Human Metabolome Database Version 2.5

Showing metabocard for Succinyl-CoA (HMDB01022)

Legend: metabolite field enzyme field

Version

2.5

Creation Date

2005-11-16 15:48:42

Update Date

2009-05-05 20:58:26

Accession Number

HMDB01022

Secondary Accession Numbers

Not Available

Common Name

Succinyl-CoA

Description

Succinyl-CoA is an important intermediate in the citric acid cycle, where it is synthesized from α-Ketoglutarate by α-ketoglutarate dehydrogenase (EC 1.2.4.2) through decarboxylation, and is converted into succinate through the hydrolytic release of coenzyme A by succinyl-CoA synthetase (EC 6.2.1.5). Succinyl-CoA may be an end product of peroxisomal beta-oxidation of dicarboxylic fatty acids; the identification of an apparently specific succinyl-CoA thioesterase (ACOT4, EC 3.1.2.3, hydrolyzes succinyl-CoA) in peroxisomes strongly suggests that succinyl-CoA is formed in peroxisomes. Acyl-CoA thioesterases (ACOTs) are a family of enzymes that catalyze the hydrolysis of the CoA esters of various lipids to the free acids and coenzyme A, thereby regulating levels of these compounds. (PMID: 16141203)

Synonyms

Coenzyme A S-(hydrogen succinate)
Coenzyme A S-succinate
S-(hydrogen butanedioate) Coenzyme A
S-Succinoylcoenzyme A
suc-co-A
suc-coa
succ-CoA
succ-Coenzyme A
succ-coenzyme-A
succ-S-CoA
succ-S-Coenzyme A
succ-S-coenzyme-A
succino-1-yl-coenzyme a
Succinyl CoA
Succinyl coenzyme A
succinyl-S-CoA
succinyl-S-Coenzyme A
succinyl-S-coenzyme-A
succinylcoenzyme-A
CoA S-(hydrogen succinate)
CoA S-succinate
S-(hydrogen butanedioate) CoA
S-(hydrogen butanedioic acid
S-(hydrogen butanedioate

Chemical IUPAC Name

4-[2-[3-[[4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanoyl]amino]propanoylamino]ethylsulfanyl]-4-oxobutanoic acid

Chemical Formula

C₂₅H₄₀N₇O₁₉P₃S

Chemical Structure

Chemical Taxonomy

Kingdom
Organic
Super Class
Nucleosides and Nucleoside conjugates
Class
Coenzyme A Derivatives
Sub Class
Short chain acyl CoAs
Family
Mammalian Metabolite
Species
secondary alcohol primary amine primary aromatic amine carboxylic acid secondary carboxylic acid amide thiocarboxylic acid ester phosphoric acid ester aromatic compound heterocyclic compound
Biofunction
Component of Butanoate metabolism Component of C5-Branched dibasic acid metabolism Component of Glycine, serine and threonine metabolism Component of Propanoate metabolism
Application
—
Source
Endogenous

Average Molecular Weight

867.607

Monoisotopic Molecular Weight

867.131226

Isomeric SMILES

CC(C)(COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=O

Canonical SMILES

CC(C)(COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)N1C=NC2=C1N=CN=C2N)C(O)C(=O)NCCC(=O)NCCSC(=O)CCC(O)=O

KEGG Compound ID

C00091

BioCyc ID

3-METHYLBENZYLSUCCINYL-COA Link Image

BiGG ID

33820

Wikipedia Link

Succinyl-CoA Link Image

NuGOwiki Link

Metagene Link

METLIN ID

PubChem Compound

PubChem Substance

ChEBI ID

CAS Registry Number

604-98-8

InChI Identifier

InChI=1/C25H40N7O19P3S/c1-25(2,20(38)23(39)28-6-5-14(33)27-7-8-55-16(36)4-3-15(34)35)10-48-54(45,46)51-53(43,44)47-9-13-19(50-52(40,41)42)18(37)24(49-13)32-12-31-17-21(26)29-11-30-22(17)32/h11-13,18-20,24,37-38H,3-10H2,1-2H3,(H,27,33)(H,28,39)(H,34,35)(H,43,44)(H,45,46)(H2,26,29,30)(H2,40,41,42)/t13-,18-,19-,20?,24-/m1/s1

Synthesis Reference

Wollemann, M. Mechanism of the succinyl-coenzyme A synthesis in brain extracts. Acta Physiologica Academiae Scientiarum Hungaricae (1959), 16 153-4.

