Human Metabolome Database Version 2.5

Showing metabocard for Adenosine triphosphate (HMDB00538)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2005-11-16 15:48:42

Update Date

2010-01-20 12:02:58

Accession Number

HMDB00538

Secondary Accession Numbers

Not Available

Common Name

Adenosine triphosphate

Description

Adenosine triphosphate (ATP) is a nucleotide consisting of a purine base (adenine) attached to the first carbon atom of ribose (a pentose sugar). Three phosphate groups are esterified at the fifth carbon atom of the ribose. ATP is incorporated into nucleic acids by polymerases in the processes of DNA replication and transcription. ATP contributes to cellular energy charge and participates in overall energy balance, maintaining cellular homeostasis. ATP can act as an extracellular signaling molecule via interactions with specific purinergic receptors to mediate a wide variety of processes as diverse as neurotransmission, inflammation, apoptosis, and bone remodelling. Extracellular ATP and its metabolite adenosine have also been shown to exert a variety of effects on nearly every cell type in human skin, and ATP seems to play a direct role in triggering skin inflammatory, regenerative, and fibrotic responses to mechanical injury, an indirect role in melanocyte proliferation and apoptosis, and a complex role in Langerhans cell-directed adaptive immunity. During exercise, intracellular homeostasis depends on the matching of adenosine triphosphate (ATP) supply and ATP demand. Metabolites play a useful role in communicating the extent of ATP demand to the metabolic supply pathways Effects as different as proliferation or differentiation, chemotaxis, release of cytokines or lysosomal constituents, and generation of reactive oxygen or nitrogen species are elicited upon stimulation of blood cells with extracellular ATP. The increased concentration of adenosine triphosphate (ATP) in erythrocytes from patients with chronic renal failure (CRF) has been observed in many studies but the mechanism leading to these abnormalities still is controversial. (PMID: 15490415, 15129319, 14707763, 14696970, 11157473)

Synonyms

5'-(tetrahydrogen triphosphate) Adenosine
5'-ATP
ATP
Adenosine 5'-triphosphate
Adenosine 5'-triphosphorate
Adenosine 5'-triphosphoric acid
Adenosine triphosphate
Adenosine triphosphic acid
Adenylpyrophosphorate
Adenylpyrophosphoric acid
Adephos
Adetol
Adynol
Atipi
Atriphos
Cardenosine
Fosfobion
Glucobasin
Myotriphos
Phosphobion
Striadyne
Triadenyl
Triphosphaden
Triphosphoric acid adenosine ester

Chemical IUPAC Name

[[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxyphosphonic acid

Chemical Formula

C₁₀H₁₆N₅O₁₃P₃

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Nucleosides and Nucleoside conjugates
Class
Nucleotides
Sub Class
Nucleotide triphosphates
Family
Mammalian Metabolite
Species
secondary alcohol 1,2-diol primary amine primary aromatic amine phosphoric acid ester aromatic compound heterocyclic compound
Biofunction
Component of Aminosugars metabolism Component of Fructose and mannose metabolism Component of Galactose metabolism Component of Starch and sucrose metabolism Component of Streptomycin biosynthesis
Application
—
Source
Endogenous

Average Molecular Weight

507.181

Monoisotopic Molecular Weight

506.995758

Isomeric SMILES

NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O

Canonical SMILES

NC1=NC=NC2=C1N=CN2C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O

KEGG Compound ID

C00002

BioCyc ID

ATP

BiGG ID

33477

Wikipedia Link

Adenosine triphosphate Link Image

NuGOwiki Link

Metagene Link

METLIN ID

PubChem Compound

PubChem Substance

ChEBI ID

CAS Registry Number

56-65-5

InChI Identifier

InChI=1/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1

Synthesis Reference

Clark, V. M.; Kirby, G. W.; Todd, Alexander. Phosphorylation. XV. Use of phosphoramidic esters in acylation-new preparation of adenosine 5'-pyrophosphate and adenosine 5'-triphosphate. Journal of the Chemical Society (1957), 1497-1501.

Melting Point (Experimental)

Not Available

Experimental Water Solubility

1000.0 mg/mL [MERCK INDEX [1996)]; 862 mg/mL (Magnesium salt, HMP experimental] Source: PhysProp

Predicted Water Solubility

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

Physiological Charge

-4

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

-0.84 [Predicted by ALOGPS]; -5.5 [Predicted by PubChem via XLOGP]; -3.61 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

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MOL File

Show

SDF File

Show

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

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

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

Not Available

Simplified TOCSY Spectrum

Not Available

BMRB Spectrum

Not Available

Cellular Location

Cytoplasm
endoplasmic reticulum
Extracellular
mitochondria
nucleus
peroxisome

Biofluid Location

Blood
Cellular Cytoplasm
Cerebrospinal Fluid

Tissue Location

Tissue	References
Adipose Tissue	—
Bladder	—
Fibroblasts	—
Intestine	—
Kidney	—
Muscle	—
Myelin	—
Nerve Cells	—
Neuron	—
Pancreas	—
Platelet	—
Skeletal Muscle	—

Concentrations (Normal)

Biofluid	Blood
Value	1077.0 +/- 210.0 uM
Age	Newborn:0-30 days old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.

Biofluid	Blood
Value	1552.0 +/- 161.0 uM
Age	Adult:>18 yrs old
Sex	Male
Patient information	Normal
Comments	Not Available
References	Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.

Biofluid	Blood
Value	1390.0 +/- 170.0 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.

Biofluid	Blood
Value	3152.0 +/- 1698.0 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Traut TW: Physiological concentrations of purines and pyrimidines. Mol Cell Biochem. 1994 Nov 9;140(1):1-22. [PubMed ]

Biofluid	Cellular Cytoplasm
Value	1540 (1290-1790) 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 ]

Biofluid	CSF
Value	1.85 +/- 0.03 uM
Age	Adult:>18 yrs old
Sex	Both
Patient information	Normal
Comments	Not Available
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Concentrations (Abnormal)

Biofluid	CSF
Value	0.23 +/- 0.19 uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Rachialgia
Comments	Not Available
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Biofluid	CSF
Value	0.80 +/- 0.63 uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Subarachnoid hemorrhage
Comments	Not Available
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Biofluid	CSF
Value	1.08 +/- 0.77 uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Epilepsy
Comments	Not Available
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Biofluid	CSF
Value	0.26 +/- 0.11 uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Stroke
Comments	Cerebral stroke
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Biofluid	CSF
Value	1.09 +/- 0.76 uM
Age	Adult:>18 yrs old
Sex	Both
Condition	Neuroinfection
Comments	Not Available
References	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

Associated Disorders

Condition	References
Epilepsy	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]
Neuroinfection	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]
Rachialgia	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]
Stroke	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]
Subarachnoid hemorrhage	Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed ]

OMIM ID

540000 (Stroke)
105800 (Subarachnoid hemorrhage)

Pathways

Name	SMPDB Link	KEGG Link
Amino Sugar Metabolism	SMP00045	map00520
Ammonia Recycling	SMP00009	map00910
Citric Acid Cycle	SMP00057	map00020
DNA Replication Fork	SMP00477
Ethanol Degradation	SMP00449
Folate Metabolism	SMP00053	map00670
Gluconeogenesis	SMP00128	map00010
Glycerolipid Metabolism	SMP00039	map00561
Glycine and Serine Metabolism	SMP00004	map00260
Glycolysis	SMP00040	map00010
Histidine Metabolism	SMP00044	map00340
Inositol Phosphate Metabolism	SMP00462	map00562
Lactose Degradation	SMP00457
Lactose Synthesis	SMP00444
Methionine Metabolism	SMP00033	map00270
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
Phosphatidylinositol Phosphate Metabolism	SMP00463	map00562
Phytanic Acid Peroxisomal Oxidation	SMP00450
Purine Metabolism	SMP00050	map00230
Spermidine and Spermine Biosynthesis	SMP00445
Threonine and 2-Oxobutanoate Degradation	SMP00452
Transcription/Translation	SMP00019
Transfer of Acetyl Groups into Mitochondria	SMP00466
Trehalose Degradation	SMP00467
Urea Cycle	SMP00059	map00330

General References

Gottlieb C, Svanborg K, Eneroth P, Bygdeman M: Effect of prostaglandins on human sperm function in vitro and seminal adenosine triphosphate content. Fertil Steril. 1988 Feb;49(2):322-7. [PubMed ]
Mahmoud AM, Comhaire FH, Vermeulen L, Andreou E: Comparison of the resazurin test, adenosine triphosphate in semen, and various sperm parameters. Hum Reprod. 1994 Sep;9(9):1688-93. [PubMed ]
Kadmon M, Klunemann C, Bohme M, Ishikawa T, Gorgas K, Otto G, Herfarth C, Keppler D: Inhibition by cyclosporin A of adenosine triphosphate-dependent transport from the hepatocyte into bile. Gastroenterology. 1993 May;104(5):1507-14. [PubMed ]
Sun Y, MaLossi J, Jacobs SC, Chai TC: Effect of doxazosin on stretch-activated adenosine triphosphate release in bladder urothelial cells from patients with benign prostatic hyperplasia. Urology. 2002 Aug;60(2):351-6. [PubMed ]
Ryan LM, Rachow JW, McCarty BA, McCarty DJ: Adenosine triphosphate levels in human plasma. J Rheumatol. 1996 Feb;23(2):214-9. [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 ]
Yoshida M, Miyamae K, Iwashita H, Otani M, Inadome A: Management of detrusor dysfunction in the elderly: changes in acetylcholine and adenosine triphosphate release during aging. Urology. 2004 Mar;63(3 Suppl 1):17-23. [PubMed ]
Bar-Meir M, Elpeleg ON, Saada A: Effect of various agents on adenosine triphosphate synthesis in mitochondrial complex I deficiency. J Pediatr. 2001 Dec;139(6):868-70. [PubMed ]
Mannucci L, Pastore A, Rizzo C, Piemonte F, Rizzoni G, Emma F: Impaired activity of the gamma-glutamyl cycle in nephropathic cystinosis fibroblasts. Pediatr Res. 2006 Feb;59(2):332-5. [PubMed ]
Livingston JH, Brown JK, Harkness RA, McCreanor GM: Cerebrospinal fluid nucleotide metabolites following non-convulsive status epilepticus. Dev Med Child Neurol. 1989 Apr;31(2):168-73. [PubMed ]
Wikipedia

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5235

Enzyme 1 Name

Deoxycytidine kinase

Enzyme 1 Synonyms

Enzyme 1 Gene Name

DCK

Enzyme 1 Protein Sequence

>Deoxycytidine kinase

MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL

Enzyme 1 Number of Residues

260

Enzyme 1 Molecular Weight

30519

Enzyme 1 Theoretical pI

4.88

Enzyme 1 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity nucleotide binding 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 1 General Function

Nucleotide transport and metabolism

Enzyme 1 Specific Function

Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents

Enzyme 1 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 1 Reactions

NTP + deoxycytidine = NDP + dCMP

Enzyme 1 Pfam Domain Function

dNK (PF01712 )

Enzyme 1 Signals

None

Enzyme 1 Transmembrane Regions

None

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

181510

Enzyme 1 UniProtKB/Swiss-Prot ID

P27707

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

DCK_HUMAN

Enzyme 1 PDB ID

1P62

Enzyme 1 PDB File

Show

Enzyme 1 3D Structure

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>783 bp

ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

4q13.3-q21.1

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed ]
Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed ]
Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5239

Enzyme 2 Name

ATP-citrate synthase

Enzyme 2 Synonyms

ATP-citrate
pro-S--lyase
Citrate cleavage enzyme

Enzyme 2 Gene Name

ACLY

Enzyme 2 Protein Sequence

>ATP-citrate synthase

MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM

Enzyme 2 Number of Residues

1101

Enzyme 2 Molecular Weight

120841

Enzyme 2 Theoretical pI

7.34

Enzyme 2 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 2 General Function

Energy production and conversion

Enzyme 2 Specific Function

ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine

Enzyme 2 Pathways

Citrate Cycle (map00020 )

Enzyme 2 Reactions

ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA

Enzyme 2 Pfam Domain Function

CoA_binding (PF02629 )
Ligase_CoA (PF00549 )

Enzyme 2 Signals

None

Enzyme 2 Transmembrane Regions

None

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

28935

Enzyme 2 UniProtKB/Swiss-Prot ID

P53396

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

ACLY_HUMAN Link Image

Enzyme 2 PDB ID

Not Available

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>3318 bp

ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA

Enzyme 2 GenBank Gene ID

Enzyme 2 GeneCard ID

Enzyme 2 GenAtlas ID

Enzyme 2 HGNC ID

Enzyme 2 Chromosome Location

Enzyme 2 Locus

17q12-q21

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5247

Enzyme 3 Name

Acetyl-CoA carboxylase 2

Enzyme 3 Synonyms

ACC-beta[Includes: Biotin carboxylase

Enzyme 3 Gene Name

ACACB

Enzyme 3 Protein Sequence

>Acetyl-CoA carboxylase 2

MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST

Enzyme 3 Number of Residues

2458

Enzyme 3 Molecular Weight

276558

Enzyme 3 Theoretical pI

6.46

Enzyme 3 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ligase activity nucleotide binding purine nucleotide binding
Process
metabolism physiological process
Component
—

Enzyme 3 General Function

Lipid transport and metabolism

Enzyme 3 Specific Function

ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase

Enzyme 3 Pathways

Fatty Acid Biosynthesis (map00061 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )
Tetracycline biosynthesis (map00253 )

Enzyme 3 Reactions

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA

Enzyme 3 Pfam Domain Function

ACC_central (PF08326 )
Biotin_carb_C (PF02785 )
Biotin_lipoyl (PF00364 )
Carboxyl_trans (PF01039 )
CPSase_L_chain (PF00289 )
CPSase_L_D2 (PF02786 )

