGGAGATGGACCCTGGTATTACTATGAGACAATTGACAAGGAACTTATTGAT
CATTCTCCGAAAGCAACTCCTGACAATTAA

Enzyme 37 GenBank Gene ID

AF047181

Enzyme 37 GeneCard ID

NDUFB5

Enzyme 37 GenAtlas ID

NDUFB5

Enzyme 37 HGNC ID

HGNC:7700

Enzyme 37 Chromosome Location

Enzyme 37 Locus

3q26.33

Enzyme 37 SNPs

SNPJam Report Link Image

Enzyme 37 General References

Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed ]

Enzyme 37 Metabolite References

Not Available

Enzyme 38 [top]

Enzyme 38 ID

5402

Enzyme 38 Name

NADH dehydrogenase [ubiquinone] 1 subunit C2

Enzyme 38 Synonyms

NADH-ubiquinone oxidoreductase subunit B14.5b
Complex I-B14.5b
CI-B14.5b

Enzyme 38 Gene Name

NDUFC2

Enzyme 38 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 subunit C2

MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQ
LLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEDKKTYGEIFEKFHPIR

Enzyme 38 Number of Residues

119

Enzyme 38 Molecular Weight

14188

Enzyme 38 Theoretical pI

9.27

Enzyme 38 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
cell membrane mitochondrial inner membrane organelle inner membrane organelle membrane

Enzyme 38 General Function

Not Available

Enzyme 38 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 38 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 38 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 38 Pfam Domain Function

NDUF_C2 (PF06374 )

Enzyme 38 Signals

None

Enzyme 38 Transmembrane Regions

56-75

Enzyme 38 Essentiality

Not Available

Enzyme 38 GenBank ID Protein

4191346

Enzyme 38 UniProtKB/Swiss-Prot ID

O95298

Enzyme 38 UniProtKB/Swiss-Prot Entry Name

NDUC2_HUMAN Link Image

Enzyme 38 PDB ID

Not Available

Enzyme 38 Cellular Location

Not Available

Enzyme 38 Gene Sequence

>360 bp

ATGATCGCACGGCGGAACCCAGAACCCTTACGGTTTCTGCCGGATGAGGCCCGGAGCCTG
CCCCCGCCCAAGCTGACCGACCCGCGGCTCCTCTACATCGGCTTCTTGGGCTACTGCTCC
GGCCTGATTGATAACCTGATCCGGCGGAGGCCGATCGCGACGGCTGGTTTGCATCGCCAG
CTTCTATATATTACGGCCTTTTTTTTTGCTGGATATTATCTTGTAAAACGTGAAGACTAC
CTGTATGCTGTGAGGGACCGTGAAATGTTTGGATATATGAAATTACATCCAGAGGATTTT
CCTGAAGAAGATAAGAAAACATATGGTGAAATTTTTGAAAAATTCCATCCAATACGTTGA

Enzyme 38 GenBank Gene ID

AF087659

Enzyme 38 GeneCard ID

NDUFC2

Enzyme 38 GenAtlas ID

NDUFC2

Enzyme 38 HGNC ID

HGNC:7706

Enzyme 38 Chromosome Location

Enzyme 38 Locus

11q14.1

Enzyme 38 SNPs

SNPJam Report Link Image

Enzyme 38 General References

Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]

Enzyme 38 Metabolite References

Not Available

Enzyme 39 [top]

Enzyme 39 ID

5404

Enzyme 39 Name

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

Enzyme 39 Synonyms

NADH-ubiquinone oxidoreductase B12 subunit
Complex I-B12
CI-B12

Enzyme 39 Gene Name

NDUFB3

Enzyme 39 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3

MAHEHGHEHGHHKMELPDYRQWKIEGTPLETIQKKLAAKGLRDPWGRNEAWRYMGGFAKS
VSFSDVFFKGFKWGFAAFVVAVGAEYYLESLNKDKKHH

Enzyme 39 Number of Residues

Enzyme 39 Molecular Weight

11402

Enzyme 39 Theoretical pI

9.73

Enzyme 39 GO Classification

Not Available

Enzyme 39 General Function

Not Available

Enzyme 39 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 39 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 39 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 39 Pfam Domain Function

NDUF_B12 (PF08122 )

Enzyme 39 Signals

None

Enzyme 39 Transmembrane Regions

66-88

Enzyme 39 Essentiality

Not Available

Enzyme 39 GenBank ID Protein

2909858

Enzyme 39 UniProtKB/Swiss-Prot ID

O43676

Enzyme 39 UniProtKB/Swiss-Prot Entry Name

NDUB3_HUMAN Link Image

Enzyme 39 PDB ID

Not Available

Enzyme 39 Cellular Location

Not Available

Enzyme 39 Gene Sequence

>297 bp

ATGGCCCATGAACATGGACATGAGCATGGACATCATAAAATGGAACTTCCAGATTATAGA
CAATGGAAGATAGAAGGGACACCATTAGAAACTATCCAGAAGAAGCTGGCTGCAAAAGGG
CTAAGGGATCCATGGGGCCGCAATGAAGCTTGGAGATACATGGGTGGCTTTGCAAAGAGT
GTTTCCTTTTCTGATGTATTCTTTAAAGGATTCAAATGGGGATTTGCTGCATTTGTGGTA
GCTGTAGGAGCTGAATATTACCTGGAGTCCCTGAATAAAGATAAGAAGCATCACTGA

Enzyme 39 GenBank Gene ID

AF047183

Enzyme 39 GeneCard ID

NDUFB3

Enzyme 39 GenAtlas ID

NDUFB3

Enzyme 39 HGNC ID

HGNC:7698

Enzyme 39 Chromosome Location

Enzyme 39 Locus

2q31.3

Enzyme 39 SNPs

SNPJam Report Link Image

Enzyme 39 General References

Ton C, Hwang DM, Dempsey AA, Liew CC: Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. Biochem Biophys Res Commun. 1997 Dec 18;241(2):589-94. [PubMed ]
Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA: cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. Biochem Biophys Res Commun. 1998 Dec 18;253(2):415-22. [PubMed ]