Melting Point (Experimental)

Not Available

Experimental Water Solubility

Not Available Source: PhysProp

Predicted Water Solubility

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

Physiological Charge

-5

State

Solid

Experimental LogP/Hydrophobicity

Not Available Source: PhysProp

Predicted LogP/Hydrophobicity

-6.7 [Predicted by PubChem via XLOGP]; -0.61 [Predicted by ALOGPS] Calculated using ALOGPS

Material Safety Data Sheet (MSDS)

Not Available

MOL File

Show

SDF File

Show

PDB File

Show

2D Structure

3D Structure

Experimental PDB ID

Not Available

Experimental ¹H NMR Spectrum

Not Available

Experimental ¹³C NMR Spectrum

Not Available

Experimental ¹³C HSQC Spectrum

Not Available

Predicted ¹H NMR Spectrum

Show Image
Show Peaklist

Predicted ¹³C NMR Spectrum

Show Image
Show Peaklist

Mass Spectrum

Not Available

Simplified TOCSY Spectrum

Not Available

BMRB Spectrum

Not Available

Cellular Location

Cytoplasm (Predicted from LogP)
mitochondria

Biofluid Location

Not Available

Tissue Location

Tissue	References
Muscle	—
Testes	—

Concentrations (Normal)

Not Available

Concentrations (Abnormal)

Not Available

Associated Disorders

Not Available

OMIM ID

Not Available

Pathways

Name	SMPDB Link	KEGG Link
Citric Acid Cycle	SMP00057	map00020
Glycine and Serine Metabolism	SMP00004	map00260
Propanoate Metabolism	SMP00016	map00640
Threonine and 2-Oxobutanoate Degradation	SMP00452
Valine, Leucine and Isoleucine Degradation	SMP00032	map00280

General References

Elpeleg O, Miller C, Hershkovitz E, Bitner-Glindzicz M, Bondi-Rubinstein G, Rahman S, Pagnamenta A, Eshhar S, Saada A: Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion. Am J Hum Genet. 2005 Jun;76(6):1081-6. Epub 2005 Apr 22. [PubMed ]
Tanaka H, Kohroki J, Iguchi N, Onishi M, Nishimune Y: Cloning and characterization of a human orthologue of testis-specific succinyl CoA: 3-oxo acid CoA transferase (Scot-t) cDNA. Mol Hum Reprod. 2002 Jan;8(1):16-23. [PubMed ]
Wikipedia

Metabolic Enzymes

Enzyme 1 [top]

Enzyme 1 ID

5246

Enzyme 1 Name

5-aminolevulinate synthase, erythroid-specific, mitochondrial precursor

Enzyme 1 Synonyms

5-aminolevulinic acid synthase
Delta- aminolevulinate synthase
Delta-ALA synthetase
ALAS-E

Enzyme 1 Gene Name

ALAS2

Enzyme 1 Protein Sequence

>5-aminolevulinate synthase, erythroid-specific, mitochondrial precursor

MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA

Enzyme 1 Number of Residues

587

Enzyme 1 Molecular Weight

64634

Enzyme 1 Theoretical pI

8.19

Enzyme 1 GO Classification

Function
5-aminolevulinate synthase activity N-acyltransferase activity N-succinyltransferase activity acyltransferase activity catalytic activity transferase activity transferase activity, transferring acyl groups transferase activity, transferring groups other than amino-acyl groups transferase activity, transferring nitrogenous groups
Process
biosynthesis cellular metabolism heme biosynthesis heterocycle metabolism metabolism physiological process porphyrin biosynthesis porphyrin metabolism
Component
—

Enzyme 1 General Function

Coenzyme transport and metabolism

Enzyme 1 Specific Function

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)

Enzyme 1 Pathways

Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 1 Reactions

succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2

Enzyme 1 Pfam Domain Function

Aminotran_1_2 (PF00155 )
Preseq_ALAS (PF09029 )

Enzyme 1 Signals

1-15

Enzyme 1 Transmembrane Regions

Not Available

Enzyme 1 Essentiality

Not Available

Enzyme 1 GenBank ID Protein

28586

Enzyme 1 UniProtKB/Swiss-Prot ID

P22557

Enzyme 1 UniProtKB/Swiss-Prot Entry Name

HEM0_HUMAN Link Image

Enzyme 1 PDB ID

Not Available

Enzyme 1 Cellular Location

Not Available

Enzyme 1 Gene Sequence

>1749 bp

ATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGCCTCCTAGGCAAGGTG
GTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATCCTGGCTACCCAAGGA
CCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGAGATTCTCCATCTTGG
GCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGGAAGAGCAAGATTGTG
CAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAGACAGATCTGCCTAGC
TCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAGGAGCAGGAGCAGATC
TCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAACTATGTCTTCAGTTAT
GACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCACACCTACCGTGTGTTC
AAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACATTTCTTTGAGGCATCT
GTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTGGGCATGAGCCGACAC
CCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGTGCTGGAGCTGGTGGC
ACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAGCAGGAGCTGGCTGAG
CTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTTGCCAATGACTCTACT
CTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCAGACGCAGGCAACCAT
GCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTTGTCTTCAGGCACAAT
GACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAGATACCCAAAATTGTG
GCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTCGAGGAGTTGTGTGAT
GTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCATGCTGTAGGACTGTAT
GGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCATAAGATTGACATCATC
TCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATTGCCAGCACCCGTGAC
TTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACCACTTCTCTGCCCCCC
ATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGAGAGGAGGGCCAAGCC
CTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTACTCATGGACAGGGGC
CTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTGGGCAATGCAGCACTC
AACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTATGTGCAGGCCATCAAC
TACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCCTCCCCCCACCACAGC
CCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGGACTGCGGTGGGGCTG
CCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGTCCTGTACACTTTGAG
CTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCCCAGTATGTCACCACC
TATGCCTGA