Enzyme 3 Signals

1-24

Enzyme 3 Transmembrane Regions

Not Available

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

2138330

Enzyme 3 UniProtKB/Swiss-Prot ID

O00763

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

COA2_HUMAN Link Image

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>7452 bp

ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGAGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCACAAAGACACCCAGCCAGGCCGAGCCCAGCCTCCCACA
AAGGCCCAAAGATCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCGCCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCAGCAAGCTGGTCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAGCTG
ATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTTGCT
GGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCCCTG
GAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGCATG
TCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGAGAC
TTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATCGAG
AAGGTGCTTATTGCCAACAACGGGATTGCCGCTGTGAAGTGCATGCGCTCCATCCGCAGG
TGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTCGCATGGTGACCCCC
GAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGGGCCCGCCCCA
GGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAGAGA
ATCCCGTTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTTAGAAAACCCTAAACTTCCG
GAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGGTTGAGGCCAATGGTG
GGTCTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCAGGAGTGGAAGCGCCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGGAAACTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCGCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATTCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGTAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGACGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGTGCCCCACTGCACCGGCTGAAAGATATCCGG
CTTCTGTATGGAGAGTCACCCTGGGGAGACTCCCCAATTTCTTTTGAAAACTCAGCTCAT
CTCCCCTGCCCCCGAGGCCACGTCATTGCCACCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTC
TGGGGTTACTTCACGGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGATTTCCCAGTTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGAAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCCTCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACTACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAAAAGAAACCGAATATCATGCTTGGGGTGGTATGCGGGGCCCTTGAA
CGTGGAGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGGGGC
CAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGAGGGT
GTAAAGTACATTCTAAAGGTGACCCGGCAGTCTCTGACCATGTTCGTTCTCATCATGAAT
GGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCCTAC
AATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGTACCATCGGC
AATAAGACGTGTGTTTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCCTCGGCT
GGGAAGCTGACACAGATCACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGACGCTAC
GCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGCCGGGTG
AAGTACATCAAGCGTCCAGGTGCGGTGCTGGAAGCAGGCTGCGTGGTGGCCAGGCTGGAG
CTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCTGCCCAG
CAGAACACTGCCGACCTCGGAAAGAAACTGCACAGGGTCTTCCACAGCGTCCTGGGAAGC
CTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCGTTTTTTAGCATAAAGCTGAAG
GAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCTGCTGGACGTGCAG
GAGATCATGACCAGTCGTGCAGGCCGCATCCCCCCCCCTGTTGAGAAGTCTGTCCGCAAG
GTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCCAGCCAGCAG
ATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGATCGAGAGGTC
TTCTTCATCAACACCCAGAGCATGGTGCAGTTGGTCCAGAGGTACCGAAGTGGAATCCGC
GGTCATATGAAAACAGTGGTGATCGATCTCTTGAGAAGATACTTGCGTGTTGAGACCATT
TTCGGCAAGGCAAGAGATGCTGATGCCAACTCCAGTGGGATGGTGGGGGGCGTGAGGAGC
CTGAGCTTTACCTCTGTGTGGGTGGTTTTGTCTCCCCCAGCCCACTACGACAAGTGTGTG
ATAAACCTCAGGGAACAGTTCAAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCC
CACGCACAGGTGACCAAGAAGAACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGC
CCAGACCCTTCCCTGTCGGACGAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGC
AAAAGCGAGCACTGCAAAGTGGCCCTCAGAGCCCGGCAGATCCTGATCGCCTCCCCCTCC
TACGAGCTGCGGCATAACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGC
CACCAGTTCTGCCCCGAGAACCTCCAGAAATTAATACTTTCGGAAACAACCATCTTCGAC
GTCCTGAATACTTTCTTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTT
TACGTGGGGGGGGCTTACATCGCCTATGTGTTAAACAGCCTGCAGCACCGGCAGCTCCCG
GACGGCACCTGCGTGGTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATG
ACCGTGCCCATCAGCATCACCAACCCTGACCTGCTGAGGCACACGACAGAGCTCTTCATG
GACAGCGGCTTCTCCCCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTC
GAGGACTTCACCAGAAATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCGAAAGAC
CCCCCCCTCTTCAGCGAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTC
AGAGAAGAGCCCATCCACATTCTGAATGTGTCCATCCAGTGTGCGGACCACCTGGAGGAT
GAGGCACTGGTGCCGATTTTACGTACATTCGTACAGTCCAAGAAAAATATCCTTGTGGAT
TATGGACTCCGACGAATCCCATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTC
ACATTCAGAGCAAGAGATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCC
CTGGCTTTCCAGCTGGAACTCAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGT
GCCAACCACAAGATGCACCTTTACCTGGGTGCTGCCAAGGTGGAAGGAAGGTATGAAGTG
ACGGACCATAGGTTCTTCATCCGTGCCATCATCAGGCACTCTGACCTGATCACAAAGGAA
GCCTCCTTCGAATACCTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAG
CTGGAGGTGGCGTTCAATAACACCAACGTGCGCACCGACTGCAACCACATCTTCCTCAAC
TTCGTGCCCACTGTCATCATGGACCCCAACAAGATCGAGGAGTCCGTGCGCTACATGGTT
ATGCGCTACGGCAGCCGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAAC
ATCCGCCAGACCACCACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCG
GGCTACTACCTGGACATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATC
ATGTTTCACTCCTTCGGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCC
TACGTCACCAAGGATCTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACC
TACATCTATGACTTCCCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCA
GACAAGTATCCCAAAGACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAG
CTGGTGGAGATGAACCGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATG
AGGTTTAAGACCCAGGAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATC
ACCTTTCGCATTGGATCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAG
ATGGCCCGGGCAGAGGCGATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATT
GGCATGGCAGAGGAGATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCC
CACAAAGGATTTAAATACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTG
AACTCCGTCCACTGTAAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGAT
ATCATCGGGAAGGATGATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCT
GGGGAGTCCTCTCTGGCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCC
ATTGGGATTGGGGCCTACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCC
CACATCATCCTCACAGGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACA
TCCAACAACCAGCTGGGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACC
GTGCCAGATGACTTTGAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAG
GATAATCACAGCCCTGTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAA
TTCCTCCCATCCAGAGCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCA
ACTCTGAAGGGAACGTGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATG
GCACCCTGGGCGCAGACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGA
GTGATTGCTGTGGAGACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTG
GATTCTGAGGCCAAGATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTAC
AAAACCGCCCAGGCCATCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCC
AACTGGAGGGGGTTCTCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGA
GCCTACATCGTGGACGGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCGCCCT
ATGCGGGAGCTCCGGGGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGC
ATAGAAATGTATGCAGACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTG
GAGATTAAGTTCCGAAAGGAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTAC
AAGAAGCTCATGGAACAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTG
GAGGGCCGGCTAAAGGCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTG
CAGTTCGCCGACTTCCATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGAC
ATCCTGGAGTGGAAGACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTG
GAGGACCAGGTCAAGCAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATC
CAGTCCATGCTGCGTCGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGG
GACAACAACCAGGTGGTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCG
CGCTCCACCATCCGTGAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATC
CGAGGCCTGGTTGAAGAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAG
CACATCAGCCCAGCTGAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCG
GCCTCCACCTGA

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

12q24.11

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed ]
Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5248

Enzyme 4 Name

Pyruvate carboxylase, mitochondrial precursor

Enzyme 4 Synonyms

Pyruvic carboxylase
PCB

Enzyme 4 Gene Name

Enzyme 4 Protein Sequence

>Pyruvate carboxylase, mitochondrial precursor

MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE

Enzyme 4 Number of Residues

1178

Enzyme 4 Molecular Weight

129635

Enzyme 4 Theoretical pI

6.83

Enzyme 4 GO Classification

Function
ATP binding adenyl nucleotide binding binding biotin binding catalytic activity ligase activity ligase activity, forming carbon-carbon bonds nucleotide binding purine nucleotide binding pyruvate carboxylase activity vitamin binding
Process
alcohol metabolism cellular metabolism gluconeogenesis glucose metabolism hexose metabolism metabolism monosaccharide metabolism physiological process
Component
cell cytoplasm intracellular

Enzyme 4 General Function

Not Available

Enzyme 4 Specific Function

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate

Enzyme 4 Pathways

Citrate Cycle (map00020 )
Pyruvate Metabolism (map00620 )

Enzyme 4 Reactions

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate

Enzyme 4 Pfam Domain Function

Biotin_carb_C (PF02785 )
Biotin_lipoyl (PF00364 )
CPSase_L_chain (PF00289 )
CPSase_L_D2 (PF02786 )
HMGL-like (PF00682 )
PYC_OADA (PF02436 )

Enzyme 4 Signals

1-21

Enzyme 4 Transmembrane Regions

Not Available

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

458236

Enzyme 4 UniProtKB/Swiss-Prot ID

P11498

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

PYC_HUMAN

Enzyme 4 PDB ID

Not Available

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>3537 bp

ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA

Enzyme 4 GenBank Gene ID

U04641

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

HGNC:8636

Enzyme 4 Chromosome Location

Not Available

Enzyme 4 Locus

Not Available

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed ]
MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [PubMed ]
Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed ]
Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed ]
Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed ]
Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5271

Enzyme 5 Name

Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor

Enzyme 5 Synonyms

Acetate--CoA ligase 2
Acetyl-CoA synthetase 2
Acyl- CoA synthetase short-chain family member 1

Enzyme 5 Gene Name

ACSS1

Enzyme 5 Protein Sequence

>Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor

MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK

Enzyme 5 Number of Residues

689

Enzyme 5 Molecular Weight

74857

Enzyme 5 Theoretical pI

7.11

Enzyme 5 GO Classification

Function
AMP binding CoA-ligase activity acetate-CoA ligase activity adenyl nucleotide binding binding catalytic activity ligase activity ligase activity, forming carbon-sulfur bonds nucleotide binding purine nucleotide binding
Process
metabolism physiological process
Component
—

Enzyme 5 General Function

Lipid transport and metabolism

Enzyme 5 Specific Function

Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2)

Enzyme 5 Pathways

Gluconeogenesis (map00010 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )

Enzyme 5 Reactions

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA

Enzyme 5 Pfam Domain Function

AMP-binding (PF00501 )

Enzyme 5 Signals

1-22

Enzyme 5 Transmembrane Regions

Not Available

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

56203089

Enzyme 5 UniProtKB/Swiss-Prot ID

Q9NUB1

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

ACS2L_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>1439 bp

CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA

Enzyme 5 GenBank Gene ID

AL035661

Enzyme 5 GeneCard ID

ACSS1

Enzyme 5 GenAtlas ID

ACSS1

Enzyme 5 HGNC ID

HGNC:16091 Link Image

Enzyme 5 Chromosome Location

Enzyme 5 Locus

20p11.23-p11.21

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed ]
Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5276

Enzyme 6 Name

Acetyl-CoA carboxylase 1

Enzyme 6 Synonyms

ACC-alpha[Includes: Biotin carboxylase

Enzyme 6 Gene Name

ACACA

Enzyme 6 Protein Sequence

>Acetyl-CoA carboxylase 1

MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST

Enzyme 6 Number of Residues

2346

Enzyme 6 Molecular Weight

265557

Enzyme 6 Theoretical pI

6.32

Enzyme 6 GO Classification

Function
ATP binding adenyl nucleotide binding binding biotin binding catalytic activity ligase activity nucleotide binding purine nucleotide binding vitamin binding
Process
metabolism physiological process
Component
—

Enzyme 6 General Function

Lipid transport and metabolism

Enzyme 6 Specific Function

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase

Enzyme 6 Pathways

Fatty Acid Biosynthesis (map00061 )
Propanoate Metabolism (map00640 )
Pyruvate Metabolism (map00620 )
Tetracycline biosynthesis (map00253 )

Enzyme 6 Reactions

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA

Enzyme 6 Pfam Domain Function

ACC_central (PF08326 )
Biotin_carb_C (PF02785 )
Biotin_lipoyl (PF00364 )
Carboxyl_trans (PF01039 )
CPSase_L_chain (PF00289 )
CPSase_L_D2 (PF02786 )