Enzyme 39 Metabolite References

Not Available

Enzyme 40 [top]

Enzyme 40 ID

5405

Enzyme 40 Name

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

Enzyme 40 Synonyms

NADH-ubiquinone oxidoreductase B18 subunit
Complex I-B18
CI-B18
Cell adhesion protein SQM1

Enzyme 40 Gene Name

NDUFB7

Enzyme 40 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7

MGAHLVRRYLGDASVEPDPLQMPTFPPDYGFPERKEREMVATQQEMMDAQLRLQLRDYCA
HHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEFERERRLLQRKKRREKKAA
ELAKGQGPGEVDPKVAL

Enzyme 40 Number of Residues

137

Enzyme 40 Molecular Weight

16402

Enzyme 40 Theoretical pI

9.21

Enzyme 40 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase activity cation transporter activity electron transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
intracellular membrane-bound organelle membrane-bound organelle mitochondrion organelle

Enzyme 40 General Function

Not Available

Enzyme 40 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 40 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 40 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 40 Pfam Domain Function

NDUF_B7 (PF05676 )

Enzyme 40 Signals

None

Enzyme 40 Transmembrane Regions

None

Enzyme 40 Essentiality

Not Available

Enzyme 40 GenBank ID Protein

180233

Enzyme 40 UniProtKB/Swiss-Prot ID

P17568

Enzyme 40 UniProtKB/Swiss-Prot Entry Name

NDUB7_HUMAN Link Image

Enzyme 40 PDB ID

Not Available

Enzyme 40 Cellular Location

Not Available

Enzyme 40 Gene Sequence

>408 bp

ATGGGGGCGCACCTGGTCCGGCGCTACCTGGGCGATGCTTCGGTGGAGCCCGACCCCCTG
CAGATGCCAACCTTCCCGCCAGACTACGGCTTCCCCGAACGCAAGGAGCGCGAGATGGTG
GCCACACAGCAGGAGATGATGGACGCGAGTGAGGCTCAGCTGCGGGACTACTGCGCCCAC
CACCTCATCCGGCTGCTCAAGTGCAAGCGTGACAGCTTCCCAAGTTGCTGGCCTGCAAGC
AGGAAGCGGCACGACTCGGGACTACTGCGCACCGCAAGCTATGTGATGCGCATGAAGGAG
TTTGAGCGGGACGAGGGCTGCTCCAGCGGAAGAAGCGGCGGGAGAAGAAGGCGGCAAATC
TGCAAAGGCCAGGGACCCGGGGAAGTGGACCCCAAGGTGGCCCTGTAG

Enzyme 40 GenBank Gene ID

M33374

Enzyme 40 GeneCard ID

NDUFB7

Enzyme 40 GenAtlas ID

NDUFB7

Enzyme 40 HGNC ID

HGNC:7702

Enzyme 40 Chromosome Location

Enzyme 40 Locus

19p13.12-p13.11

Enzyme 40 SNPs

SNPJam Report Link Image

Enzyme 40 General References

Wong YC, Tsao SW, Kakefuda M, Bernal SD: cDNA cloning of a novel cell adhesion protein expressed in human squamous carcinoma cells. Biochem Biophys Res Commun. 1990 Jan 30;166(2):984-92. [PubMed ]
Triepels R, Smeitink J, Loeffen J, Smeets R, Trijbels F, van den Heuvel L: Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and mutational analysis of 19 genes of the HP fraction in complex I-deficient-patients. Hum Genet. 2000 Apr;106(4):385-91. [PubMed ]
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]

Enzyme 40 Metabolite References

Not Available

Enzyme 41 [top]

Enzyme 41 ID

5409

Enzyme 41 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial precursor

Enzyme 41 Synonyms

NADH-ubiquinone oxidoreductase 39 kDa subunit
Complex I-39kD
CI-39kD

Enzyme 41 Gene Name

NDUFA9

Enzyme 41 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial precursor

MAAAAQSRVVRVLSMSRSAITAIATSVCHGPPCRQLHHALMPHGKGGRSSVSGIVATVFG
ATGFLGRYVVNHLGRMGSQVIIPYRCDKYDIMHLRPMGDLGQLLFLEWDARDKDSIRRVV
QHSNVVINLIGRDWETKNFDFEDVFVKIPQAIAQLSKEAGVEKFIHVSHLNANIKSSSRY
LRNKAVGEKVVRDAFPEAIIVKPSDIFGREDRFLNSFASMHRFGPIPLGSLGWKTVKQPV
YVVDVSKGIVNAVKDPDANGKSFAFVGPSRYLLFHLVKYIFAVAHRLFLPFPLPLFAYRW
VARVFEISPFEPWITRDKVERMHITDMKLPHLPGLEDLGIQATPLELKAIEVLRRHRTYR
WLSAEIEDVKPAKTVNI

Enzyme 41 Number of Residues

377

Enzyme 41 Molecular Weight

42510

Enzyme 41 Theoretical pI

10.37

Enzyme 41 GO Classification

Function
NAD binding binding catalytic activity coenzyme binding cofactor binding
Process
cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleotide-sugar metabolism physiological process
Component
—

Enzyme 41 General Function

Cell wall/membrane/envelope biogenesis

Enzyme 41 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 41 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 41 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 41 Pfam Domain Function

Epimerase (PF01370 )