Enzyme 1 GenBank Gene ID

Enzyme 1 GeneCard ID

Enzyme 1 GenAtlas ID

Enzyme 1 HGNC ID

Enzyme 1 Chromosome Location

Enzyme 1 Locus

Xp11.21

Enzyme 1 SNPs

SNPJam Report Link Image

Enzyme 1 General References

Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed ]
Cox TC, Bawden MJ, Martin A, May BK: Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991 Jul;10(7):1891-902. [PubMed ]
Surinya KH, Cox TC, May BK: Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene. J Biol Chem. 1998 Jul 3;273(27):16798-809. [PubMed ]
Cox TC, Bottomley SS, Wiley JS, Bawden MJ, Matthews CS, May BK: X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. N Engl J Med. 1994 Mar 10;330(10):675-9. [PubMed ]
Cotter PD, Baumann M, Bishop DF: Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4028-32. [PubMed ]
Furuyama K, Uno R, Urabe A, Hayashi N, Fujita H, Kondo M, Sassa S, Yamamoto M: R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity. Br J Haematol. 1998 Dec;103(3):839-41. [PubMed ]
Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T: A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am J Hematol. 1999 Oct;62(2):112-4. [PubMed ]
Cotter PD, May A, Li L, Al-Sabah AI, Fitzsimons EJ, Cazzola M, Bishop DF: Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. Blood. 1999 Mar 1;93(5):1757-69. [PubMed ]

Enzyme 1 Metabolite References

Not Available

Enzyme 2 [top]

Enzyme 2 ID

5251

Enzyme 2 Name

5-aminolevulinate synthase, nonspecific, mitochondrial precursor

Enzyme 2 Synonyms

5-aminolevulinic acid synthase
Delta-aminolevulinate synthase
Delta-ALA synthetase
ALAS-H

Enzyme 2 Gene Name

ALAS1

Enzyme 2 Protein Sequence

>5-aminolevulinate synthase, nonspecific, mitochondrial precursor

MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA

Enzyme 2 Number of Residues

640

Enzyme 2 Molecular Weight

70582

Enzyme 2 Theoretical pI

8.57

Enzyme 2 GO Classification

Function
5-aminolevulinate synthase activity N-acyltransferase activity N-succinyltransferase activity acyltransferase activity catalytic activity transferase activity transferase activity, transferring acyl groups transferase activity, transferring groups other than amino-acyl groups transferase activity, transferring nitrogenous groups
Process
biosynthesis cellular metabolism heme biosynthesis heterocycle metabolism metabolism physiological process porphyrin biosynthesis porphyrin metabolism
Component
—

Enzyme 2 General Function

Coenzyme transport and metabolism

Enzyme 2 Specific Function

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)

Enzyme 2 Pathways

Glycine, Serine and Threonine Metabolism (map00260 )

Enzyme 2 Reactions

succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2

Enzyme 2 Pfam Domain Function

Aminotran_1_2 (PF00155 )

Enzyme 2 Signals

None

Enzyme 2 Transmembrane Regions

None

Enzyme 2 Essentiality

Not Available

Enzyme 2 GenBank ID Protein

28583

Enzyme 2 UniProtKB/Swiss-Prot ID

P13196

Enzyme 2 UniProtKB/Swiss-Prot Entry Name

HEM1_HUMAN Link Image

Enzyme 2 PDB ID

Not Available

Enzyme 2 Cellular Location

Not Available

Enzyme 2 Gene Sequence

>1923 bp

ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA

Enzyme 2 GenBank Gene ID

Enzyme 2 GeneCard ID

Enzyme 2 GenAtlas ID

Enzyme 2 HGNC ID

Enzyme 2 Chromosome Location

Not Available

Enzyme 2 Locus

Not Available

Enzyme 2 SNPs

SNPJam Report Link Image

Enzyme 2 General References

Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed ]
Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [PubMed ]

Enzyme 2 Metabolite References

Not Available

Enzyme 3 [top]

Enzyme 3 ID

5277

Enzyme 3 Name

Trifunctional enzyme subunit beta, mitochondrial precursor

Enzyme 3 Synonyms

TP-beta[Includes: 3-ketoacyl-CoA thiolase
Acetyl-CoA acyltransferase
Beta-ketothiolase]