Enzyme 6 Signals

None

Enzyme 6 Transmembrane Regions

None

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

849083

Enzyme 6 UniProtKB/Swiss-Prot ID

Q13085

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

COA1_HUMAN Link Image

Enzyme 6 PDB ID

Not Available

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>7041 bp

ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCAGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGCTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTGCCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCTGGTCT
GGCTTGCACCTAGTAAAGCAGGGCGGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTCATCGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCGGTGCCTGGA
GGAGCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTGCAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAACCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTAAAGGCA
GCTGAGAAGGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTTAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTAGAATTGAACCCT
CGGCTACAGGTTGAACAACCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCCGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCTTGGGGTGATTCTCCCATTGATTTTGAAAATTCTGCTCACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGGTTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAAGCAATTTCAAACATGGTGGTGGCATTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAAATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACGGGCTGAGCGTCCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTCGGA
GATGTGAGCCTGCGAAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCGGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTACACCACGTATATGAAGGAGGAAGTAGACAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCA
GAGATTGAGGTAATGAAGATGGTAATGACTTTGACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGTCCTGGAGCAGCTCTTGACCCTGGCTGTGTACTCGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACCGCTCTCCGAGGCGAGAAGCTCCATCGAGTGTTCCACTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAACGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTCCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTTCGAGAAGAGAATAAGAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTAACTGATGAGCTGCTG
AGTATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGACGTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTACGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGCGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTT
CTGTTGGACAACGCCTTCACACCACCTTGTCAACGCATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTAATGGGCTGCTTCTGTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACGGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTCACCCAGCAAAATAAAGCTACCCTGGCT
GACCATGGGATCCGGCGCCTGACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAGTGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCCTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTTTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAGCAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACGTACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCAACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGAGCCTTAAAAGTCCTGAATATCCAGAAGGCCGAGATGTTATTGTTATT
GGCAATGACATTACATACCGAATTGGGTCCTTTGGGCCTCAAGAAGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCCGAAGGCATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
TCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCGGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATCGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTCCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTGATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTACGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGACGGCTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTACACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATATGATCCTCGATGGATGCTAGCAGGC
CGCCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACGGTGGTGGTTGGTAGAGCCAGGTTAGGGGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGGACAGTAGAACTAAGTGTACCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCACGCCGGCCAAGTTTGGTTTCCG
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTACCTCTA
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTATCACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGCGGGAATGTTCCCAGCCTGTGCTGGTC
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATCGACCCAACCATC
AATCCTCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACGGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTGAGCCCAACTGAG
CGGAAGGAGTTGGAGAGCAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCAATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACTCCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGACTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAGTGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGACGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGGGCAGAAGTCATAAGGATCCTTTCCACT
ATGGACTCCCCTTCTACGTAG

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

17q21

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed ]
Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5312

Enzyme 7 Name

Thymidylate kinase

Enzyme 7 Synonyms

dTMP kinase

Enzyme 7 Gene Name

DTYMK

Enzyme 7 Protein Sequence

>Thymidylate kinase

MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK

Enzyme 7 Number of Residues

212

Enzyme 7 Molecular Weight

23820

Enzyme 7 Theoretical pI

8.49

Enzyme 7 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding thymidylate kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular metabolism dTDP biosynthesis dTTP biosynthesis metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleotide metabolism physiological process pyrimidine deoxyribonucleoside diphosphate biosynthesis pyrimidine deoxyribonucleoside triphosphate biosynthesis pyrimidine nucleoside diphosphate biosynthesis pyrimidine nucleoside triphosphate biosynthesis pyrimidine nucleotide biosynthesis pyrimidine nucleotide metabolism
Component
—

Enzyme 7 General Function

Nucleotide transport and metabolism

Enzyme 7 Specific Function

Catalyzes the conversion of dTMP to dTDP

Enzyme 7 Pathways

Pyrimidine Metabolism (map00240 )

Enzyme 7 Reactions

ATP + dTMP = ADP + dTDP

Enzyme 7 Pfam Domain Function

Thymidylate_kin (PF02223 )

Enzyme 7 Signals

None

Enzyme 7 Transmembrane Regions

None

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

37206

Enzyme 7 UniProtKB/Swiss-Prot ID

P23919

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

DTYMK_HUMAN Link Image

Enzyme 7 PDB ID

1E9A

Enzyme 7 PDB File

Show

Enzyme 7 3D Structure

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>636 bp

ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA

Enzyme 7 GenBank Gene ID

Enzyme 7 GeneCard ID

Enzyme 7 GenAtlas ID

Enzyme 7 HGNC ID

Enzyme 7 Chromosome Location

Enzyme 7 Locus

2q37.3

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed ]
Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [PubMed ]

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

5313

Enzyme 8 Name

Ectonucleoside triphosphate diphosphohydrolase 1

Enzyme 8 Synonyms

NTPDase 1
Ecto-ATP diphosphohydrolase
ATPDase
Lymphoid cell activation antigen
Ecto-apyrase
CD39 antigen

Enzyme 8 Gene Name

ENTPD1

Enzyme 8 Protein Sequence

>Ectonucleoside triphosphate diphosphohydrolase 1

MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV

Enzyme 8 Number of Residues

510

Enzyme 8 Molecular Weight

57965

Enzyme 8 Theoretical pI

6.29

Enzyme 8 GO Classification

Function
catalytic activity hydrolase activity
Process
—
Component
—

Enzyme 8 General Function

Not Available

Enzyme 8 Specific Function

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well

Enzyme 8 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 8 Reactions

ATP + 2 H2O = AMP + 2 phosphate

Enzyme 8 Pfam Domain Function

GDA1_CD39 (PF01150 )

Enzyme 8 Signals

None

Enzyme 8 Transmembrane Regions

17-37 479-499

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

765256

Enzyme 8 UniProtKB/Swiss-Prot ID

P49961

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

ENTP1_HUMAN Link Image

Enzyme 8 PDB ID

Not Available

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>1533 bp

ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG

Enzyme 8 GenBank Gene ID

Enzyme 8 GeneCard ID

Enzyme 8 GenAtlas ID

Enzyme 8 HGNC ID

Enzyme 8 Chromosome Location

Enzyme 8 Locus

10q24

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed ]
Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed ]
Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed ]
Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed ]
Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed ]
Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed ]
Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed ]
Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

5314

Enzyme 9 Name

Soluble calcium-activated nucleotidase 1

Enzyme 9 Synonyms

SCAN-1
Apyrase homolog
Putative NF-kappa-B-activating protein 107
Putative MAPK-activating protein PM09

Enzyme 9 Gene Name

CANT1

Enzyme 9 Protein Sequence

>Soluble calcium-activated nucleotidase 1

MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI

Enzyme 9 Number of Residues

401

Enzyme 9 Molecular Weight

44840

Enzyme 9 Theoretical pI

5.98

Enzyme 9 GO Classification

Not Available

Enzyme 9 General Function

Not Available

Enzyme 9 Specific Function

Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP

Enzyme 9 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 9 Reactions

A nucleoside diphosphate + H2O = a nucleotide + phosphate

Enzyme 9 Pfam Domain Function

Apyrase (PF06079 )

Enzyme 9 Signals

None

Enzyme 9 Transmembrane Regions

45-62

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

22218108

Enzyme 9 UniProtKB/Swiss-Prot ID

Q8WVQ1

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

CANT1_HUMAN Link Image

Enzyme 9 PDB ID

1S1D

Enzyme 9 PDB File

Show

Enzyme 9 3D Structure

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>1116 bp

ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA

Enzyme 9 GenBank Gene ID

AF328554

Enzyme 9 GeneCard ID

CANT1

Enzyme 9 GenAtlas ID

CANT1

Enzyme 9 HGNC ID

HGNC:19721 Link Image

Enzyme 9 Chromosome Location

Enzyme 9 Locus

17q25.3

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed ]
Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed ]
Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

5317

Enzyme 10 Name

Thymidine kinase, cytosolic

Enzyme 10 Synonyms

Not Available

Enzyme 10 Gene Name

TK1

Enzyme 10 Protein Sequence

>Thymidine kinase, cytosolic

MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR
YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI
VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK
YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN

Enzyme 10 Number of Residues

234

Enzyme 10 Molecular Weight

25469

Enzyme 10 Theoretical pI

8.61

Enzyme 10 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity deoxynucleoside kinase activity kinase activity nucleobase, nucleoside, nucleotide kinase activity nucleoside kinase activity nucleotide binding purine nucleotide binding thymidine kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
—
Component
—

Enzyme 10 General Function

Nucleotide transport and metabolism

Enzyme 10 Specific Function

ATP + thymidine = ADP + thymidine 5'- phosphate

Enzyme 10 Pathways

Pyrimidine Metabolism (map00240 )

Enzyme 10 Reactions

ATP + thymidine = ADP + thymidine 5'-phosphate

Enzyme 10 Pfam Domain Function

TK (PF00265 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

None

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

339709

Enzyme 10 UniProtKB/Swiss-Prot ID

P04183

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

KITH_HUMAN Link Image

Enzyme 10 PDB ID

1XBT

Enzyme 10 PDB File

Show

Enzyme 10 3D Structure

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>705 bp

ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG
ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC
CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC
TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG
CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG
TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT
GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG
CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC
GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG
TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG
GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG
CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA

Enzyme 10 GenBank Gene ID

K02581

Enzyme 10 GeneCard ID

TK1

Enzyme 10 GenAtlas ID

TK1

Enzyme 10 HGNC ID

HGNC:11830 Link Image

Enzyme 10 Chromosome Location

Enzyme 10 Locus

17q23.2-q25.3

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Bradshaw HD Jr, Deininger PL: Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol. 1984 Nov;4(11):2316-20. [PubMed ]
Flemington E, Bradshaw HD Jr, Traina-Dorge V, Slagel V, Deininger PL: Sequence, structure and promoter characterization of the human thymidine kinase gene. Gene. 1987;52(2-3):267-77. [PubMed ]
Chang ZF, Huang DY, Chi LM: Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J Biol Chem. 1998 May 15;273(20):12095-100. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

5338

Enzyme 11 Name

Nucleoside diphosphate kinase, mitochondrial precursor

Enzyme 11 Synonyms

NDP kinase, mitochondrial
NDK
nm23-H4
Nucleoside diphosphate kinase D
NDPKD

Enzyme 11 Gene Name

NME4

Enzyme 11 Protein Sequence

>Nucleoside diphosphate kinase, mitochondrial precursor

MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA

Enzyme 11 Number of Residues

187

Enzyme 11 Molecular Weight

20659

Enzyme 11 Theoretical pI

10.75

Enzyme 11 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ion binding magnesium ion binding metal ion binding nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 11 General Function

Nucleotide transport and metabolism

Enzyme 11 Specific Function

Major role in the synthesis of nucleoside triphosphates other than ATP

Enzyme 11 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 11 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 11 Pfam Domain Function

NDK (PF00334 )

Enzyme 11 Signals

1-15

Enzyme 11 Transmembrane Regions

Not Available

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

1945762

Enzyme 11 UniProtKB/Swiss-Prot ID

O00746

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

NDKM_HUMAN Link Image

Enzyme 11 PDB ID

1EHW

Enzyme 11 PDB File

Show

Enzyme 11 3D Structure

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

>564 bp

ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA

Enzyme 11 GenBank Gene ID

Y07604

Enzyme 11 GeneCard ID

NME4

Enzyme 11 GenAtlas ID

NME4

Enzyme 11 HGNC ID

HGNC:7852

Enzyme 11 Chromosome Location

Enzyme 11 Locus

16p13.3

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed ]
Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]
Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

5340

Enzyme 12 Name

Ribonucleoside-diphosphate reductase large subunit

Enzyme 12 Synonyms

Ribonucleoside-diphosphate reductase M1 subunit
Ribonucleotide reductase large chain

Enzyme 12 Gene Name

RRM1

Enzyme 12 Protein Sequence

>Ribonucleoside-diphosphate reductase large subunit

MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS

Enzyme 12 Number of Residues

792

Enzyme 12 Molecular Weight

90071

Enzyme 12 Theoretical pI

7.16

Enzyme 12 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on CH2 groups oxidoreductase activity, acting on CH2 groups, disulfide as acceptor ribonucleoside-diphosphate reductase activity
Process
DNA metabolism DNA replication cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism physiological process
Component
protein complex ribonucleoside-diphosphate reductase complex

Enzyme 12 General Function

Nucleotide transport and metabolism

Enzyme 12 Specific Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides

Enzyme 12 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 12 Reactions

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin

Enzyme 12 Pfam Domain Function

ATP-cone (PF03477 )
Ribonuc_red_lgC (PF02867 )
Ribonuc_red_lgN (PF00317 )

Enzyme 12 Signals

None

Enzyme 12 Transmembrane Regions

None

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

36065

Enzyme 12 UniProtKB/Swiss-Prot ID

P23921

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

RIR1_HUMAN Link Image

Enzyme 12 PDB ID

Not Available

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

>2379 bp

ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA

Enzyme 12 GenBank Gene ID

X59543

Enzyme 12 GeneCard ID

RRM1

Enzyme 12 GenAtlas ID

RRM1

Enzyme 12 HGNC ID

HGNC:10451 Link Image

Enzyme 12 Chromosome Location

Enzyme 12 Locus

11p15.5

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed ]
Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed ]
Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed ]

Enzyme 12 Metabolite References

Not Available

Enzyme 13 [top]

Enzyme 13 ID

5341

Enzyme 13 Name

Nucleoside diphosphate kinase A

Enzyme 13 Synonyms

NDK A
NDP kinase A
Tumor metastatic process-associated protein
Metastasis inhibition factor nm23
nm23-H1
Granzyme A-activated DNase
GAAD

Enzyme 13 Gene Name

NME1

Enzyme 13 Protein Sequence

>Nucleoside diphosphate kinase A

MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE

Enzyme 13 Number of Residues

152

Enzyme 13 Molecular Weight

17149

Enzyme 13 Theoretical pI

6.11

Enzyme 13 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ion binding magnesium ion binding metal ion binding nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 13 General Function

Nucleotide transport and metabolism

Enzyme 13 Specific Function

Major role in the synthesis of nucleoside triphosphates other than ATP

Enzyme 13 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 13 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 13 Pfam Domain Function

NDK (PF00334 )

Enzyme 13 Signals

None

Enzyme 13 Transmembrane Regions

None

Enzyme 13 Essentiality

Not Available

Enzyme 13 GenBank ID Protein

35068

Enzyme 13 UniProtKB/Swiss-Prot ID

P15531

Enzyme 13 UniProtKB/Swiss-Prot Entry Name

NDKA_HUMAN Link Image

Enzyme 13 PDB ID

1JXV

Enzyme 13 PDB File

Show

Enzyme 13 3D Structure

Enzyme 13 Cellular Location

Not Available

Enzyme 13 Gene Sequence

>543 bp

TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA

Enzyme 13 GenBank Gene ID

X17620

Enzyme 13 GeneCard ID

NME1

Enzyme 13 GenAtlas ID

NME1

Enzyme 13 HGNC ID

HGNC:7849

Enzyme 13 Chromosome Location

Enzyme 13 Locus

17q21.3

Enzyme 13 SNPs

SNPJam Report Link Image

Enzyme 13 General References

Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed ]
Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed ]
Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed ]
Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed ]
Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed ]
Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed ]
Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed ]
Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed ]
Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed ]