Enzyme 41 Signals

1-24

Enzyme 41 Transmembrane Regions

Not Available

Enzyme 41 Essentiality

Not Available

Enzyme 41 GenBank ID Protein

5326823

Enzyme 41 UniProtKB/Swiss-Prot ID

Q16795

Enzyme 41 UniProtKB/Swiss-Prot Entry Name

NDUA9_HUMAN Link Image

Enzyme 41 PDB ID

Not Available

Enzyme 41 Cellular Location

Not Available

Enzyme 41 Gene Sequence

>1134 bp

ATGGCGGCTGCCGCACAATCCCGGGTTGTCCGGGTCCTGTCAATGTCACGTTCTGCCATT
ACTGCAATAGCCACATCTGTGTGTCACGGCCCACCCTGTCGCCAGCTTCATCATGCCCTC
ATGCCTCATGGGAAAGGTGGACGTTCCTCAGTCAGTGGGATTGTGGCCACTGTGTTTGGA
GCAACAGGATTCCTGGGGCGATATGTTGTCAACCACCTTGGACGCATGGGGTCACAGGTA
ATCATACCCTATCGGTGTGATAAATATGACATCATGCACCTTCGTCCCATGGGTGACCTG
GGCCAGCTTCTGTTTCTGGAATGGGACGCGAGAGATAAAGATTCTATCCGACGAGTAGTA
CAACACAGCAATGTGGTCATCAATCTTATTGGACGAGACTGGGAAACCAAAAACTTTGAT
TTTGAGGATGTTTTTGTGAAGATTCCCCAAGCAATTGCTCAACTGTCCAAGGAAGCTGGA
GTTGAAAAATTCATTCATGTTTCACATCTGAATGCGAATATTAAAAGCTCTTCTAGATAT
TTGAGAAATAAGGCTGTTGGAGAGAAAGTAGTGAGAGATGCATTTCCGGAAGCCATTATC
GTAAAGCCGTCGGACATCTTTGGAAGAGAGGATAGATTCCTTAATTCTTTTGCAAGTATG
CATCGGTTTGGTCCTATACCCCTTGGTTCCTTGGGCTGGAAGACAGTTAAACAACCAGTA
TATGTCGTAGATGTATCCAAAGGAATTGTTAATGCAGTTAAGGATCCTGATGCCAATGGG
AAATCCTTTGCTTTCGTTGGTCCCAGTCGGTACCTCCTTTTCCACCTGGTGAAGTACATC
TTTGCTGTGGCTCACAGATTGTTCCTCCCATTCCCCTTGCCGCTTTTTGCCTATCGATGG
GTAGCAAGAGTCTTTGAAATAAGCCCATTTGAGCCCTGGATAACAAGGGATAAAGTGGAG
CGGATGCACATCACAGACATGAAATTGCCTCACCTGCCTGGCTTAGAAGACCTTGGTATT
CAGGCAACACCACTGGAACTCAAGGCCATTGAGGTGCTGCGGCGTCATCGCACTTACCGC
TGGCTGTCTGCTGAAATTGAGGATGTGAAGCCGGCCAAGACCGTCAACATTTAG

Enzyme 41 GenBank Gene ID

AF050641

Enzyme 41 GeneCard ID

NDUFA9

Enzyme 41 GenAtlas ID

NDUFA9

Enzyme 41 HGNC ID

HGNC:7693

Enzyme 41 Chromosome Location

Enzyme 41 Locus

12p13.3

Enzyme 41 SNPs

SNPJam Report Link Image

Enzyme 41 General References

Cross SH, Charlton JA, Nan X, Bird AP: Purification of CpG islands using a methylated DNA binding column. Nat Genet. 1994 Mar;6(3):236-44. [PubMed ]
Baens M, Chaffanet M, Cassiman JJ, van den Berghe H, Marynen P: Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid. Genomics. 1993 Apr;16(1):214-8. [PubMed ]

Enzyme 41 Metabolite References

Not Available

Enzyme 42 [top]

Enzyme 42 ID

5410

Enzyme 42 Name

NADH-ubiquinone oxidoreductase chain 4

Enzyme 42 Synonyms

NADH dehydrogenase subunit 4

Enzyme 42 Gene Name

MT-ND4

Enzyme 42 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 4

MLKLIVPTIMLLPLTWLSKKHMIWINTTTHSLIISIIPLLFFNQINNNLFSCSPTFSSDP
LTTPLLMLTTWLLPLTIMASQRHLSSEPLSRKKLYLSMLISLQISLIMTFTATELIMFYI
FFETTLIPTLAIITRWGNQPERLNAGTYFLFYTLVGSLPLLIALIYTHNTLGSLNILLLT
LTAQELSNSWANNLMWLAYTMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGG
YGMMRLTLILNPLTKHMAYPFLVLSLWGMIMTSSICLRQTDLKSLIAYSSISHMALVVTA
ILIQTPWSFTGAVILMIAHGLTSSLLFCLANSNYERTHSRIMILSQGLQTLLPLMAFWWL
LASLANLALPPTINLLGELSVLVTTFSWSNITLLLTGLNMLVTALYSLYMFTTTQWGSLT
HHINNMKPSFTRENTLMFMHLSPILLLSLNPDIITGFSS

Enzyme 42 Number of Residues

459

Enzyme 42 Molecular Weight

51582

Enzyme 42 Theoretical pI

9.67

Enzyme 42 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
intracellular membrane-bound organelle membrane-bound organelle mitochondrion organelle

Enzyme 42 General Function

Energy production and conversion

Enzyme 42 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 42 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 42 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 42 Pfam Domain Function

Oxidored_q1 (PF00361 )
Oxidored_q5_N (PF01059 )