Enzyme 3 Gene Name

HADHB

Enzyme 3 Protein Sequence

>Trifunctional enzyme subunit beta, mitochondrial precursor

MTILTYPFKNLPTASKWALRFSIRPLSCSSQLRAAPAVQTKTKKTLAKPNIRNVVVVDGV
RTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAA
LGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR
KLMLDLNKAKSMGQRLSLISKFRFNFLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLE
QDEYALRSHSLAKKAQDEGLLSDVVPFKVPGKDTVTKDNGIRPSSLEQMAKLKPAFIKPY
GTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATP
KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNW
GGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYPK

Enzyme 3 Number of Residues

474

Enzyme 3 Molecular Weight

51295

Enzyme 3 Theoretical pI

9.94

Enzyme 3 GO Classification

Not Available

Enzyme 3 General Function

Lipid transport and metabolism

Enzyme 3 Specific Function

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA

Enzyme 3 Pathways

Benzoate Degradation via Hydroxylation (map00362 )
Bile Acid Biosynthesis (map00120 )
Fatty Acid Elongation In Mitochondria (map00062 )
Fatty Acid Metabolism (map00071 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 3 Reactions

acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA

Enzyme 3 Pfam Domain Function

Thiolase_C (PF02803 )
Thiolase_N (PF00108 )

Enzyme 3 Signals

None

Enzyme 3 Transmembrane Regions

None

Enzyme 3 Essentiality

Not Available

Enzyme 3 GenBank ID Protein

862458

Enzyme 3 UniProtKB/Swiss-Prot ID

P55084

Enzyme 3 UniProtKB/Swiss-Prot Entry Name

ECHB_HUMAN Link Image

Enzyme 3 PDB ID

Not Available

Enzyme 3 Cellular Location

Not Available

Enzyme 3 Gene Sequence

>1425 bp

ATGACTATCTTGACTTACCCCTTTAAAAATCTTCCCACTGCATCAAAATGGGCCCTCAGA
TTTTCCATAAGACCTCTGAGCTGTTCCTCCCAGCTACGAGCTGCCCCAGCTGTCCAGACC
AAAACGAAGAAGACGTTAGCCAAACCCAATATAAGGAATGTTGTGGTGGTGGATGGTGTT
CGCACTCCATTTTTGCTGTCTGGCACTTCATATAAAGACCTGATGCCACATGATTTGGCT
AGAGCAGCGCTTACGGGTTTGTTGCATCGGACCAGTGTCCCTAAGGAAGTAGTTGATTAT
ATCATCTTTGGTACAGTTATTCAGGAAGTGAAAACAAGCAATGTGGCTAGAGAGGCTGCC
CTTGGAGCTGGCTTCTCTGACAAGACTCCTGCTCACACTGTCACCATGGCTTGTATCTCT
GCCAACCAAGCCATGACCACAGGTGTTGGCTTGATTGCTTCTGGCCAGTGTGATGTGATC
GTGGCAGGTGGTGTTGAGTTGATGTCCGATGTCCCTATTCGTCACTCAAGGAAAATGAGA
AAACTGATGCTTGATCTCAATAAGGCCAAATCTATGGGCCAGCGACTGTCTTTAATCTCT
AAATTCCGATTTAATTTCCTAGCACCTGAGCTCCCTGCGGTTTCTGAGTTCTCCACCAGT
GAGACCATGGGCCACTCTGCAGACCGACTGGCCGCTGCCTTTGCTGTTTCTCGGCTGGAA
CAGGATGAATATGCACTGCGCTCTCACAGTCTAGCCAAGAAGGCACAGGATGAAGGACTC
CTTTCTGATGTGGTACCCTTCAAAGTACCAGGAAAAGATACAGTTACCAAAGATAATGGC
ATCCGTCCTTCCTCACTGGAGCAGATGGCCAAACTAAAACCTGCATTCATCAAGCCCTAC
GGCACAGTGACAGCTGCAAATTCTTCTTTCTTGACTGATGGTGCATCTGCAATGTTAATC
ATGGCGGAGGAAAAGGCTCTGGCCATGGGTTATAAGCCGAAGGCATATTTGAGGGATTTT
ATGTATGTGTCTCAGGATCCAAAAGATCAACTATTACTTGGACCAACATATGCTACTCCA
AAAGTTCTAGAAAAGGCAGGATTGACCATGAATGATATTGATGCTTTTGAATTTCATGAA
GCTTTCTCGGGTCAGATTTTGGCAAATTTTAAAGCCATGGATTCTGATTGGTTTGCAGAA
AACTACATGGGTAGAAAAACCAAGGTTGGATTGCCTCCTTTGGAGAAGTTTAATAACTGG
GGTGGATCTCTGTCCCTGGGACACCCATTTGGAGCCACTGGCTGCAGGTTGGTCATGGCT
GCTGCCAACAGATTACGGAAAGAAGGAGGCCAGTATGGCTTAGTGGCTGCGTGTGCAGCT
GGAGGGCAGGGCCATGCTATGATAGTGGAAGCTTATCCAAAATAA