Enzyme 13 Metabolite References

Not Available

Enzyme 14 [top]

Enzyme 14 ID

5342

Enzyme 14 Name

Nucleoside diphosphate kinase 7

Enzyme 14 Synonyms

NDK 7
NDP kinase 7
nm23-H7

Enzyme 14 Gene Name

NME7

Enzyme 14 Protein Sequence

>Nucleoside diphosphate kinase 7

MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN

Enzyme 14 Number of Residues

376

Enzyme 14 Molecular Weight

42492

Enzyme 14 Theoretical pI

6.44

Enzyme 14 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 14 General Function

Nucleotide transport and metabolism

Enzyme 14 Specific Function

Enzyme 14 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 14 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 14 Pfam Domain Function

NDK (PF00334 )

Enzyme 14 Signals

None

Enzyme 14 Transmembrane Regions

None

Enzyme 14 Essentiality

Not Available

Enzyme 14 GenBank ID Protein

4960169

Enzyme 14 UniProtKB/Swiss-Prot ID

Q9Y5B8

Enzyme 14 UniProtKB/Swiss-Prot Entry Name

NDK7_HUMAN Link Image

Enzyme 14 PDB ID

Not Available

Enzyme 14 Cellular Location

Not Available

Enzyme 14 Gene Sequence

>1131 bp

ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG

Enzyme 14 GenBank Gene ID

AF153191

Enzyme 14 GeneCard ID

NME7

Enzyme 14 GenAtlas ID

NME7

Enzyme 14 HGNC ID

HGNC:20461 Link Image

Enzyme 14 Chromosome Location

Enzyme 14 Locus

1q24

Enzyme 14 SNPs

SNPJam Report Link Image

Enzyme 14 General References

Not Available

Enzyme 14 Metabolite References

Not Available

Enzyme 15 [top]

Enzyme 15 ID

5343

Enzyme 15 Name

Ribonucleoside-diphosphate reductase M2 subunit

Enzyme 15 Synonyms

Ribonucleotide reductase small subunit
Ribonucleotide reductase small chain

Enzyme 15 Gene Name

RRM2

Enzyme 15 Protein Sequence

>Ribonucleoside-diphosphate reductase M2 subunit

MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF

Enzyme 15 Number of Residues

389

Enzyme 15 Molecular Weight

44878

Enzyme 15 Theoretical pI

5.05

Enzyme 15 GO Classification

Function
catalytic activity oxidoreductase activity oxidoreductase activity, acting on CH2 groups oxidoreductase activity, acting on CH2 groups, disulfide as acceptor ribonucleoside-diphosphate reductase activity
Process
cellular metabolism deoxyribonucleoside diphosphate metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside diphosphate metabolism nucleotide metabolism physiological process
Component
—

Enzyme 15 General Function

Nucleotide transport and metabolism

Enzyme 15 Specific Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides

Enzyme 15 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 15 Reactions

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin

Enzyme 15 Pfam Domain Function

Ribonuc_red_sm (PF00268 )

Enzyme 15 Signals

None

Enzyme 15 Transmembrane Regions

None

Enzyme 15 Essentiality

Not Available

Enzyme 15 GenBank ID Protein

36155

Enzyme 15 UniProtKB/Swiss-Prot ID

P31350

Enzyme 15 UniProtKB/Swiss-Prot Entry Name

RIR2_HUMAN Link Image

Enzyme 15 PDB ID

1H0N

Enzyme 15 PDB File

Show

Enzyme 15 3D Structure

Enzyme 15 Cellular Location

Not Available

Enzyme 15 Gene Sequence

>1170 bp

ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA

Enzyme 15 GenBank Gene ID

X59618

Enzyme 15 GeneCard ID

RRM2

Enzyme 15 GenAtlas ID

RRM2

Enzyme 15 HGNC ID

HGNC:10452 Link Image

Enzyme 15 Chromosome Location

Enzyme 15 Locus

2p25-p24

Enzyme 15 SNPs

SNPJam Report Link Image

Enzyme 15 General References

Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed ]

Enzyme 15 Metabolite References

Not Available

Enzyme 16 [top]

Enzyme 16 ID

5344

Enzyme 16 Name

Nucleoside diphosphate kinase B

Enzyme 16 Synonyms

NDK B
NDP kinase B
nm23-H2
C-myc purine-binding transcription factor PUF

Enzyme 16 Gene Name

NME2

Enzyme 16 Protein Sequence

>Nucleoside diphosphate kinase B

MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE

Enzyme 16 Number of Residues

152

Enzyme 16 Molecular Weight

17298

Enzyme 16 Theoretical pI

8.69

Enzyme 16 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ion binding magnesium ion binding metal ion binding nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 16 General Function

Nucleotide transport and metabolism

Enzyme 16 Specific Function

Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)

Enzyme 16 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 16 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 16 Pfam Domain Function

NDK (PF00334 )

Enzyme 16 Signals

None

Enzyme 16 Transmembrane Regions

None

Enzyme 16 Essentiality

Not Available

Enzyme 16 GenBank ID Protein

4467843

Enzyme 16 UniProtKB/Swiss-Prot ID

P22392

Enzyme 16 UniProtKB/Swiss-Prot Entry Name

NDKB_HUMAN Link Image

Enzyme 16 PDB ID

1NSK

Enzyme 16 PDB File

Show

Enzyme 16 3D Structure

Enzyme 16 Cellular Location

Not Available

Enzyme 16 Gene Sequence

>459 bp

ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA

Enzyme 16 GenBank Gene ID

X58965

Enzyme 16 GeneCard ID

NME2

Enzyme 16 GenAtlas ID

NME2

Enzyme 16 HGNC ID

HGNC:7850

Enzyme 16 Chromosome Location

Enzyme 16 Locus

17q21.3

Enzyme 16 SNPs

SNPJam Report Link Image

Enzyme 16 General References

Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed ]
Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed ]
Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed ]
Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed ]
Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed ]

Enzyme 16 Metabolite References

Not Available

Enzyme 17 [top]

Enzyme 17 ID

5345

Enzyme 17 Name

Nucleoside diphosphate kinase 3

Enzyme 17 Synonyms

NDK 3
NDP kinase 3
Nucleoside diphosphate kinase C
NDPKC
nm23-H3
DR-nm23

Enzyme 17 Gene Name

NME3

Enzyme 17 Protein Sequence

>Nucleoside diphosphate kinase 3

MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE

Enzyme 17 Number of Residues

169

Enzyme 17 Molecular Weight

19015

Enzyme 17 Theoretical pI

7.97

Enzyme 17 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ion binding magnesium ion binding metal ion binding nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 17 General Function

Nucleotide transport and metabolism

Enzyme 17 Specific Function

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis

Enzyme 17 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 17 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 17 Pfam Domain Function

NDK (PF00334 )

Enzyme 17 Signals

1-19

Enzyme 17 Transmembrane Regions

Not Available

Enzyme 17 Essentiality

Not Available

Enzyme 17 GenBank ID Protein

1051256

Enzyme 17 UniProtKB/Swiss-Prot ID

Q13232

Enzyme 17 UniProtKB/Swiss-Prot Entry Name

NDK3_HUMAN Link Image

Enzyme 17 PDB ID

Not Available

Enzyme 17 Cellular Location

Not Available

Enzyme 17 Gene Sequence

>507 bp

ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG

Enzyme 17 GenBank Gene ID

U29656

Enzyme 17 GeneCard ID

NME3

Enzyme 17 GenAtlas ID

NME3

Enzyme 17 HGNC ID

HGNC:7851

Enzyme 17 Chromosome Location

Enzyme 17 Locus

16q13

Enzyme 17 SNPs

SNPJam Report Link Image

Enzyme 17 General References

Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed ]
Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]

Enzyme 17 Metabolite References

Not Available

Enzyme 18 [top]

Enzyme 18 ID

5346

Enzyme 18 Name

Nucleoside diphosphate kinase 6

Enzyme 18 Synonyms

NDK 6
NDP kinase 6
nm23-H6
Inhibitor of p53-induced apoptosis-alpha
IPIA-alpha

Enzyme 18 Gene Name

NME6

Enzyme 18 Protein Sequence

>Nucleoside diphosphate kinase 6

MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA

Enzyme 18 Number of Residues

186

Enzyme 18 Molecular Weight

21142

Enzyme 18 Theoretical pI

8.49

Enzyme 18 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity ion binding magnesium ion binding metal ion binding nucleoside diphosphate kinase activity nucleotide binding phosphotransferase activity, phosphate group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
CTP biosynthesis GTP biosynthesis UTP biosynthesis cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleoside triphosphate biosynthesis nucleoside triphosphate metabolism nucleotide metabolism physiological process purine nucleoside triphosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside triphosphate biosynthesis pyrimidine ribonucleoside triphosphate biosynthesis ribonucleoside triphosphate biosynthesis
Component
—

Enzyme 18 General Function

Nucleotide transport and metabolism

Enzyme 18 Specific Function

Enzyme 18 Pathways

Purine Metabolism (map00230 )
Pyrimidine Metabolism (map00240 )

Enzyme 18 Reactions

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate

Enzyme 18 Pfam Domain Function

NDK (PF00334 )

Enzyme 18 Signals

1-24

Enzyme 18 Transmembrane Regions

Not Available

Enzyme 18 Essentiality

Not Available

Enzyme 18 GenBank ID Protein

3228530

Enzyme 18 UniProtKB/Swiss-Prot ID

O75414

Enzyme 18 UniProtKB/Swiss-Prot Entry Name

NDK6_HUMAN Link Image

Enzyme 18 PDB ID

Not Available

Enzyme 18 Cellular Location

Not Available

Enzyme 18 Gene Sequence

>561 bp

ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA

Enzyme 18 GenBank Gene ID

AF051941

Enzyme 18 GeneCard ID

NME6

Enzyme 18 GenAtlas ID

NME6

Enzyme 18 HGNC ID

HGNC:20567 Link Image

Enzyme 18 Chromosome Location

Enzyme 18 Locus

3p21

Enzyme 18 SNPs

SNPJam Report Link Image

Enzyme 18 General References

Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed ]

Enzyme 18 Metabolite References

Not Available

Enzyme 19 [top]

Enzyme 19 ID

5442

Enzyme 19 Name

Glucokinase

Enzyme 19 Synonyms

Hexokinase-4
Hexokinase type IV
HK IV
HK4
Hexokinase-D

Enzyme 19 Gene Name

GCK

Enzyme 19 Protein Sequence

>Glucokinase

MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ

Enzyme 19 Number of Residues

465

Enzyme 19 Molecular Weight

52192

Enzyme 19 Theoretical pI

4.85

Enzyme 19 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity hexokinase activity nucleotide binding phosphotransferase activity, alcohol group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 19 General Function

Not Available

Enzyme 19 Specific Function

Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage

Enzyme 19 Pathways

Galactose Metabolism (map00052 )
Gluconeogenesis (map00010 )
Starch and Sucrose Metabolism (map00500 )
Streptomycin biosynthesis (map00521 )

Enzyme 19 Reactions

ATP + D-glucose = ADP + D-glucose 6-phosphate

Enzyme 19 Pfam Domain Function

Hexokinase_1 (PF00349 )
Hexokinase_2 (PF03727 )

Enzyme 19 Signals

None

Enzyme 19 Transmembrane Regions

None

Enzyme 19 Essentiality

Not Available

Enzyme 19 GenBank ID Protein

179427

Enzyme 19 UniProtKB/Swiss-Prot ID

P35557

Enzyme 19 UniProtKB/Swiss-Prot Entry Name

HXK4_HUMAN Link Image

Enzyme 19 PDB ID

1V4T

Enzyme 19 PDB File

Show

Enzyme 19 3D Structure

Enzyme 19 Cellular Location

Not Available

Enzyme 19 Gene Sequence

>1398 bp

ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA

Enzyme 19 GenBank Gene ID

M88011

Enzyme 19 GeneCard ID

GCK

Enzyme 19 GenAtlas ID

GCK

Enzyme 19 HGNC ID

HGNC:4195

Enzyme 19 Chromosome Location

Enzyme 19 Locus

7p15.3-p15.1

Enzyme 19 SNPs

SNPJam Report Link Image

Enzyme 19 General References

Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed ]
Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed ]
Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed ]
Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed ]
Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed ]
Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed ]
St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed ]
Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed ]
Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed ]
Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed ]
Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed ]
Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed ]
Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed ]
Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed ]
Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed ]
Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed ]
Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed ]
Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed ]
Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed ]

Enzyme 19 Metabolite References

Not Available

Enzyme 20 [top]

Enzyme 20 ID

5444

Enzyme 20 Name

Hexokinase-3

Enzyme 20 Synonyms

Hexokinase type III
HK III

Enzyme 20 Gene Name

HK3

Enzyme 20 Protein Sequence

>Hexokinase-3

MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV

Enzyme 20 Number of Residues

923

Enzyme 20 Molecular Weight

98921

Enzyme 20 Theoretical pI

5.11

Enzyme 20 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity hexokinase activity nucleotide binding phosphotransferase activity, alcohol group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 20 General Function

Not Available

Enzyme 20 Specific Function

ATP + D-hexose = ADP + D-hexose 6-phosphate

Enzyme 20 Pathways

Aminosugars metabolism (map00530 )
Fructose and Mannose Metabolism (map00051 )
Galactose Metabolism (map00052 )
Gluconeogenesis (map00010 )
Starch and Sucrose Metabolism (map00500 )
Streptomycin biosynthesis (map00521 )