Enzyme 42 Signals

1-17

Enzyme 42 Transmembrane Regions

23-45
100-122
143-165
194-216
221-243
258-277
284-303
308-330
351-373
388-410

Enzyme 42 Essentiality

Not Available

Enzyme 42 GenBank ID Protein

Not Available

Enzyme 42 UniProtKB/Swiss-Prot ID

P03905

Enzyme 42 UniProtKB/Swiss-Prot Entry Name

NU4M_HUMAN Link Image

Enzyme 42 PDB ID

Not Available

Enzyme 42 Cellular Location

Not Available

Enzyme 42 Gene Sequence

Not Available

Enzyme 42 GenBank Gene ID

J01415

Enzyme 42 GeneCard ID

MT-ND4

Enzyme 42 GenAtlas ID

MT-ND4

Enzyme 42 HGNC ID

HGNC:7459

Enzyme 42 Chromosome Location

Enzyme 42 Locus

Enzyme 42 SNPs

SNPJam Report Link Image

Enzyme 42 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Lu X, Walker T, MacManus JP, Seligy VL: Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation. Cancer Res. 1992 Jul 1;52(13):3718-25. [PubMed ]
Silva WA Jr, Bonatto SL, Holanda AJ, Ribeiro-Dos-Santos AK, Paixao BM, Goldman GH, Abe-Sandes K, Rodriguez-Delfin L, Barbosa M, Paco-Larson ML, Petzl-Erler ML, Valente V, Santos SE, Zago MA: Mitochondrial genome diversity of Native Americans supports a single early entry of founder populations into America. Am J Hum Genet. 2002 Jul;71(1):187-92. Epub 2002 May 17. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Brown WM, Prager EM, Wang A, Wilson AC: Mitochondrial DNA sequences of primates: tempo and mode of evolution. J Mol Evol. 1982;18(4):225-39. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Wallace DC, Singh G, Lott MT, Hodge JA, Schurr TG, Lezza AM, Elsas LJ 2nd, Nikoskelainen EK: Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. Science. 1988 Dec 9;242(4884):1427-30. [PubMed ]
Majander A, Huoponen K, Savontaus ML, Nikoskelainen E, Wikstrom M: Electron transfer properties of NADH:ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON). FEBS Lett. 1991 Nov 4;292(1-2):289-92. [PubMed ]
Kormann BA, Schuster H, Berninger TA, Leo-Kottler B: Detection of the G to A mitochondrial DNA mutation at position 11778 in German families with Leber's hereditary optic neuropathy. Hum Genet. 1991 Nov;88(1):98-100. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Lertrit P, Noer AS, Jean-Francois MJ, Kapsa R, Dennett X, Thyagarajan D, Lethlean K, Byrne E, Marzuki S: A new disease-related mutation for mitochondrial encephalopathy lactic acidosis and strokelike episodes (MELAS) syndrome affects the ND4 subunit of the respiratory complex I. Am J Hum Genet. 1992 Sep;51(3):457-68. [PubMed ]
De Vries DD, Went LN, Bruyn GW, Scholte HR, Hofstra RM, Bolhuis PA, van Oost BA: Genetic and biochemical impairment of mitochondrial complex I activity in a family with Leber hereditary optic neuropathy and hereditary spastic dystonia. Am J Hum Genet. 1996 Apr;58(4):703-11. [PubMed ]
Sudoyo H, Sitepu M, Malik S, Poesponegoro HD, Marzuki S: Leber's hereditary optic neuropathy in Indonesia: two families with the mtDNA 11778G>A and 14484T>C mutations. Hum Mutat. 1998;Suppl 1:S271-4. [PubMed ]

Enzyme 42 Metabolite References

Not Available

Enzyme 43 [top]

Enzyme 43 ID

5412

Enzyme 43 Name

NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial precursor

Enzyme 43 Synonyms

NADH-ubiquinone oxidoreductase 20 kDa subunit
Complex I-20kD
CI-20kD
PSST subunit

Enzyme 43 Gene Name

NDUFS7

Enzyme 43 Protein Sequence

>NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial precursor

MAVLSAPGLRGFRILGLRSSVGPAVQARGVHQSVATDGPSSTQPALPKARAVAPKPSSRG
EYVVAKLDDLVNWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQSDVM
IVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYI
PGCPPTAEALLYGILQLQRKIKRERRLQIWYRR

Enzyme 43 Number of Residues

213

Enzyme 43 Molecular Weight

23564

Enzyme 43 Theoretical pI

10.36

Enzyme 43 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 43 General Function

Energy production and conversion

Enzyme 43 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 43 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 43 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 43 Pfam Domain Function

Oxidored_q6 (PF01058 )

Enzyme 43 Signals

None

Enzyme 43 Transmembrane Regions

None

Enzyme 43 Essentiality

Not Available

Enzyme 43 GenBank ID Protein

Not Available

Enzyme 43 UniProtKB/Swiss-Prot ID

O75251

Enzyme 43 UniProtKB/Swiss-Prot Entry Name

NDUS7_HUMAN Link Image

Enzyme 43 PDB ID

Not Available

Enzyme 43 Cellular Location

Not Available

Enzyme 43 Gene Sequence

Not Available

Enzyme 43 GenBank Gene ID

AC005329

Enzyme 43 GeneCard ID

NDUFS7

Enzyme 43 GenAtlas ID

NDUFS7

Enzyme 43 HGNC ID

HGNC:7714

Enzyme 43 Chromosome Location

Enzyme 43 Locus

19p13.3

Enzyme 43 SNPs

SNPJam Report Link Image

Enzyme 43 General References

Hyslop SJ, Duncan AM, Pitkanen S, Robinson BH: Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13. Genomics. 1996 Nov 1;37(3):375-80. [PubMed ]
Triepels RH, van den Heuvel LP, Loeffen JL, Buskens CA, Smeets RJ, Rubio Gozalbo ME, Budde SM, Mariman EC, Wijburg FA, Barth PG, Trijbels JM, Smeitink JA: Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I. Ann Neurol. 1999 Jun;45(6):787-90. [PubMed ]
Smeitink J, van den Heuvel L: Human mitochondrial complex I in health and disease. Am J Hum Genet. 1999 Jun;64(6):1505-10. [PubMed ]

Enzyme 43 Metabolite References

Not Available

Enzyme 44 [top]

Enzyme 44 ID

5413

Enzyme 44 Name

Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase

Enzyme 44 Synonyms

XD
Xanthine oxidase
XO
Xanthine oxidoreductase]

Enzyme 44 Gene Name

XDH

Enzyme 44 Protein Sequence

>Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase

MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV

Enzyme 44 Number of Residues

1333

Enzyme 44 Molecular Weight

146426

Enzyme 44 Theoretical pI

7.70

Enzyme 44 GO Classification

Function
binding catalytic activity cation binding electron transporter activity ion binding iron ion binding metal ion binding oxidoreductase activity transition metal ion binding transporter activity
Process
cellular metabolism electron transport generation of precursor metabolites and energy metabolism physiological process
Component
—