Enzyme 3 GenBank Gene ID

Enzyme 3 GeneCard ID

Enzyme 3 GenAtlas ID

Enzyme 3 HGNC ID

Enzyme 3 Chromosome Location

Enzyme 3 Locus

2p23

Enzyme 3 SNPs

SNPJam Report Link Image

Enzyme 3 General References

Kamijo T, Aoyama T, Komiyama A, Hashimoto T: Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein. Biochem Biophys Res Commun. 1994 Mar 15;199(2):818-25. [PubMed ]
Orii KE, Aoyama T, Wakui K, Fukushima Y, Miyajima H, Yamaguchi S, Orii T, Kondo N, Hashimoto T: Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency. Hum Mol Genet. 1997 Aug;6(8):1215-24. [PubMed ]
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
Ushikubo S, Aoyama T, Kamijo T, Wanders RJ, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both alpha- and beta-subunits. Am J Hum Genet. 1996 May;58(5):979-88. [PubMed ]

Enzyme 3 Metabolite References

Not Available

Enzyme 4 [top]

Enzyme 4 ID

5489

Enzyme 4 Name

Methylmalonyl-CoA mutase, mitochondrial precursor

Enzyme 4 Synonyms

MCM
Methylmalonyl-CoA isomerase

Enzyme 4 Gene Name

MUT

Enzyme 4 Protein Sequence

>Methylmalonyl-CoA mutase, mitochondrial precursor

MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLI
WHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESN
KFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLE
KMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMK
IIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDE
FAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTE
QDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPK
VADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARID
SGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTEC
AASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSA
IKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQ
AVDADVHAVGVSTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSN
VFGPGTRIPKAAVQVLDDIEKCLEKKQQSV

Enzyme 4 Number of Residues

750

Enzyme 4 Molecular Weight

83121

Enzyme 4 Theoretical pI

6.92

Enzyme 4 GO Classification

Function
binding catalytic activity cation binding cobalt ion binding intramolecular transferase activity ion binding isomerase activity methylmalonyl-CoA mutase activity transition metal ion binding
Process
metabolism physiological process
Component
—

Enzyme 4 General Function

Lipid transport and metabolism

Enzyme 4 Specific Function

Involved in the degradation of several amino acids, odd- chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species

Enzyme 4 Pathways

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

Enzyme 4 Reactions

(R)-methylmalonyl-CoA = succinyl-CoA

Enzyme 4 Pfam Domain Function

B12-binding (PF02310 )
MM_CoA_mutase (PF01642 )