Enzyme 20 Reactions

ATP + D-hexose = ADP + D-hexose 6-phosphate

Enzyme 20 Pfam Domain Function

Hexokinase_1 (PF00349 )
Hexokinase_2 (PF03727 )

Enzyme 20 Signals

None

Enzyme 20 Transmembrane Regions

None

Enzyme 20 Essentiality

Not Available

Enzyme 20 GenBank ID Protein

1255788

Enzyme 20 UniProtKB/Swiss-Prot ID

P52790

Enzyme 20 UniProtKB/Swiss-Prot Entry Name

HXK3_HUMAN Link Image

Enzyme 20 PDB ID

Not Available

Enzyme 20 Cellular Location

Not Available

Enzyme 20 Gene Sequence

>2772 bp

ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA

Enzyme 20 GenBank Gene ID

U51333

Enzyme 20 GeneCard ID

HK3

Enzyme 20 GenAtlas ID

HK3

Enzyme 20 HGNC ID

HGNC:4925

Enzyme 20 Chromosome Location

Enzyme 20 Locus

5q35.2

Enzyme 20 SNPs

SNPJam Report Link Image

Enzyme 20 General References

Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed ]
Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed ]

Enzyme 20 Metabolite References

Not Available

Enzyme 21 [top]

Enzyme 21 ID

5445

Enzyme 21 Name

Hexokinase-2

Enzyme 21 Synonyms

Hexokinase type II
HK II
Muscle form hexokinase

Enzyme 21 Gene Name

HK2

Enzyme 21 Protein Sequence

>Hexokinase-2

MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR

Enzyme 21 Number of Residues

917

Enzyme 21 Molecular Weight

102381

Enzyme 21 Theoretical pI

5.93

Enzyme 21 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity hexokinase activity nucleotide binding phosphotransferase activity, alcohol group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 21 General Function

Not Available

Enzyme 21 Specific Function

ATP + D-hexose = ADP + D-hexose 6-phosphate

Enzyme 21 Pathways

Aminosugars metabolism (map00530 )
Fructose and Mannose Metabolism (map00051 )
Galactose Metabolism (map00052 )
Gluconeogenesis (map00010 )
Starch and Sucrose Metabolism (map00500 )
Streptomycin biosynthesis (map00521 )

Enzyme 21 Reactions

ATP + D-hexose = ADP + D-hexose 6-phosphate

Enzyme 21 Pfam Domain Function

Hexokinase_1 (PF00349 )
Hexokinase_2 (PF03727 )

Enzyme 21 Signals

None

Enzyme 21 Transmembrane Regions

None

Enzyme 21 Essentiality

Not Available

Enzyme 21 GenBank ID Protein

587202

Enzyme 21 UniProtKB/Swiss-Prot ID

P52789

Enzyme 21 UniProtKB/Swiss-Prot Entry Name

HXK2_HUMAN Link Image

Enzyme 21 PDB ID

Not Available

Enzyme 21 Cellular Location

Not Available

Enzyme 21 Gene Sequence

>2754 bp

ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG

Enzyme 21 GenBank Gene ID

Z46376

Enzyme 21 GeneCard ID

HK2

Enzyme 21 GenAtlas ID

HK2

Enzyme 21 HGNC ID

HGNC:4923

Enzyme 21 Chromosome Location

Enzyme 21 Locus

2p13

Enzyme 21 SNPs

SNPJam Report Link Image

Enzyme 21 General References

Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed ]
Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed ]
Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed ]
Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed ]
Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed ]
Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed ]

Enzyme 21 Metabolite References

Not Available

Enzyme 22 [top]

Enzyme 22 ID

5465

Enzyme 22 Name

Diacylglycerol kinase alpha

Enzyme 22 Synonyms

Diglyceride kinase alpha
DGK-alpha
DAG kinase alpha
80 kDa diacylglycerol kinase

Enzyme 22 Gene Name

DGKA

Enzyme 22 Protein Sequence

>Diacylglycerol kinase alpha

MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS

Enzyme 22 Number of Residues

735

Enzyme 22 Molecular Weight

82673

Enzyme 22 Theoretical pI

6.71

Enzyme 22 GO Classification

Function
binding calcium ion binding catalytic activity cation binding diacylglycerol kinase activity ion binding kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
G-protein coupled receptor protein signaling pathway G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) cell communication cell surface receptor linked signal transduction cellular process intracellular signaling cascade protein kinase C activation signal transduction
Component
—

Enzyme 22 General Function

Not Available

Enzyme 22 Specific Function

Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity

Enzyme 22 Pathways

Glycerolipid Metabolism (map00561 )
Phospholipid Synthesis (map00564 )
Phosphatidylinositol signaling system (map04070 )

Enzyme 22 Reactions

ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate

Enzyme 22 Pfam Domain Function

C1_1 (PF00130 )
DAGK_acc (PF00609 )
DAGK_cat (PF00781 )
efhand (PF00036 )

Enzyme 22 Signals

None

Enzyme 22 Transmembrane Regions

None

Enzyme 22 Essentiality

Not Available

Enzyme 22 GenBank ID Protein

30823

Enzyme 22 UniProtKB/Swiss-Prot ID

P23743

Enzyme 22 UniProtKB/Swiss-Prot Entry Name

DGKA_HUMAN Link Image

Enzyme 22 PDB ID

Not Available

Enzyme 22 Cellular Location

Not Available

Enzyme 22 Gene Sequence

>2208 bp

ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA

Enzyme 22 GenBank Gene ID

X62535

Enzyme 22 GeneCard ID

DGKA

Enzyme 22 GenAtlas ID

DGKA

Enzyme 22 HGNC ID

HGNC:2849

Enzyme 22 Chromosome Location

Enzyme 22 Locus

12q13.3

Enzyme 22 SNPs

SNPJam Report Link Image

Enzyme 22 General References

Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed ]
Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed ]
Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed ]

Enzyme 22 Metabolite References

Not Available

Enzyme 23 [top]

Enzyme 23 ID

5466

Enzyme 23 Name

Diacylglycerol kinase delta

Enzyme 23 Synonyms

Diglyceride kinase delta
DGK-delta
DAG kinase delta
130 kDa diacylglycerol kinase

Enzyme 23 Gene Name

DGKD

Enzyme 23 Protein Sequence

>Diacylglycerol kinase delta

MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA

Enzyme 23 Number of Residues

1214

Enzyme 23 Molecular Weight

134527

Enzyme 23 Theoretical pI

7.58

Enzyme 23 GO Classification

Function
catalytic activity diacylglycerol kinase activity kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
G-protein coupled receptor protein signaling pathway G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) cell communication cell surface receptor linked signal transduction cellular process intracellular signaling cascade protein kinase C activation signal transduction
Component
—

Enzyme 23 General Function

Not Available

Enzyme 23 Specific Function

May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis

Enzyme 23 Pathways

Glycerolipid Metabolism (map00561 )
Phospholipid Synthesis (map00564 )
Phosphatidylinositol signaling system (map04070 )

Enzyme 23 Reactions

ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate

Enzyme 23 Pfam Domain Function

C1_1 (PF00130 )
DAGK_acc (PF00609 )
DAGK_cat (PF00781 )
PH (PF00169 )
SAM_2 (PF07647 )

Enzyme 23 Signals

None

Enzyme 23 Transmembrane Regions

None

Enzyme 23 Essentiality

Not Available

Enzyme 23 GenBank ID Protein

22773821

Enzyme 23 UniProtKB/Swiss-Prot ID

Q16760

Enzyme 23 UniProtKB/Swiss-Prot Entry Name

DGKD_HUMAN Link Image

Enzyme 23 PDB ID

Not Available

Enzyme 23 Cellular Location

Not Available

Enzyme 23 Gene Sequence

>3645 bp

ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG

Enzyme 23 GenBank Gene ID

AB078966

Enzyme 23 GeneCard ID

DGKD

Enzyme 23 GenAtlas ID

DGKD

Enzyme 23 HGNC ID

HGNC:2851

Enzyme 23 Chromosome Location

Enzyme 23 Locus

2q37.1

Enzyme 23 SNPs

SNPJam Report Link Image

Enzyme 23 General References

Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed ]
Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed ]
Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [PubMed ]

Enzyme 23 Metabolite References

Not Available

Enzyme 24 [top]

Enzyme 24 ID

5472

Enzyme 24 Name

Diacylglycerol kinase iota

Enzyme 24 Synonyms

Diglyceride kinase iota
DGK-iota
DAG kinase iota

Enzyme 24 Gene Name

DGKI

Enzyme 24 Protein Sequence

>Diacylglycerol kinase iota

MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV

Enzyme 24 Number of Residues

1065

Enzyme 24 Molecular Weight

116998

Enzyme 24 Theoretical pI

7.81

Enzyme 24 GO Classification

Function
catalytic activity diacylglycerol kinase activity kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
G-protein coupled receptor protein signaling pathway G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) cell communication cell surface receptor linked signal transduction cellular process intracellular signaling cascade protein kinase C activation signal transduction
Component
—

Enzyme 24 General Function

Not Available

Enzyme 24 Specific Function

ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate

Enzyme 24 Pathways

Glycerolipid Metabolism (map00561 )
Phospholipid Synthesis (map00564 )
Phosphatidylinositol signaling system (map04070 )

Enzyme 24 Reactions

ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate

Enzyme 24 Pfam Domain Function

Ank (PF00023 )
C1_1 (PF00130 )
DAGK_acc (PF00609 )
DAGK_cat (PF00781 )

Enzyme 24 Signals

None

Enzyme 24 Transmembrane Regions

None

Enzyme 24 Essentiality

Not Available

Enzyme 24 GenBank ID Protein

3676530

Enzyme 24 UniProtKB/Swiss-Prot ID

O75912

Enzyme 24 UniProtKB/Swiss-Prot Entry Name

DGKI_HUMAN Link Image

Enzyme 24 PDB ID

Not Available

Enzyme 24 Cellular Location

Not Available

Enzyme 24 Gene Sequence

>3198 bp

ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA

Enzyme 24 GenBank Gene ID

AF061936

Enzyme 24 GeneCard ID

DGKI

Enzyme 24 GenAtlas ID

DGKI

Enzyme 24 HGNC ID

HGNC:2855

Enzyme 24 Chromosome Location

Not Available

Enzyme 24 Locus

Not Available

Enzyme 24 SNPs

SNPJam Report Link Image

Enzyme 24 General References

Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed ]
Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed ]

Enzyme 24 Metabolite References

Not Available

Enzyme 25 [top]

Enzyme 25 ID

5478

Enzyme 25 Name

Diacylglycerol kinase zeta

Enzyme 25 Synonyms

Diglyceride kinase zeta
DGK-zeta
DAG kinase zeta

Enzyme 25 Gene Name

DGKZ

Enzyme 25 Protein Sequence

>Diacylglycerol kinase zeta

METFFRRHFRGKVPGPGEGQRRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYVRRASSHCCPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV

Enzyme 25 Number of Residues

1117

Enzyme 25 Molecular Weight

124124

Enzyme 25 Theoretical pI

9.27

Enzyme 25 GO Classification

Function
catalytic activity diacylglycerol kinase activity kinase activity transferase activity transferase activity, transferring phosphorus-containing groups
Process
G-protein coupled receptor protein signaling pathway G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) cell communication cell surface receptor linked signal transduction cellular process intracellular signaling cascade protein kinase C activation signal transduction
Component
—

Enzyme 25 General Function

Not Available

Enzyme 25 Specific Function

Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols

Enzyme 25 Pathways

Glycerolipid Metabolism (map00561 )
Phospholipid Synthesis (map00564 )
Phosphatidylinositol signaling system (map04070 )

Enzyme 25 Reactions

ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate

Enzyme 25 Pfam Domain Function

Ank (PF00023 )
C1_1 (PF00130 )
DAGK_acc (PF00609 )
DAGK_cat (PF00781 )