Enzyme 44 General Function

Nucleotide transport and metabolism

Enzyme 44 Specific Function

This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups

Enzyme 44 Pathways

Purine Metabolism (map00230 )

Enzyme 44 Reactions

xanthine + H2O + O2 = urate + H2O2

Enzyme 44 Pfam Domain Function

Ald_Xan_dh_C (PF01315 )
Ald_Xan_dh_C2 (PF02738 )
CO_deh_flav_C (PF03450 )
FAD_binding_5 (PF00941 )
Fer2 (PF00111 )
Fer2_2 (PF01799 )

Enzyme 44 Signals

None

Enzyme 44 Transmembrane Regions

None

Enzyme 44 Essentiality

Not Available

Enzyme 44 GenBank ID Protein

10336525

Enzyme 44 UniProtKB/Swiss-Prot ID

P47989

Enzyme 44 UniProtKB/Swiss-Prot Entry Name

XDH_HUMAN

Enzyme 44 PDB ID

1V97

Enzyme 44 PDB File

Show

Enzyme 44 3D Structure

Enzyme 44 Cellular Location

Not Available

Enzyme 44 Gene Sequence

>4002 bp

ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA

Enzyme 44 GenBank Gene ID

D11456

Enzyme 44 GeneCard ID

XDH

Enzyme 44 GenAtlas ID

XDH

Enzyme 44 HGNC ID

HGNC:12805 Link Image

Enzyme 44 Chromosome Location

Enzyme 44 Locus

2p23.1

Enzyme 44 SNPs

SNPJam Report Link Image

Enzyme 44 General References

Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed ]
Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [PubMed ]
Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1995 Oct 4;215(1):429. [PubMed ]
Saksela M, Raivio KO: Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochem J. 1996 Apr 1;315 ( Pt 1):235-9. [PubMed ]

Enzyme 44 Metabolite References

Not Available

Enzyme 45 [top]

Enzyme 45 ID

5414

Enzyme 45 Name

NADH-ubiquinone oxidoreductase chain 3

Enzyme 45 Synonyms

NADH dehydrogenase subunit 3

Enzyme 45 Gene Name

MT-ND3

Enzyme 45 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 3

MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAI
TFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE

Enzyme 45 Number of Residues

115

Enzyme 45 Molecular Weight

13186

Enzyme 45 Theoretical pI

4.08

Enzyme 45 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 45 General Function

Energy production and conversion

Enzyme 45 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 45 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 45 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 45 Pfam Domain Function

Oxidored_q4 (PF00507 )

Enzyme 45 Signals

1-29

Enzyme 45 Transmembrane Regions

55-77
84-106

Enzyme 45 Essentiality

Not Available

Enzyme 45 GenBank ID Protein

Not Available

Enzyme 45 UniProtKB/Swiss-Prot ID

P03897

Enzyme 45 UniProtKB/Swiss-Prot Entry Name

NU3M_HUMAN Link Image

Enzyme 45 PDB ID

Not Available

Enzyme 45 Cellular Location

Not Available

Enzyme 45 Gene Sequence

Not Available

Enzyme 45 GenBank Gene ID

J01415

Enzyme 45 GeneCard ID

MT-ND3

Enzyme 45 GenAtlas ID

MT-ND3

Enzyme 45 HGNC ID

HGNC:7458

Enzyme 45 Chromosome Location

Enzyme 45 Locus

Enzyme 45 SNPs

SNPJam Report Link Image

Enzyme 45 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G: Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. Nature. 1985 Apr 18-24;314(6012):592-7. [PubMed ]
Oliver NA, Greenberg BD, Wallace DC: Assignment of a polymorphic polypeptide to the human mitochondrial DNA unidentified reading frame 3 gene by a new peptide mapping strategy. J Biol Chem. 1983 May 10;258(9):5834-9. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]

Enzyme 45 Metabolite References

Not Available

Enzyme 46 [top]

Enzyme 46 ID

5418

Enzyme 46 Name

NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor

Enzyme 46 Synonyms

NADH-ubiquinone oxidoreductase 51 kDa subunit
Complex I-51kD
CI-51kD
NADH dehydrogenase flavoprotein 1

Enzyme 46 Gene Name

NDUFV1

Enzyme 46 Protein Sequence

>NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor

MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRG
DWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEG
EPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAG
LIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPT
TVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELI
EKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRS
TDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIE
GHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS

Enzyme 46 Number of Residues

464

Enzyme 46 Molecular Weight

50818

Enzyme 46 Theoretical pI

8.29

Enzyme 46 GO Classification

Function
FMN binding NAD binding NADH dehydrogenase (ubiquinone) activity binding catalytic activity cation binding cation transporter activity coenzyme binding cofactor binding hydrogen ion transporter activity ion binding ion transporter activity iron ion binding monovalent inorganic cation transporter activity nucleotide binding oxidoreductase activity oxidoreductase activity, acting on NADH or NADPH transition metal ion binding transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 46 General Function

Energy production and conversion

Enzyme 46 Specific Function

Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone

Enzyme 46 Pathways

Oxidative phosphorylation (map00190 )

Enzyme 46 Reactions

NADH + H+ + acceptor = NAD+ + reduced acceptor

Enzyme 46 Pfam Domain Function

Complex1_51K (PF01512 )