Enzyme 4 Signals

None

Enzyme 4 Transmembrane Regions

None

Enzyme 4 Essentiality

Not Available

Enzyme 4 GenBank ID Protein

187452

Enzyme 4 UniProtKB/Swiss-Prot ID

P22033

Enzyme 4 UniProtKB/Swiss-Prot Entry Name

MUTA_HUMAN Link Image

Enzyme 4 PDB ID

Not Available

Enzyme 4 Cellular Location

Not Available

Enzyme 4 Gene Sequence

>2253 bp

ATGTTAAGAGCTAAGAATCAGCTTTTTTTACTTTCACCTCATTACCTGAGGCAGGTAAAA
GAATCATCAGGCTCCAGGCTCATACAGCAACGACTTCTACACCAGCAACAGCCCCTTCAC
CCAGAATGGGCTGCCCTGGCTAAAAAGCAGCTGAAAGGCAAAAACCCAGAAGACCTAATA
TGGCACACCCCGGAAGGGATCTCTATAAAACCCTTGTATTCCAAGAGAGATACTATGGAC
TTACCTGAAGAACTTCCAGGAGTGAAGCCATTCACACGTGGACCATATCCTACCATGTAT
ACCTTTAGGCCCTGGACCATCCGCCAGTATGCTGGTTTTAGTACTGTGGAAGAAAGCAAT
AAGTTCTATAAGGACAACATTAAGGCTGGTCAGCAGGGATTATCAGTTGCCTTTGATCTG
GCGACACATCGTGGCTATGATTCAGACAACCCTCGAGTTCGTGGTGATGTTGGAATGGCT
GGAGTTGCTATTGACACTGTGGAAGATACCAAAATTCTTTTTGATGGAATTCCTTTAGAA
AAAATGTCAGTTTCCATGACTATGAATGGAGCAGTTATTCCAGTTCTTGCAAATTTTATA
GTAACTGGAGAAGAACAAGGTGTACCTAAAGAGAAACTTACTGGTACCATCCAAAATGAT
ATACTAAAGGAATTTATGGTTCGAAATACATACATTTTTCCTCCAGAACCATCCATGAAA
ATTATTGCTGACATATTTGAATATACAGCAAAGCACATGCCAAAATTTAATTCAATTTCA
ATTAGTGGATACCATATGCAGGAAGCAGGGGCTGATGCCATTCTGGAGCTGGCCTATACT
TTAGCAGATGGATTGGAGTACTCTAGAACTGGACTCCAGGCTGGCCTGACAATTGATGAA
TTTGCACCAAGGTTGTCTTTCTTCTGGGGAATTGGAATGAATTTCTATATGGAAATAGCA
AAGATGAGAGCTGGTAGAAGACTCTGGGCTCACTTAATAGAGAAAATGTTTCAGCCTAAA
AACTCAAAATCTCTTCTTCTAAGAGCACACTGTCAGACATCTGGATGGTCACTTACTGAG
CAGGATCCCTACAATAATATTGTCCGTACTGCAATAGAAGCAATGGCAGCAGTATTTGGA
GGGACTCAGTCTTTGCACACAAATTCTTTTGATGAAGCTTTGGGTTTGCCAACTGTGAAA
AGTGCTCGAATTGCCAGGAACACACAAATCATCATTCAAGAAGAATCTGGGATTCCCAAA
GTGGCTGATCCTTGGGGAGGTTCTTACATGATGGAATGTCTCACAAATGATGTTTATGAT
GCTGCTTTAAAGCTCATTAATGAAATTGAAGAAATGGGTGGAATGGCCAAAGCTGTAGCT
GAGGGAATACCTAAACTTCGAATTGAAGAATGTGCTGCCCGAAGACAAGCTAGAATAGAT
TCTGGTTCTGAAGTAATTGTTGGAGTAAATAAGTACCAGTTGGAAAAAGAAGACGCTGTA
GAAGTTCTGGCAATTGATAATACTTCAGTGCGAAACAGGCAGATTGAAAAACTTAAGAAG
ATCAAATCCAGCAGGGATCAAGCTTTGGCTGAACATTGTCTTGCTGCACTAACCGAATGT
GCTGCTAGCGGAGATGGAAATATCCTGGCTCTTGCAGTGGATGCATCTCGGGCAAGATGT
ACAGTGGGAGAAATCACAGATGCCCTGAAAAAGGTATTTGGTGAACATAAAGCGAATGAT
CGAATGGTGAGTGGAGCATATCGCCAGGAATTTGGAGAAAGTAAAGAGATAACATCTGCT
ATCAAGAGGGTTCATAAATTCATGGAACGTGAAGGTCGCAGACCTCGTCTTCTTGTAGCA
AAAATGGGACAAGATGGCCATGACAGAGGAGCAAAAGTTATTGCTACAGGATTTGCTGAT
CTTGGTTTTGATGTGGACATAGGCCCTCTTTTCCAGACTCCTCGTGAAGTGGCCCAGCAG
GCTGTGGATGCGGATGTGCATGCTGTGGGCGTAAGCACCCTCGCTGCTGGTCATAAAACC
CTAGTTCCTGAACTCATCAAAGAACTTAACTCCCTTGGACGGCCAGATATTCTTGTCATG
TGTGGAGGGGTGATACCACCTCAGGATTATGAATTTCTGTTTGAAGTTGGTGTTTCCAAT
GTATTTGGTCCTGGGACTCGAATTCCAAAGGCTGCCGTTCAGGTGCTTGATGATATTGAG
AAGTGTTTGGAAAAGAAGCAGCAATCTGTATAA

Enzyme 4 GenBank Gene ID

Enzyme 4 GeneCard ID

Enzyme 4 GenAtlas ID

Enzyme 4 HGNC ID

Enzyme 4 Chromosome Location

Enzyme 4 Locus

6p21

Enzyme 4 SNPs

SNPJam Report Link Image

Enzyme 4 General References

Jansen R, Kalousek F, Fenton WA, Rosenberg LE, Ledley FD: Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. Genomics. 1989 Feb;4(2):198-205. [PubMed ]
Nham SU, Wilkemeyer MF, Ledley FD: Structure of the human methylmalonyl-CoA mutase (MUT) locus. Genomics. 1990 Dec;8(4):710-6. [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 ]
Crane AM, Ledley FD: Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia. Am J Hum Genet. 1994 Jul;55(1):42-50. [PubMed ]
Ledley FD, Rosenblatt DS: Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations. Hum Mutat. 1997;9(1):1-6. [PubMed ]
Raff ML, Crane AM, Jansen R, Ledley FD, Rosenblatt DS: Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation. J Clin Invest. 1991 Jan;87(1):203-7. [PubMed ]
Jansen R, Ledley FD: Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning. Am J Hum Genet. 1990 Nov;47(5):808-14. [PubMed ]
Crane AM, Jansen R, Andrews ER, Ledley FD: Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria. J Clin Invest. 1992 Feb;89(2):385-91. [PubMed ]
Crane AM, Martin LS, Valle D, Ledley FD: Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase. Hum Genet. 1992 May;89(3):259-64. [PubMed ]
Qureshi AA, Crane AM, Matiaszuk NV, Rezvani I, Ledley FD, Rosenblatt DS: Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria. J Clin Invest. 1994 Apr;93(4):1812-9. [PubMed ]
Adjalla CE, Hosack AR, Matiaszuk NV, Rosenblatt DS: A common mutation among blacks with mut- methylmalonic aciduria. Hum Mutat. 1998;Suppl 1:S248-50. [PubMed ]
Adjalla CE, Hosack AR, Gilfix BM, Lamothe E, Sun S, Chan A, Evans S, Matiaszuk NV, Rosenblatt DS: Seven novel mutations in mut methylmalonic aciduria. Hum Mutat. 1998;11(4):270-4. [PubMed ]