Enzyme 25 Signals

None

Enzyme 25 Transmembrane Regions

None

Enzyme 25 Essentiality

Not Available

Enzyme 25 GenBank ID Protein

1293079

Enzyme 25 UniProtKB/Swiss-Prot ID

Q13574

Enzyme 25 UniProtKB/Swiss-Prot Entry Name

DGKZ_HUMAN Link Image

Enzyme 25 PDB ID

Not Available

Enzyme 25 Cellular Location

Not Available

Enzyme 25 Gene Sequence

>2787 bp

ATGGAGCCGCGGGACGGTAGCCCCGAGGCCCGGAGCAGCGACTCCGAGTCGGCTTCCGCC
TCGTCCAGCGGCTCCGAGCGCGACGCCGGTCCCGAGCCGGACAAGGCGCCGCGGCGACTC
AACAAGCGGCGCTTCCCGGGGCTGCGGCTCTTCGGGCACAGGAAAGCCATCACCAAGTCG
GGCCTCCAGCACCTGGCCCCCCCTCCGCCCACCCCTGGGGCCCCGTGCAGCGAGTCAGAG
CGGCAGATCCGGAGTACAGTGGACTGGAGCGAGTCAGCGACATATGGGGAGCACATCTGG
TTCGAGACCAACGTGTCCGGGGACTTCTGCTACGTTGGGGAGCAGTACTGTGTAGCCAGG
ATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCAGCCTGCAAGATTGTGGTGCACACGCCC
TGCATCGAGCAGCTGGAGAAGATAAATTTCCGCTGTAAGCCGTCCTTCCGTGAATCAGGC
TCCAGGAATGTCCGCGAGCCAACCTTTGTACGGCACCACTGGGTACACAGACGACGCCAG
GACGGCAAGTGTCGGCACTGTGGGAAGGGATTCCAGCAGAAGTTCACCTTCCACAGCAAG
GAGATTGTGGCCATCAGCTGCTCGTGGTGCAAGCAGGCATACCACAGCAAGGTGTCCTGC
TTCATGCTGCAGCAGATCGAGGAGCCGTGCTCGCTGGGGGTCCACGCAGCCGTGGTCATC
CCGCCCACCTGGATCCTCCGCGCCCGGAGGCCCCAGAATACTCTGAAAGCAAGCAAGAAG
AAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGCAAGAAAGGGCCTGAGGAGGGCCGCTGG
AGACCCTTCATCATCAGGCCCACCCCCTCCCCGCTCATGAAGCCCCTGCTGGTGTTTGTG
AACCCCAAGAGTGGGGGCAACCAGGGTGCAAAGATCATCCAGTCTTTCCTCTGGTATCTC
AATCCCCGACAAGTCTTCGACCTGAGCCAGGGAGGGCCCAAGGAGGCGCTGGAGATGTAC
CGCAAAGTGCACAACCTGCGGATCCTGGCGTGCGGGGGCGACGGCACGGTGGGCTGGATC
CTCTCCACCCTGGACCAGCTACGCCTGAAGCCGCCACCCCCTGTTGCCATCCTGCCCCTG
GGTACTGGCAACGACTTGGCCCGAACCCTCAACTGGGGTGGGGGCTACACAGATGAGCCT
GTGTCCAAGATCCTCTCCCACGTGGAGGAGGGGAACGTGGTACAGCTGGACCGCTGGGAC
CTCCACGCTGAGCCCAACCCCGAGGCAGGGCCTGAGGACCGAGATGAAGGCGCCACCGAC
CGGTTGCCCCTGGATGTCTTCAACAACTACTTCAGCCTGGGCTTTGACGCCCACGTCACC
CTGGAGTTCCACGAGTCTCGAGAGGCCAACCCAGAGAAATTCAACAGCCGCTTTCGGAAT
AAGATGTTCTACGCCGGGACAGCTTTCTCTGACTTCCTGATGGGCAGCTCCAAGGACCTG
GCCAAGCACATCCGAGTGGTGTGTGATGGAATGGACTTGACTCCCAAGATCCAGGACCTG
AAACCCCAGTGTGTTGTTTTCCTGAACATCCCCAGGTACTGTGCGGGCACCATGCCCTGG
GGCCACCCTGGGGAGCACCACGACTTTGAGCCCCAGCGGCATGACGACGGCTACCTCGAG
GTCATTGGCTTCACCATGACGTCGTTGGCCGCGCTGCAGGTGGGCGGACACGGCGAGCGG
CTGACGCAGTGTCGCGAGGTGGTGCTCACCACATCCAAGGCCATCCCGGTGCAGGTGGAT
GGCGAGCCCTGCAAGCTTGCAGCCTCACGCATCCGCATCGCCCTGCGCAACCAGGCCACC
ATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCCCCCCTGCACAGCGACCAGCAGCCGGTG
CCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTCAGCATGCACGACTATGAGGCCCTGCAC
TACGACAAGGAGCAGCTCAAGGAGGCCTCTGTGCCGCTGGGCACTGTGGTGGTCCCAGGA
GACAGTGACCTAGAGCTCTGCCGTGCCCACATTGAGAGACTCCAGCAGGAGCCCGATGGT
GCTGGAGCCAAGTCCCCGACATGCCAGAAACTGTCCCCCAAGTGGTGCTTCCTGGACGCC
ACCACTGCCAGCCGCTTCTACAGGATCGACCGAGCCCAGGAGCACCTCAACTATGTGACT
GAGATCGCACAGGATGAGATTTATATCCTGGACCCTGAGCTGCTGGGGGCATCGGCCCGG
CCTGACCTCCCAACCCCCACTTCCCCTCTCCCCACCTCACCCTGCTCACCCACGCCCCGG
TCACTGCAAGGGGATGCTGCACCCCCTCAAGGTGAAGAGCTGATTGAGGCTGCCAAGAGG
AACGACTTCTGTAAGCTCCAGGAGCTGCACCGAGCTGGGGGCGACCTCATGCACCGAGAC
GAGCAGAGTCGCACGCTCCTGCACCACGCAGTCAGCACTGGCAGCAAGGATGTGGTCCGC
TACCTGCTGGACCACGCCCCCCCAGAGATCCTTGATGCGGTGGAGGAAAACGGGGAGACC
TGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGCACCATCTGCCACTACATCGTGGAGGCC
GGGGCCTCGCTCATGAAGACAGACCAGCAGGGCGACACTCCCCGGCAGCGGGCTGAGAAG
GCTCAGGACACCGAGCTGGCCGCCTACCTGGAGAACCGGCAGCACTACCAGATGATCCAG
CGGGAGGACCAGGAGACGGCTGTGTAG

Enzyme 25 GenBank Gene ID

U51477

Enzyme 25 GeneCard ID

DGKZ

Enzyme 25 GenAtlas ID

DGKZ

Enzyme 25 HGNC ID

HGNC:2857

Enzyme 25 Chromosome Location

Enzyme 25 Locus

11p11.2

Enzyme 25 SNPs

SNPJam Report Link Image

Enzyme 25 General References

Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed ]
Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed ]
Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed ]
Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed ]

Enzyme 25 Metabolite References

Not Available

Enzyme 26 [top]

Enzyme 26 ID

5487

Enzyme 26 Name

L-fucose kinase

Enzyme 26 Synonyms

Fucokinase

Enzyme 26 Gene Name

FUK

Enzyme 26 Protein Sequence

>L-fucose kinase

MEQPKGVDWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTLLLAVEDPEKRVGSGGAT
LNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPEAPV
EALVCNLDCLLDIMTYRLGPGSPPGVWVCSTDMLLSVPANPGISWDSFRGARVIALPGSP
AYAQNHGVYLTDPQGLVLDIYYQGTEAEIQRCVRPDGRVPLVSGVVFFSVETAERLLATH
VSPPLDACTYLGLDSGARPVQLSLFFDILHCMAENVTREDFLVGRPPELGQGDADVAGYL
QSARAQLWRELRDQPLTMAYVSSGSYSYMTSSASEFLLSLTLPGAPGAQIVHSQVEEQQL
LAAGSSVVSCLLEGPVQLGPGSVLQHCHLQGPIHIGAGCLVTGLDTAHSKALHGRELRDL
VLQGHHTRLHGSPGHAFTLVGRLDSWERQGAGTYLNVPWSEFFKRTGVRAWDLWDPETLP
AEYCLPSARLFPVLHPSRELGPQDLLWMLDHQEDGGEALRAWRASWRLSWEQLQPCLDRA
ATLASRRDLFFRQALHKARHVLEARQDLSLRPLIWAAVREGCPGPLLATLDQVAAGAGDP
GVAARALACVADVLGCMAEGRGGLRSGPAANPEWMRPFSYLECGDLAAGVEALAQERDKW
LSRPALLVRAARHYEGAGQILIRQAVMSAQHFVSTEQVELPGPGQWVVAECPARVDFSGG
WSDTPPLAYELGGAVLGLAVRVDGRRPIGARARRIPEPELWLAVGPRQDEMTVKIVCRCL
ADLRDYCQPHAPGALLKAAFICAGIVHVHSELQLSEQLLRTFGGGFELHTWSELPHGSGL
GTSSILAGTALAALQRAAGRVVGTEALIHAVLHLEQVLTTGGGWQDQVGGLMPGIKVGRS
RAQLPLKVEVEEVTVPEGFVQKLNDHLLLVYTGKTRLARNLLQDVLRSWYARLPAVVQNA
HSLVRQTEECAEGFRQGSLPLLGQCLTSYWEQKKLMAPGCEPLTVRRMMDVLAPHVHGQS
LAGAGGGGFLYLLTKEPQQKEALEAVLAKTEGLGNYSIHLVEVDTQGLSLKLLGTEASTC
CPFP

Enzyme 26 Number of Residues

1084

Enzyme 26 Molecular Weight

117624

Enzyme 26 Theoretical pI

6.21

Enzyme 26 GO Classification

Function
ATP binding adenyl nucleotide binding binding catalytic activity kinase activity nucleotide binding phosphotransferase activity, alcohol group as acceptor purine nucleotide binding transferase activity transferase activity, transferring phosphorus-containing groups
Process
cellular metabolism metabolism phosphate metabolism phosphorus metabolism phosphorylation physiological process
Component
cell cytoplasm intracellular

Enzyme 26 General Function

Not Available

Enzyme 26 Specific Function

Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides

Enzyme 26 Pathways

Fructose and Mannose Metabolism (map00051 )

Enzyme 26 Reactions

ATP + L-fucose = ADP + beta-L-fucose 1-phosphate

Enzyme 26 Pfam Domain Function

Fucokinase (PF07959 )
GHMP_kinases_C (PF08544 )
GHMP_kinases_N (PF00288 )

Enzyme 26 Signals

None

Enzyme 26 Transmembrane Regions

None

Enzyme 26 Essentiality

Not Available

Enzyme 26 GenBank ID Protein

21212956

Enzyme 26 UniProtKB/Swiss-Prot ID

Q8N0W3

Enzyme 26 UniProtKB/Swiss-Prot Entry Name

FUK_HUMAN

Enzyme 26 PDB ID

Not Available

Enzyme 26 Cellular Location

Not Available

Enzyme 26 Gene Sequence

>2973 bp

ATGGGTCGAGACTTCCCCTTTGATGACTGTGGCAGGGCTTTCACCTGCCTCCCCGTGGAG
AACCCCGAGGCCCCCGTGGAAGCCTTGGTCTGCAACCTGGACTGCCTGCTGGACATCATG
ACCTATCGGCTGGGCCCGGGCTCCCCGCCAGGCGTGTGGGTCTGCAGCACCGACATGCTG
CTGTCTGTTCCTGCAAATCCTGGTATCAGCTGGGACAGCTTCCGGGGAGCCAGAGTGATC
GCCCTCCCAGGGAGCCCGGCCTACGCTCAGAATCATGGCGTCTACCTAACTGACCCCCAG
GGCCTTGTTTTGGACATTTACTACCAGGGCACTGAGGCAGAGATTCAGCGGTGTGTCAGG
CCTGATGGGCGGGTGCCACTGGTCTCTGGGGTTGTCTTCTTCTCTGTGGAGACTGCCGAG
CGCCTCCTAGCCACCCACGTGAGCCCGCCCCTGGATGCCTGCACCTACCTAGGCTTGGAC
TCCGGAGCCCGGCCTGTCCAGCTGTCTCTGTTTTTTGACATTCTCCACTGCATGGCTGAG
AACGTGACCAGGGAGGACTTCCTGGTGGGGAGGCCCCCAGAGTTGGGGCAAGGCGATGCA
GATGTAGCGGGTTATCTGCAGAGCGCCCGGGCCCAGCTGTGGAGGGAGCTTCGCGATCAG
CCCCTTACCATGGCCTATGTCTCCAGCGGCAGCTACAGCTACATGACCTCCTCAGCCAGT
GAGTTCCTGCTCAGCCTCACACTCCCCGGGGCTCCTGGGGCCCAGATTGTGCACTCCCAG
GTGGAGGAGCAGCAGCTTCTGGCGGCCGGGAGCTCTGTGGTCAGCTGCCTGCTGGAGGGC
CCTGTCCAGCTGGGTCCTGGGAGCGTCCTGCAGCACTGCCACCTGCAGGGCCCCATTCAC
ATAGGCGCTGGCTGCTTGGTGACTGGCCTGGATACAGCCCACTCCAAGGCCCTGCATGGC
CGGGAGCTGCGTGACCTTGTCCTGCAGGGACACCACACGCGGCTACACGGCTCCCCGGGC
CACGCCTTCACCCTCGTTGGCCGTCTGGACAGCTGGGAGAGACAGGGGGCAGGCACATAT
CTCAACGTGCCCTGGAGTGAATTCTTCAAGAGGACAGGTGTTCGAGCCTGGGACCTGTGG
GACCCCGAGACGCTGCCCGCAGAGTACTGCCTTCCCAGCGCCCGCCTCTTTCCTGTGCTC
CACCCCTCGAGGGAGCTGGGACCCCAGGACCTGCTGTGGATGCTGGACCACCAGGAGGAT
GGGGGCGAGGCCCTGCGAGCCTGGCGGGCCTCCTGGCGCCTGTCCTGGGAGCAGCTGCAG
CCGTGCCTGGATCGGGCTGCCACGCTGGCCTCTCGCCGGGACCTGTTCTTCCGCCAGGCC
CTGCATAAGGCGCGGCACGTGCTGGAGGCCCGGCAGGACCTCAGCCTGCGCCCGCTGATC
TGGGCTGCTGTCCGCGAGGGCTGCCCCGGGCCCCTGCTGGCCACGCTGGACCAGGTTGCA
GCTGGGGCAGGAGACCCTGGTGTGGCGGCACGGGCACTGGCCTGTGTGGCGGACGTCCTG
GGCTGCATGGCAGAGGGCCGTGGGGGCTTGCGGAGCGGGCCAGCTGCCAACCCTGAGTGG
ATGCGGCCCTTCTCATACCTGGAGTGTGGAGACCTGGCAGCGGGCGTGGAGGCGCTTGCC
CAGGAGAGGGACAAGTGGCTAAGCAGGCCAGCCTTGCTGGTGCGAGCGGCCCGCCACTAT
GAGGGGGCTGGTCAGATCCTGATCCGCCAGGCTGTGATGTCAGCCCAGCACTTTGTCTCC
ACAGAGCAGGTGGAACTGCCGGGACCTGGGCAGTGGGTGGTGGCTGAGTGCCCGGCCCGT
GTGGATTTCTCTGGGGGCTGGAGTGACACGCCACCCCTTGCCTATGAGCTTGGCGGGGCT
GTGCTGGGCCTGGCTGTGCGAGTGGACGGCCGCCGGCCCATCGGAGCCAGGGCACGCCGC
ATCCCGGAGCCTGAGCTGTGGCTGGCGGTGGGGCCTCGGCAGGATGAGATGACTGTGAAG
ATAGTGTGCCGGTGCCTGGCTGACCTGCGGGACTACTGCCAGCCTCATGCCCCAGGGGCC
CTGCTGAAGGCGGCCTTCATCTGTGCAGGGATCGTGCATGTCCACTCGGAACTCCAGCTG
AGTGAGCAGCTGCTCCGCACCTTCGGGGGCGGCTTTGAGCTGCACACCTGGTCTGAGCTG
CCCCACGGCTCTGGCCTGGGCACCAGCAGCATCCTGGCAGGCACTGCCCTGGCTGCCTTG
CAGCGAGCCGCAGGCCGGGTGGTGGGCACGGAAGCCCTGATCCACGCAGTGCTGCACCTG
GAGCAGGTGCTCACCACTGGAGGTGGCTGGCAGGACCAAGTAGGTGGCCTAATGCCTGGC
ATCAAGGTGGGGCGCTCCCGGGCTCAGCTGCCACTGAAGGTGGAGGTAGAAGAGGTCACG
GTGCCTGAGGGCTTTGTCCAGAAGCTCAATGACCACCTGCTCTTGGTGTACACTGGCAAG
ACCCGCCTGGCTCGGAACCTGCTGCAGGATGTGCTGAGGAGCTGGTATGCCCGACTTCCT
GCTGTGGTGCAGAATGCCCACAGCCTGGTACGGCAAACTGAGGAGTGTGCTGAAGGCTTC
CGCCAAGGAAGCCTGCCTCTGCTGGGCCAGTGCCTGACCTCGTACTGGGAGCAGAAGAAG
CTCATGGCTCCAGGCTGTGAGCCCCTGACTGTGCGGCGTATGATGGATGTCCTGGCCCCC
CACGTGCATGGCCAGAGCCTGGCTGGGGCAGGCGGTGGAGGCTTTCTCTATCTGTTGACC
AAGGAGCCACAGCAAAAGGAGGCCTTGGAGGCGGTGCTGGCCAAGACCGAGGGCCTTGGG
AATTACAGCATCCACCTGGTTGAAGTGGACACTCAGGGCCTGAGCCTGAAGCTGCTGGGG
ACCGAGGCCTCAACCTGTTGCCCTTTCCCATGA