Enzyme 46 Signals

1-18

Enzyme 46 Transmembrane Regions

Not Available

Enzyme 46 Essentiality

Not Available

Enzyme 46 GenBank ID Protein

3184148

Enzyme 46 UniProtKB/Swiss-Prot ID

P49821

Enzyme 46 UniProtKB/Swiss-Prot Entry Name

NDUV1_HUMAN Link Image

Enzyme 46 PDB ID

Not Available

Enzyme 46 Cellular Location

Not Available

Enzyme 46 Gene Sequence

>72 bp

ATGCTGGCAACACGGCGGCTGCTCGGCTGGTCGCTTCCCGCGCGGGTATCTGTGCGTTTC
AGCGGCGACACG

Enzyme 46 GenBank Gene ID

Y17379

Enzyme 46 GeneCard ID

NDUFV1

Enzyme 46 GenAtlas ID

NDUFV1

Enzyme 46 HGNC ID

HGNC:7716

Enzyme 46 Chromosome Location

Enzyme 46 Locus

11q13

Enzyme 46 SNPs

SNPJam Report Link Image

Enzyme 46 General References

Schuelke M, Loeffen J, Mariman E, Smeitink J, van den Heuvel L: Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon inducible protein (IP-30) precursor: is this a link between mitochondrial myopathy and inflammation? Biochem Biophys Res Commun. 1998 Apr 17;245(2):599-606. [PubMed ]
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]
Spencer SR, Taylor JB, Cowell IG, Xia CL, Pemble SE, Ketterer B: The human mitochondrial NADH: ubiquinone oxidoreductase 51-kDa subunit maps adjacent to the glutathione S-transferase P1-1 gene on chromosome 11q13. Genomics. 1992 Dec;14(4):1116-8. [PubMed ]
Ali ST, Duncan AM, Schappert K, Heng HH, Tsui LC, Chow W, Robinson BH: Chromosomal localization of the human gene encoding the 51-kDa subunit of mitochondrial complex I (NDUFV1) to 11q13. Genomics. 1993 Nov;18(2):435-9. [PubMed ]
Schuelke M, Smeitink J, Mariman E, Loeffen J, Plecko B, Trijbels F, Stockler-Ipsiroglu S, van den Heuvel L: Mutant NDUFV1 subunit of mitochondrial complex I causes leukodystrophy and myoclonic epilepsy. Nat Genet. 1999 Mar;21(3):260-1. [PubMed ]

Enzyme 46 Metabolite References

Not Available

Enzyme 47 [top]

Enzyme 47 ID

5420

Enzyme 47 Name

Methylenetetrahydrofolate reductase

Enzyme 47 Synonyms

Not Available

Enzyme 47 Gene Name

MTHFR

Enzyme 47 Protein Sequence

>Methylenetetrahydrofolate reductase

MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP

Enzyme 47 Number of Residues

656

Enzyme 47 Molecular Weight

74597

Enzyme 47 Theoretical pI

5.00

Enzyme 47 GO Classification

Function
catalytic activity methylenetetrahydrofolate reductase (NADPH) activity methylenetetrahydrofolate reductase (NADPH) activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
amino acid and derivative metabolism amino acid metabolism cellular metabolism metabolism methionine metabolism physiological process sulfur amino acid metabolism
Component
—

Enzyme 47 General Function

Amino acid transport and metabolism

Enzyme 47 Specific Function

Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine

Enzyme 47 Pathways

One Carbon Pool By Folate (map00670 )

Enzyme 47 Reactions

5-methyltetrahydrofolate + NADP+ = 5,10-methylenetetrahydrofolate + NADPH + H+

Enzyme 47 Pfam Domain Function

MTHFR (PF02219 )

Enzyme 47 Signals

None

Enzyme 47 Transmembrane Regions

None

Enzyme 47 Essentiality

Not Available

Enzyme 47 GenBank ID Protein

6139053

Enzyme 47 UniProtKB/Swiss-Prot ID

P42898

Enzyme 47 UniProtKB/Swiss-Prot Entry Name

MTHR_HUMAN Link Image

Enzyme 47 PDB ID

Not Available

Enzyme 47 Cellular Location

Not Available

Enzyme 47 Gene Sequence

>1971 bp

ATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGCAGTGCCAGC
AGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTGGACCCTGAG
CGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGACAAGTGGTTC
TCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATCTCAAGGTTT
GACCGGATGGCAGCAGGTGGCCCCCTCTACATAGACGTGACCTGGCACCCAGCAGGTGAC
CCTGGCTCAGACAAGGAGACCTCCTCCATGATGATCGCCAGCACCGCCGTGAACTACTGT
GGCCTGGAGACCATCCTGCACATGACCTGCTGCCGTCAGCGCCTGGAGGAGATCACGGGC
CATCTGCACAAAGCTAAGCAGCTGGGCCTGAAGAACATCATGGCGCTGCGGGGAGACCCA
ATAGGTGACCAGTGGGAAGAGGAGGAGGGAGGCTTCAACTACGCAGTGGACCTGGTGAAG
CACATCCGAAGTGAGTTTGGTGACTACTTTGACATCTGTGTGGCAGGTTACCCCAAAGGC
CACCCCGAAGCAGGGAGCTTTGAGGCTGACCTGAAGCACTTGAAGGAGAAGGTGTCTGCG
GGAGCCGATTTCATCATCACGCAGCTTTTCTTTGAGGCTGACACATTCTTCCGCTTTGTG
AAGGCATGCACCGACATGGGCATCACTTGCCCCATCGTCCCCGGGATCTTTCCCATCCAG
GGCTACCACTCCCTTCGGCAGCTTGTGAAGCTGTCCAAGCTGGAGGTGCCACAGGAGATC
AAGGACGTGATTGAGCCAATCAAAGACAACGATGCTGCCATCCGCAACTATGGCATCGAG
CTGGCCGTGAGCCTGTGCCAGGAGCTTCTGGCCAGTGGCTTGGTGCCAGGCCTCCACTTC
TACACCCTCAACCGCGAGATGGCTACCACAGAGGTGCTGAAGCGCCTGGGGATGTGGACT
GAGGACCCCAGGCGTCCCCTACCCTGGGCTCTCAGTGCCCACCCCAAGCGCCGAGAGGAA
GATGTACGTCCCATCTTCTGGGCCTCCAGACCAAAGAGTTACATCTACCGTACCCAGGAG
TGGGACGAGTTCCCTAACGGCCGCTGGGGCAATTCCTCTTCCCCTGCCTTTGGGGAGCTG
AAGGACTACTACCTCTTCTACCTGAAGAGCAAGTCCCCCAAGGAGGAGCTGCTGAAGATG
TGGGGGGAGGAGCTGACCAGTGAAGCAAGTGTCTTTGAAGTCTTTGTTCTTTACCTCTCG
GGAGAACCAAACCGGAATGGTCACAAAGTGACTTGCCTGCCCTGGAACGATGAGCCCCTG
GCGGCTGAGACCAGCCTGCTGAAGGAGGAGCTGCTGCGGGTGAACCGCCAGGGCATCCTC
ACCATCAACTCACAGCCCAACATCAACGGGAAGCCGTCCTCCGACCCCATCGTGGGCTGG
GGCCCCAGCGGGGGCTATGTCTTCCAGAAGGCCTACTTAGAGTTTTTCACTTCCCGCGAG
ACAGCGGAAGCACTTCTGCAAGTGCTGAAGAAGTACGAGCTCCGGGTTAATTACCACCTT
GTCAATGTGAAGGGTGAAAACATCACCAATGCCCCTGAACTGCAGCCGAATGCTGTCACT
TGGGGCATCTTCCCTGGGCGAGAGATCATCCAGCCCACCGTAGTGGATCCCGTCAGCTTC
ATGTTCTGGAAGGACGAGGCCTTTGCCCTGTGGATTGAGCGGTGGGGAAAGCTGTATGAG
GAGGAGTCCCCGTCCCGCACCATCATCCAGTACATCCACGACAACTACTTCCTGGTCAAC
CTGGTGGACAATGACTTCCCACTGGACAACTGCCTCTGGCAGGTGGTGGAAGACACATTG
GAGCTTCTCAACAGGCCCACCCAGAATGCGAGAGAAACGGAGGCTCCATGA