Enzyme 4 Metabolite References

Not Available

Enzyme 5 [top]

Enzyme 5 ID

5677

Enzyme 5 Name

2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor

Enzyme 5 Synonyms

Alpha-ketoglutarate dehydrogenase

Enzyme 5 Gene Name

OGDH

Enzyme 5 Protein Sequence

>2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor

MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFEAGLRMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRNPAAAPATGNKKTH

Enzyme 5 Number of Residues

1002

Enzyme 5 Molecular Weight

113477

Enzyme 5 Theoretical pI

7.08

Enzyme 5 GO Classification

Function
binding catalytic activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor oxoglutarate dehydrogenase (succinyl-transferring) activity thiamin pyrophosphate binding vitamin binding
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 5 General Function

Energy production and conversion

Enzyme 5 Specific Function

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

Enzyme 5 Pathways

Citrate Cycle (map00020 )
Lysine Degradation (map00310 )
Tryptophan Metabolism (map00380 )

Enzyme 5 Reactions

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2

Enzyme 5 Pfam Domain Function

E1_dh (PF00676 )
Transket_pyr (PF02779 )

Enzyme 5 Signals

None

Enzyme 5 Transmembrane Regions

None

Enzyme 5 Essentiality

Not Available

Enzyme 5 GenBank ID Protein

531241

Enzyme 5 UniProtKB/Swiss-Prot ID

Q02218

Enzyme 5 UniProtKB/Swiss-Prot Entry Name

ODO1_HUMAN Link Image

Enzyme 5 PDB ID

Not Available

Enzyme 5 Cellular Location

Not Available

Enzyme 5 Gene Sequence

>3009 bp

ATGTTTCATTTAAGGACTTGTGCTGCTAAGTTGAGGCCATTGACGGCTTCCCAGACTGTT
AAGACATTTTCACAAAACAGACCAGCAGCAGCTAGGACATTTCAACAGATTCGGTGCTAT
TCTGCACCTGTTGCTGCTGAGCCCTTTCTCAGTGGGACTAGTTCGAACTATGTGGAGGAG
ATGTACTGTGCTTGGCTGGAAAACCCCAAAAGTGTACATAAGTCATGGGACATTTTTTTT
CGCAACACGAATGCCGGAGCCCCACCGGGCACTGCCTACCAGAGTCCCCTTCCCCTGAGC
CGAGGCTCCCTGGCTGCTGTGGCCCATGCACAGTCCCTGGTAGAAGCACAGCCCAACGTG
GACAAGCTCGTGGAGGACCACCTGGCAGTGCAGTCACTCATCAGGGCATATCAGATACGA
GGGCACCATGTAGCACAGCTGGACCCCCTGGGGATTTTGGATGCTGATCTGGACTCCTCC
GTGCCCGCTGACATTATCTCATCCACAGACAAACTTGGGTTCTATGGCCTGGATGAGTCT
GACCTCGACAAGGTCTTCCACTTGCCCACCACCACTTTCATCGGGGGACAGGAATCAGCA
CTTCCTCTGCGGGAGATCATCCGTCGGCTGGAGATGGCCTACTGCCAGCATATTGGGGTG
GAGTTCATGTTCATCAATGACCTGGAGCAGTGCCAGTGGATCCGGCAGAAGTTTGAGACC
CCTGGGATCATGCAGTTCACAAATGAGGAGAAACGGACCCTGCTGGCCAGGCTTGTGCGG
TCCACCAGGTTTGAGGAGTTCCTACAGCGGAAGTGGTCCTCTGAGAAGCGCTTTGGTCTA
GAAGGCTGCGAGGTACTGATCCCTGCCCTCAAGACCATCATTGACAAGTCTAGTGAGAAT