Enzyme 26 GenBank Gene ID

AJ441184

Enzyme 26 GeneCard ID

FUK

Enzyme 26 GenAtlas ID

FUK

Enzyme 26 HGNC ID

HGNC:29500 Link Image

Enzyme 26 Chromosome Location

Not Available

Enzyme 26 Locus

Not Available

Enzyme 26 SNPs

SNPJam Report Link Image

Enzyme 26 General References

Hinderlich S, Berger M, Blume A, Chen H, Ghaderi D, Bauer C: Identification of human L-fucose kinase amino acid sequence. Biochem Biophys Res Commun. 2002 Jun 14;294(3):650-4. [PubMed ]

Enzyme 26 Metabolite References

Not Available

Enzyme 27 [top]

Enzyme 27 ID

5490

Enzyme 27 Name

Propionyl-CoA carboxylase beta chain, mitochondrial precursor

Enzyme 27 Synonyms

PCCase subunit beta
Propanoyl-CoA:carbon dioxide ligase subunit beta

Enzyme 27 Gene Name

PCCB

Enzyme 27 Protein Sequence

>Propionyl-CoA carboxylase beta chain, mitochondrial precursor

MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL

Enzyme 27 Number of Residues

539

Enzyme 27 Molecular Weight

58216

Enzyme 27 Theoretical pI

7.69

Enzyme 27 GO Classification

Function
catalytic activity ligase activity
Process
—
Component
—

Enzyme 27 General Function

Not Available

Enzyme 27 Specific Function

ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA

Enzyme 27 Pathways

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

Enzyme 27 Reactions

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA

Enzyme 27 Pfam Domain Function

Carboxyl_trans (PF01039 )

Enzyme 27 Signals

1-23

Enzyme 27 Transmembrane Regions

Not Available

Enzyme 27 Essentiality

Not Available

Enzyme 27 GenBank ID Protein

312812

Enzyme 27 UniProtKB/Swiss-Prot ID

P05166

Enzyme 27 UniProtKB/Swiss-Prot Entry Name

PCCB_HUMAN Link Image

Enzyme 27 PDB ID

Not Available

Enzyme 27 Cellular Location

Not Available

Enzyme 27 Gene Sequence

>1620 bp

ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA

Enzyme 27 GenBank Gene ID

X73424

Enzyme 27 GeneCard ID

PCCB

Enzyme 27 GenAtlas ID

PCCB

Enzyme 27 HGNC ID

HGNC:8654

Enzyme 27 Chromosome Location

Enzyme 27 Locus

3q21-q22

Enzyme 27 SNPs

SNPJam Report Link Image

Enzyme 27 General References

Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed ]
Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed ]
Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [PubMed ]
Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed ]
Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed ]
Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed ]
Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed ]
Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed ]
Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed ]

Enzyme 27 Metabolite References

Not Available

Enzyme 28 [top]

Enzyme 28 ID

5507

Enzyme 28 Name

Phenylalanyl-tRNA synthetase, mitochondrial precursor

Enzyme 28 Synonyms

Phenylalanine--tRNA ligase
PheRS

Enzyme 28 Gene Name

FARS2

Enzyme 28 Protein Sequence

>Phenylalanyl-tRNA synthetase, mitochondrial precursor

MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQ
DDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVV
TTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRR
DQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVE
FDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVN
SAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKY
PAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRH
MERTLSQREVRHIHQALQEAAVQLLGVEGRF

Enzyme 28 Number of Residues

451

Enzyme 28 Molecular Weight

52357

Enzyme 28 Theoretical pI

7.48

Enzyme 28 GO Classification

Function
ATP binding RNA ligase activity adenyl nucleotide binding binding catalytic activity ligase activity ligase activity, forming phosphoric ester bonds nucleotide binding phenylalanine-tRNA ligase activity purine nucleotide binding tRNA ligase activity
Process
RNA metabolism cellular metabolism metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism phenylalanyl-tRNA aminoacylation physiological process tRNA aminoacylation tRNA aminoacylation for protein translation tRNA metabolism
Component
cell cytoplasm intracellular

Enzyme 28 General Function

Translation, ribosomal structure and biogenesis

Enzyme 28 Specific Function

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)

Enzyme 28 Pathways

Aminoacyl-tRNA biosynthesis (map00970 )
Phenylalanine and Tyrosine Metabolism (map00400 )

Enzyme 28 Reactions

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)

Enzyme 28 Pfam Domain Function

FDX-ACB (PF03147 )
tRNA-synt_2d (PF01409 )

Enzyme 28 Signals

None

Enzyme 28 Transmembrane Regions

None

Enzyme 28 Essentiality

Not Available

Enzyme 28 GenBank ID Protein

3983103

Enzyme 28 UniProtKB/Swiss-Prot ID

O95363

Enzyme 28 UniProtKB/Swiss-Prot Entry Name

SYFM_HUMAN Link Image

Enzyme 28 PDB ID

Not Available

Enzyme 28 Cellular Location

Not Available

Enzyme 28 Gene Sequence

>1356 bp

ATGGTGGGCTCAGCTCTCAGGAGAGGTGCCCATGCATATGTCTACCTGGTGAGTAAGGCC
AGTCACATCTCCAGAGGCCATCAGCACCAGGCCTGGGGATCGAGGCCTCCTGCAGCAGAG
TGTGCCACCCAAAGAGCTCCAGGCAGTGTGGTGGAGCTGCTGGGCAAATCCTACCCTCAG
GACGACCACAGCAACCTCACCCGGAAGGTCCTCACCAGAGTTGGCAGGAACCTGCACAAC
CAGCAGCATCACCCTCTGTGGCTGATCAAGGAGAGGGTGAAGGAGCACTTCTACAAGCAG
TATGTGGGCCGCTTTGGGACCCCGTTGTTCTCGGTCTACGACAACCTTTCTCCAGTGGTC
ACGACCTGGCAGAACTTTGACAGCCTGCTCATCCCAGCTGATCACCCCAGCAGGAAGAAG
GGGGACAACTATTACCTGAATCGGACTCACATGCTGAGAGCGCACACGTCTGCACACCAG
TGGGACTTGCTGCACGCGGGACTGGATGCCTTCCTGGTGGTGGGTGATGTCTACAGGCGT
GACCAGATCGACTCCCAGCACTACCCTATTTTCCACCAGCTGGAGGCCGTGCGGCTCTTC
TCCAAGCATGAGTTATTTGCTGGTATAAAGGATGGAGAAAGCCTGCAGCTCTTTGAACAA
AGTTCTCGCTCTGCGCATAAACAAGAGACACACACCATGGAGGCCGTGAAGCTTGTAGAG
TTTGATCTTAAGCAAACGCTTACCAGGCTCATGGCACATCTTTTTGGAGATGAGCTGGAG
ATAAGATGGGTAGACTGCTACTTCCCTTTTACACATCCTTCCTTTGAGATGGAGATCAAC
TTTCATGGAGAATGGCTGGAAGTTCTTGGCTGCGGGGTGATGGAACAACAACTGGTCAAT
TCAGCTGGTGCTCAAGACCGAATCGGCTGGGCTTTTGGCCTAGGATTAGAAAGGCTAGCC
ATGATCCTCTACGACATCCCTGATATCCGTCTCTTCTGGTGTGAGGACGAGCGCTTCCTG
AAGCAGTTCTGTGTATCCAACATTAATCAGAAGGTGAAGTTTCAGCCTCTTAGCAAATAT
CCGGCTGTGATCAATGATATTTCATTCTGGTTGCCCTCTGAGAATTACGCAGAAAATGAT
TTCTATGACTTAGTCCGAACAATTGGAGGAGACCTGGTGGAAAAGGTTGATCTCATAGAC
AAGTTTGTACATCCAAAGACGCACAAGACCAGCCACTGCTACCGCATCACGTACCGCCAC
ATGGAACGGACTCTGTCCCAGAGAGAGGTCAGGCACATCCACCAGGCCTTGCAGGAGGCT
GCAGTCCAGCTGTTGGGTGTGGAGGGCAGGTTCTGA

Enzyme 28 GenBank Gene ID

AF097441

Enzyme 28 GeneCard ID

FARS2

Enzyme 28 GenAtlas ID

FARS2

Enzyme 28 HGNC ID

HGNC:21062 Link Image

Enzyme 28 Chromosome Location

Enzyme 28 Locus

6p25.1

Enzyme 28 SNPs

SNPJam Report Link Image

Enzyme 28 General References

Bullard JM, Cai YC, Demeler B, Spremulli LL: Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase. J Mol Biol. 1999 May 14;288(4):567-77. [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 ]

Enzyme 28 Metabolite References

Not Available

Enzyme 29 [top]

Enzyme 29 ID

5566

Enzyme 29 Name

Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase

Enzyme 29 Synonyms

GARS
Glycinamide ribonucleotide synthetase
Phosphoribosylglycinamide synthetase
Phosphoribosylformylglycinamidine cyclo-ligase
AIRS
Phosphoribosyl-aminoimidazole synthetase
AIR synthase
Phosphoribosylglycinamide formyltransferase
GART
GAR transformylase
5'-phosphoribosylglycinamide transformylase]

Enzyme 29 Gene Name

GART

Enzyme 29 Protein Sequence

>Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase

MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE

Enzyme 29 Number of Residues

1010

Enzyme 29 Molecular Weight

107768

Enzyme 29 Theoretical pI

6.68

Enzyme 29 GO Classification

Function
catalytic activity cyclo-ligase activity glycine hydroxymethyltransferase activity hydroxymethyl-, formyl- and related transferase activity ligase activity ligase activity, forming carbon-nitrogen bonds methyltransferase activity phosphoribosylamine-glycine ligase activity phosphoribosylformylglycinamidine cyclo-ligase activity phosphoribosylglycinamide formyltransferase activity transferase activity transferase activity, transferring one-carbon groups
Process
'de novo' IMP biosynthesis IMP biosynthesis biosynthesis cellular metabolism metabolism nucleobase metabolism nucleobase, nucleoside, nucleotide and nucleic acid metabolism nucleotide metabolism physiological process purine base biosynthesis purine base metabolism purine nucleoside monophosphate biosynthesis purine nucleotide biosynthesis purine nucleotide metabolism purine ribonucleoside monophosphate biosynthesis
Component
cell cytoplasm intracellular

Enzyme 29 General Function

Nucleotide transport and metabolism

Enzyme 29 Specific Function

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + 1-N-(5-phospho-D-ribosyl)glycinamide

Enzyme 29 Pathways

Purine Metabolism (map00230 )

Enzyme 29 Reactions

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide

Enzyme 29 Pfam Domain Function

AIRS (PF00586 )
AIRS_C (PF02769 )
Formyl_trans_N (PF00551 )
GARS_A (PF01071 )
GARS_C (PF02843 )
GARS_N (PF02844 )