Enzyme 47 GenBank Gene ID

U09806

Enzyme 47 GeneCard ID

MTHFR

Enzyme 47 GenAtlas ID

MTHFR

Enzyme 47 HGNC ID

HGNC:7436

Enzyme 47 Chromosome Location

Enzyme 47 Locus

1p36.3

Enzyme 47 SNPs

SNPJam Report Link Image

Enzyme 47 General References

Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nat Genet. 1994 Jun;7(2):195-200. [PubMed ]
Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA mapping and mutation identification. Nat Genet. 1994 Aug;7(4):551. [PubMed ]
Goyette P, Pai A, Milos R, Frosst P, Tran P, Chen Z, Chan M, Rozen R: Gene structure of human and mouse methylenetetrahydrofolate reductase (MTHFR) Mamm Genome. 1998 Aug;9(8):652-6. [PubMed ]
Goyette P, Frosst P, Rosenblatt DS, Rozen R: Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency. Am J Hum Genet. 1995 May;56(5):1052-9. [PubMed ]
Frosst P, Blom HJ, Milos R, Goyette P, Sheppard CA, Matthews RG, Boers GJ, den Heijer M, Kluijtmans LA, van den Heuvel LP, et al.: A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet. 1995 May;10(1):111-3. [PubMed ]
Goyette P, Christensen B, Rosenblatt DS, Rozen R: Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am J Hum Genet. 1996 Dec;59(6):1268-75. [PubMed ]
Schneider JA, Rees DC, Liu YT, Clegg JB: Worldwide distribution of a common methylenetetrahydrofolate reductase mutation. Am J Hum Genet. 1998 May;62(5):1258-60. [PubMed ]
van der Put NM, Gabreels F, Stevens EM, Smeitink JA, Trijbels FJ, Eskes TK, van den Heuvel LP, Blom HJ: A second common mutation in the methylenetetrahydrofolate reductase gene: an additional risk factor for neural-tube defects? Am J Hum Genet. 1998 May;62(5):1044-51. [PubMed ]
Kluijtmans LA, Wendel U, Stevens EM, van den Heuvel LP, Trijbels FJ, Blom HJ: Identification of four novel mutations in severe methylenetetrahydrofolate reductase deficiency. Eur J Hum Genet. 1998 May-Jun;6(3):257-65. [PubMed ]
Weisberg I, Tran P, Christensen B, Sibani S, Rozen R: A second genetic polymorphism in methylenetetrahydrofolate reductase (MTHFR) associated with decreased enzyme activity. Mol Genet Metab. 1998 Jul;64(3):169-72. [PubMed ]
Sibani S, Christensen B, O'Ferrall E, Saadi I, Hiou-Tim F, Rosenblatt DS, Rozen R: Characterization of six novel mutations in the methylenetetrahydrofolate reductase (MTHFR) gene in patients with homocystinuria. Hum Mutat. 2000;15(3):280-7. [PubMed ]

Enzyme 47 Metabolite References

Not Available

Enzyme 48 [top]

Enzyme 48 ID

5421

Enzyme 48 Name

NADH-ubiquinone oxidoreductase chain 6

Enzyme 48 Synonyms

NADH dehydrogenase subunit 6

Enzyme 48 Gene Name

MT-ND6

Enzyme 48 Protein Sequence

>NADH-ubiquinone oxidoreductase chain 6

MMYALFLLSVGLVMGFVGFSSKPSPIYGGLVLIVSGVVGCVIILNFGGGYMGLMVFLIYL
GGMMVVFGYTTAMAIEEYPEAWGSGVEVLVSVLVGLAMEVGLVLWVKEYDGVVVVVNFNS
VGSWMIYEGEGSGLIREDPIGAGALYDYGRWLVVVTGWTLFVGVYIVIEIARGN

Enzyme 48 Number of Residues

174

Enzyme 48 Molecular Weight

18622

Enzyme 48 Theoretical pI

3.90

Enzyme 48 GO Classification

Function
NADH dehydrogenase (ubiquinone) activity cation transporter activity hydrogen ion transporter activity ion transporter activity monovalent inorganic cation transporter activity transporter activity
Process
ATP synthesis coupled electron transport ATP synthesis coupled electron transport (sensu Eukaryota) cellular metabolism electron transport generation of precursor metabolites and energy metabolism mitochondrial electron transport, NADH to ubiquinone physiological process
Component
—

Enzyme 48 General Function

Not Available

Enzyme 48 Specific Function

NADH + ubiquinone = NAD(+) + ubiquinol

Enzyme 48 Pathways

Oxidative phosphorylation (map00190 )
Ubiquinone Biosynthesis (map00130 )

Enzyme 48 Reactions

NADH + H+ + ubiquinone = NAD+ + ubiquinol

Enzyme 48 Pfam Domain Function

Oxidored_q3 (PF00499 )

Enzyme 48 Signals

1-15

Enzyme 48 Transmembrane Regions

26-48
55-74
84-106
111-128
148-170

Enzyme 48 Essentiality

Not Available

Enzyme 48 GenBank ID Protein

Not Available

Enzyme 48 UniProtKB/Swiss-Prot ID

P03923

Enzyme 48 UniProtKB/Swiss-Prot Entry Name

NU6M_HUMAN Link Image

Enzyme 48 PDB ID

Not Available

Enzyme 48 Cellular Location

Not Available

Enzyme 48 Gene Sequence

Not Available

Enzyme 48 GenBank Gene ID

J01415

Enzyme 48 GeneCard ID

MT-ND6

Enzyme 48 GenAtlas ID

MT-ND6

Enzyme 48 HGNC ID

HGNC:7462

Enzyme 48 Chromosome Location

Enzyme 48 Locus

Enzyme 48 SNPs

SNPJam Report Link Image

Enzyme 48 General References

Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG: Sequence and organization of the human mitochondrial genome. Nature. 1981 Apr 9;290(5806):457-65. [PubMed ]
Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N: Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):532-6. [PubMed ]
Sudoyo H, Sitepu M, Malik S, Poesponegoro HD, Marzuki S: Leber's hereditary optic neuropathy in Indonesia: two families with the mtDNA 11778G>A and 14484T>C mutations. Hum Mutat. 1998;Suppl 1:S271-4. [PubMed ]
Ingman M, Kaessmann H, Paabo S, Gyllensten U: Mitochondrial genome variation and the origin of modern humans. Nature. 2000 Dec 7;408(6813):708-13. [PubMed ]
Ingman M, Gyllensten U: Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. Genome Res. 2003 Jul;13(7):1600-6. [PubMed ]
Ozawa T, Tanaka M, Sugiyama S, Ino H, Ohno K, Hattori K, Ohbayashi T, Ito T, Deguchi H, Kawamura K, et al.: Patients with idiopathic cardiomyopathy belong to the same mitochondrial DNA gene family of Parkinson's disease and mitochondrial encephalomyopathy. Biochem Biophys Res Commun. 1991 May 31;177(1):518-25. [PubMed ]
Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E: Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. Hum Genet. 1991 Dec;88(2):139-45. [PubMed ]
Johns DR, Neufeld MJ, Park RD: An ND-6 mitochondrial DNA mutation associated with Leber hereditary optic neuropathy. Biochem Biophys Res Commun. 1992 Sep 30;187(3):1551-7. [PubMed ]
Jun AS, Brown MD, Wallace DC: A mitochondrial DNA mutation at nucleotide pair 14459 of the NADH dehydrogenase subunit 6 gene associated with maternally inherited Leber hereditary optic neuropathy and dystonia. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):6206-10. [PubMed ]
De Vries DD, Went LN, Bruyn GW, Scholte HR, Hofstra RM, Bolhuis PA, van Oost BA: Genetic and biochemical impairment of mitochondrial complex I activity in a family with Leber hereditary optic neuropathy and hereditary spastic dystonia. Am J Hum Genet. 1996 Apr;58(4):703-11. [PubMed ]
Leo-Kottler B, Christ-Adler M, Baumann B, Zrenner E, Wissinger B: Leber's hereditary optic neuropathy: clinical and molecular genetic results obtained in a family with a new point mutation at nucleotide position 14498 in the ND 6 gene. Ger J Ophthalmol. 1996 Jul;5(4):233-40. [PubMed ]
Besch D, Leo-Kottler B, Zrenner E, Wissinger B: Leber's hereditary optic neuropathy: clinical and molecular genetic findings in a patient with a new mutation in the ND6 gene. Graefes Arch Clin Exp Ophthalmol. 1999 Sep;237(9):745-52. [PubMed ]
Chinnery PF, Brown DT, Andrews RM, Singh-Kler R, Riordan-Eva P, Lindley J, Applegarth DA, Turnbull DM, Howell N: The mitochondrial ND6 gene is a hot spot for mutations that cause Leber's hereditary optic neuropathy. Brain. 2001 Jan;124(Pt 1):209-18. [PubMed ]
Ravn K, Wibrand F, Hansen FJ, Horn N, Rosenberg T, Schwartz M: An mtDNA mutation, 14453G-->A, in the NADH dehydrogenase subunit 6 associated with severe MELAS syndrome. Eur J Hum Genet. 2001 Oct;9(10):805-9. [PubMed ]

Enzyme 48 Metabolite References

Not Available

Enzyme 49 [top]

Enzyme 49 ID

5422

Enzyme 49 Name

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

Enzyme 49 Synonyms

NADH-ubiquinone oxidoreductase B16.6 subunit
Complex I-B16.6
CI-B16.6
Gene associated with retinoic- interferon-induced mortality 19 protein
GRIM-19
Cell death- regulatory protein GRIM-19

Enzyme 49 Gene Name

NDUFA13

Enzyme 49 Protein Sequence

>NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13

MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRL
QIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPL
IGELYGLRTTEEALHASHGFMWYT

Enzyme 49 Number of Residues

144

Enzyme 49 Molecular Weight

16699

Enzyme 49 Theoretical pI

8.84

Enzyme 49 GO Classification

Not Available

Enzyme 49 General Function

Not Available

Enzym

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Human Metabolome Database Version 2.5

Showing metabocard for NAD (HMDB00902)