Enzyme 29 Signals

None

Enzyme 29 Transmembrane Regions

None

Enzyme 29 Essentiality

Not Available

Enzyme 29 GenBank ID Protein

31642

Enzyme 29 UniProtKB/Swiss-Prot ID

P22102

Enzyme 29 UniProtKB/Swiss-Prot Entry Name

PUR2_HUMAN Link Image

Enzyme 29 PDB ID

Not Available

Enzyme 29 Cellular Location

Not Available

Enzyme 29 Gene Sequence

>3033 bp

ATGGCAGCCCGAGTACTTATAATTGGCAGTGGAGGAAGGGAACATACGCTGGCCTGGAAA
CTTGCACAGTCTCATCATGTCAAACAAGTGTTGGTTGCCCCAGGAAACGCAGGCACTGCC
TGCTCTGAAAAGATTTCAAATACCGCCATCTCAATCAGTGACCACACTGCCCTTGCTCAA
TTCTGCAAAGAGAAGAAAATTGAATTTGTAGTTGTTGGACCAGAAGCACCTCTGGCTGCT
GGGATTGTTGGGAACCTGAGGTCTGCAGGAGTGCAATGCTTTGGCCCAACAGCAGAAGCG
GCTCAGTTAGAGTCCAGCAAAAGGTTTGCCAAAGAGTTTATGGACAGACATGGAATCCCA
ACCGCACAATGGAAGGCTTTCACCAAACCTGAAGAAGCCTGCAGCTTCATTTTGAGTGCA
GACTTCCCTGCTTTGGTTGTGAAGGCCAGTGGTCTTGCAGCTGGAAAAGGGGTGATTGTT
GCAAAGAGCAAAGAAGAGGCCTGCAAAGCTGTACAAGAGATCATGCAGGAGAAAGCCTTT
GGGGCAGCTGGAGAAACAATTGTCATTGAAGAACTTCTTGACGGAGAAGAGGTGTCGTGT
CTGTGTTTCACTGATGGCAAGACTGTGGCCCCCATGCCCCCAGCACAGGACCATAAGCGA
TTACTGGAGGGAGATGGTGGCCCTAACACAGGGGGAATGGGAGCCTATTGTCCAGCCCCT
CAGGTTTCTAATGATCTATTACTAAAAATTAAAGATACTGTTCTTCAGAGGACAGTGGAT
GGCATGCAGCAAGAGGGTACTCCATATACAGGTATTCTCTATGCTGGAATAATGCTGACC
AAGAATGGCCCAAAAGTTCTAGAGTTTAATTGCCGTTTTGGTGATCCAGAGTGCCAAGTA
ATCCTCCCACTTCTTAAAAGTGATCTTTATGAAGTGATTCAGTCCACCTTAGATGGACTG
CTCTGCACATCTCTGCCTGTTTGGCTAGAAAACCACACCGCCCTAACTGTTGTCATGGCA
AGTAAAGGTTATCCTGGAGACTACACCAAGGGTGTAGAGATAACAGGGTTTCCTGAGGCT
CAAGCTCTAGGACTGGAGGTGTTCCATGCAGGCACTGCCCTCAAAAATGGCAAAGTAGTA
ACTCATGGGGGTAGAGTTCTTGCAGTCACAGCCATCCGGGAAAATCTCATATCAGCCCTT
GAGGAAGCCAAGAAAGGACTAGCTGCTATAAAGTTTGAGGGAGCAATTTATAGGAAAGAC
GTCGGCTTTCGTGCCATAGCTTTCCTCCAGCAGCCCAGGAGTTTGACTTACAAGGAATCT
GGAGTAGATATCGCAGCTGGAAATATGCTGGTCAAGAAAATTCAGCCTTTAGCAAAAGCC
ACTTCCAGATCAGGCTGTAAAGTTGATCTTGGAGGTTTTGCTGGTCTTTTTGATTTAAAA
GCAGCTGGTTTCAAAGATCCCCTTCTGGCCTCTGGAACAGATGGCGTTGGAACTAAACTA
AAGATTGCCCAGCTATGCAATAAACATGATACCATTGGTCAAGATTTGGTAGCAATGTGT
GTTAATGATATTCTGGCACAAGGAGCAGAGCCCCTCTTCTTCCTTGATTACTTTTCCTGT
GGAAAACTTGACCTCAGTGTAACTGAAGCTGTTGTTGCTGGAATTGCTAAAGCTTGTGGA
AAAGCTGGATGTGCTCTCCTTGGAGGTGAAACAGCAGAAATGCCTGACATGTATCCCCCT
GGAGAGTATGACCTAGCTGGGTTTGCCGTTGGTGCCATGGAGCGAGATCAGAAACTCCCT
CACCTGGAAAGAATCACTGAGGGTGATGTTGTTGTTGGAATAGCTTCATCTGGTCTTCAT
AGCAATGGATTTAGCCTTGTGAGGAAAATCGTTGCAAAATCTTCCCTCCAGTACTCCTCT
CCAGCACCTGATGGTTGTGGTGACCAGACTTTAGGGGACTTACTTCTCACGCCTACCAGA
ATCTACAGCCATTCACTGTTACCTGTCCTACGTTCAGGACATGTCAAAGCCTTTGCCCAT
ATTACTGGTGGAGGATTACTAGAGAACATCCCCAGAGTCCTCCCTGAGAAACTTGGGGTA
GATTTAGATGCCCAGACCTGGAGGATCCCCAGGGTTTTCTCATGGTTGCAGCAGGAAGGA
CACCTCTCTGAGGAAGAGATGGCCAGAACATTTAACTGTGGGGTTGGCGCTGTCCTTGTG
GTATCAAAGGAGCAGACAGAGCAGATTCTGAGGGATATCCAGCAGCACAAGGAAGAAGCC
TGGGTGATTGGCAGTGTGGTTGCACGAGCTGAAGGTTCCCCACGTGTGAAAGTCAAGAAT
CTGATTGAAAGCATGCAAATAAATGGGTCAGTGTTGAAGAATGGCTCCCTGACAAATCAT
TTCTCTTTTGAAAAAAAAAAGGCCAGAGTGGCTGTCTTAATATCTGGAACAGGATCGAAC
CTGCAAGCACTTATAGACAGTACTCGGGAACCAAATAGCTCTGCACAAATTGATATTGTT
ATCTCCAACAAAGCCGCAGTAGCTGGGTTAGATAAAGCGGAAAGAGCTGGTATTCCCACT
AGAGTAATTAATCATAAACTGTATAAAAATCGTGTAGAATTTGACAGTGCAATTGACCTA
GTCCTTGAAGAGTTCTCCATAGACATAGTCTGTCTTGCAGGATTCATGAGAATTCTTTCT
GGCCCCTTTGTCCAAAAGTGGAATGGAAAAATGCTCAATATCCACCCATCCTTGCTCCCT
TCTTTTAAGGGTTCAAATGCCCATGAGCAAGCCCTGGAAACCGGAGTCACAGTTACTGGG
TGCACTGTACACTTTGTAGCTGAAGATGTGGATGCTGGACAGATTATTTTGCAAGAAGCT
GTTCCCGTGAAGAGGGGTGATACTGTCGCAACTCTTTCTGAAAGAGTAAAATTAGCAGAA
CATAAAATATTTCCTGCAGCCCTTCAGCTGGTGGCCAGTGGAACTGTACAGCTTGGAGAA
AATGGCAAGATCTGTTGGGTTAAAGAGGAATGA

Enzyme 29 GenBank Gene ID

X54199

Enzyme 29 GeneCard ID

GART

Enzyme 29 GenAtlas ID

GART

Enzyme 29 HGNC ID

HGNC:4163

Enzyme 29 Chromosome Location

Not Available

Enzyme 29 Locus

Not Available

Enzyme 29 SNPs

SNPJam Report Link Image

Enzyme 29 General References

Aimi J, Qiu H, Williams J, Zalkin H, Dixon JE: De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Nucleic Acids Res. 1990 Nov 25;18(22):6665-72. [PubMed ]
Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed ]
Schild D, Brake AJ, Kiefer MC, Young D, Barr PJ: Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2916-20. [PubMed ]

Enzyme 29 Metabolite References

Not Available

Enzyme 30 [top]

Enzyme 30 ID

5570

Enzyme 30 Name

N-acylglucosamine 2-epimerase

Enzyme 30 Synonyms

GlcNAc 2-epimerase
N- acetyl-D-glucosamine 2-epimerase
AGE
Renin-binding protein
RnBP

Enzyme 30 Gene Name

RENBP

Enzyme 30 Protein Sequence

>N-acylglucosamine 2-epimerase

MEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGR
QVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRT
IFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMA
VPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCL
GRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADN
FCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFG
YLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE

Enzyme 30 Number of Residues

417

Enzyme 30 Molecular Weight

47747

Enzyme 30 Theoretical pI

6.20

Enzyme 30 GO Classification

Function
catalytic activity hydrolase activity hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds intramolecular oxidoreductase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses isomerase activity mannose-6-phosphate isomerase activity
Process
alcohol metabolism cellular metabolism hexose metabolism mannose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 30 General Function

Carbohydrate transport and metabolism

Enzyme 30 Specific Function

Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine. Binds to renin forming a protein complex called high molecular weight (HMW) renin and inhibits renin activity

Enzyme 30 Pathways

Aminosugars metabolism (map00530 )

Enzyme 30 Reactions

N-acyl-D-glucosamine = N-acyl-D-mannosamine

Enzyme 30 Pfam Domain Function

GlcNAc_2-epim (PF07221 )

Enzyme 30 Signals

None

Enzyme 30 Transmembrane Regions

None

Enzyme 30 Essentiality

Not Available

Enzyme 30 GenBank ID Protein

220053

Enzyme 30 UniProtKB/Swiss-Prot ID

P51606

Enzyme 30 UniProtKB/Swiss-Prot Entry Name

RENBP_HUMAN Link Image

Enzyme 30 PDB ID

Not Available

Enzyme 30 Cellular Location

Not Available

Enzyme 30 Gene Sequence

>1254 bp

ATGGAGAAAGAGCGAGAGACTCTGCAGGCCTGGAAGGAGCGCGTGGGGCAGGAGCTGGAC
CGCGTGGTGGCTTTCTGGATGGAGCACTCCCACGACCAGGAGCACGGGGGCTTCTTCACG
TGCCTTGGCCGCGAGGGGCGGGTGTATGATGACCTCAAGTATGTGTGGCTGCAGGGGAGG
CAGGTATGGATGTATTGTCGCCTGTACCGCACTTTCGAGCGCTTCCGCCATGCTCAGCTT
CTGGACGCAGCAAAAGCAGGTGGTGAGTTCTTGCTGCGGTATGCCCGGGTGGCACCTCCT
GGCAAGAAGTGTGCCTTTGTGCTGACTCGGGACGGCCGCCCGGTCAAGGTGCAGCGAACC
ATCTTCAGTGAGTGTTTCTACACCATGGCCATGAACGAGCTGTGGAGAGCCACAGGGGAA
GTGCGGTACCAGACGGAAGCGGTGGAGATGATGGATCAGATCGTCCACTGGGTGCAGGAG
GACGCGTCGGGACTGGGCCGGCCCCAGCTCCAGGGGGCCCCGGCTGCGGAGCCCATGGCG
GTGCCCATGATGCTACTGAACCTGGTGGAGCAGCTCGGGGAGGCAGATGAGGAGCTGGCG
GGCAAATACGCAGAGCTGGGGGACTGGTGCGCCCGGAGGATTCTGCAGCACGTGCAGAGG
GATGGACAAGCTGTGCTGGAGAATGTGTCAGAGGGTGGCAAGGAACTTCCTGGCTGCCTG
GGGAGACAGCAGAACCCAGGCCACACGCTGGAAGCCGGCTGGTTTCTGCTCCGTCATTGC
ATTCGGAAAGGCGACCCCGAACTTCGAGCCCACGTGATTGACAAGTTCCTATTGTTGCCC
TTCCACTCCGGATGGGACCCTGACCACGGAGGCCTCTTTTACTTCCAGGATGCTGATAAC
TTCTGCCCCACCCAGCTGGAGTGGGCCATGAAGCTCTGGTGGCCACACAGTGAAGCCATG
ATTGCCTTCCTCATGGGTTACAGTGACAGTGGGGACCCTGTGCTGCTGCGCCTCTTCTAC
CAAGTGGCTGAGTACACCTTCCGCCAGTTTCGCGATCCCGAGTACGGGGAATGGTTTGGC
TACCTGAGCCGAGAGGGCAAGGTGGCCCTCTCCATCAAGGGAGGTCCTTTCAAAGGCTGC
TTCCACGTGCCGCGGTGCCTAGCCATGTGCGAGGAGATGCTGGGCGCCCTGCTGAGCCGC
CCCGCCCCCGCCCCCTCCCCCGCCCCCACCCCCGCCTGCCGAGGCGCGGAATAA

Enzyme 30 GenBank Gene ID

D10232

Enzyme 30 GeneCard ID

RENBP

Enzyme 30 GenAtlas ID

RENBP

Enzyme 30 HGNC ID

HGNC:9959

Enzyme 30 Chromosome Location

Enzyme 30 Locus

Xq28

Enzyme 30 SNPs

SNPJam Report Link Image

Enzyme 30 General References

Inoue H, Takahashi S, Fukui K, Miyake Y: Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif. J Biochem (Tokyo). 1991 Oct;110(4):493-500. [PubMed ]
Takahashi S, Takahashi K, Kaneko T, Ogasawara H, Shindo S, Kobayashi M: Human renin-binding protein is the enzyme N-acetyl-D-glucosamine 2-epimerase. J Biochem (Tokyo). 1999 Feb;125(2):348-53. [PubMed

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Human Metabolome Database Version 2.5

Showing metabocard for Adenosine triphosphate (HMDB00538)