GGCGTGGACTACGTGATCATGGGCATGCCACACAGAGGGCGGCTGAACGTGCTTGCAAAT
GTCATCAGGAAGGAGCTGGAACAGATCTTCTGTCAATTCGATTCAAAGCTGGAGGCAGCT
GATGAGGGCTCCGGAGATGTGAAGTACCACCTGGGCATGTATCACCGCAGGATCAATCGT
GTCACCGACAGGAACATTACCTTGTCCTTGGTGGCCAACCCTTCCCACCTTGAGGCCGCT
GACCCCGTGGTGATGGGCAAGACCAAAGCCGAACAGTTTTACTGTGGCGACACTGAAGGG
AAAAAGGTCATGTCCATCCTGTTGCATGGGGATGCTGCATTTGCTGGCCAGGGCATTGTG
TACGAGACCTTCCACCTCAGCGACCTGCCATCCTACACAACTCATGGCACCGTGCACGTG
GTCGTCAACAACCAGATCGGCTTCACCACCGACCCTCGGATGGCCCGCTCCTCCCCCTAC
CCCACTGACGTGGCCCGAGTGGTGAATGCCCCCATTTTCCACGTGAACTCAGATGACCCC
GAGGCTGTCATGTACGTGTGCAAAGTGGCGGCCGAGTGGAGGAGCACCTTCCACAAGGAC
GTGGTTGTCGATTTGGTGTGTTACCGGCGCAACGGCCACAACGAGATGGATGAGCCCATG
TTCACGCAGCCGCTCATGTACAAGCAGATCCGCAAGCAGAAGCCTGTGTTACAGAAGTAC
GCTGAGCTGCTGGTGTCGCAGGGTGTGGTCAACCAGCCTGAGTATGAGGAGGAAATTTCC
AAGTATGATAAGATCTGTGAGGAAGCTTTTGCCAGATCTAAAGATGAGAAGATCTTGCAC
ATTAAGCACTGGCTGGACTCTCCCTGGCCTGGCTTCTTCACCCTGGACGGGCAGCCCAGG
AGCATGTCCTGCCCCTCCACGGGTCTGACGGAGGATATTCTGACACACATCGGGAATGTG
GCTAGTTCTGTGCCTGTGGAAAACTTTACTATTCATGGAGGGCTGAGCCGGATCTTGAAG
ACTCGTGGGGAAATGGTGAAGAACCGGACTGTGGACTGGGCTCTAGCGGAGTACATGGCG
TTTGGCTCGCTCCTGAAGGAGGGCATCCACATTCGGCTGAGCGGCCAGGACGTGGAGCGG
GGCACATTCAGCCACCGCCACCATGTGCTCCATGACCAGAATGTGGACAAGAGAACCTGC
ATCCCCATGAACCATCTCTGGCCCAATCAGGCCCCCTATACTGTGTGCAACAGCTCACTG
TCTGAGTACGGCGTGCTGGGCTTTGAAGCTGGGCTTCGCATGGCCAGTCCTAATGCCCTG
GTCCTCTGGGAAGCCCAATTTGGTGACTTCCACAACACGGCCCAGTGTATCATCGACCAG
TTCATCTGCCCGGGACAAGCCAAGTGGGTGCGGCAGAATGGCATCGTGTTGCTGCTGCCC
CATGGCATGGAGGGCATGGGTCCAGAACATTCCTCCGCCCGCCCAGAGCGGTTCTTGCAG
ATGTGCAACGATGACCCAGATGTCCTGCCAGACCTTAAAGAAGCCAACTTCGACATCAAT
CAGCTATATGACTGCAATTGGGTTGTTGTCAACTGCTCCACTCCTGGCAACTTCTTCCAC
GTGCTACGACGCCAGATCCTGCTGCCATTCCGGAAGCCGTTAATTATCTTCACCCCCAAA
TCCCTGTTGCGCCACCCCGAGGCCAGATCCAGCTTTGATGAGATGCTTCCAGGAACCCAC
TTCCAGCGGGTGATCCCAGAAGATGGCCCTGCAGCTCAGAACCCAGAAAATGTCAAAAGG
CTTCTCTTCTGCACCGGCAAAGTGTATTATGACCTCACCCGGGAGCGCAAAGCACGCGAC
ATGGTGGGGCAGGTGGCCATCACAAGGATTGAGCAGCTGTCGCCATTCCCCTTTGACCTC
CTGCTGAAGGAGGTGCAGAAGTACCCCAATGCTGAGCTGGCCTGGTGCCAGGAGGAGCAC
AAGAACCAAGGCTACTATGACTACGTGAAGCCAAGACTTCGGACCACCATCAGCCGCGCC
AAGCCCGTCTGGTATGCCGGCCGGAACCCAGCGGCTGCTCCAGCCACCGGCAACAAGAAG
ACCCACTGA

Enzyme 5 GenBank Gene ID

Enzyme 5 GeneCard ID

Enzyme 5 GenAtlas ID

Enzyme 5 HGNC ID

Enzyme 5 Chromosome Location

Enzyme 5 Locus

7p14-p13

Enzyme 5 SNPs

SNPJam Report Link Image

Enzyme 5 General References

Koike K, Urata Y, Goto S: Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1963-7. [PubMed ]
Koike K: The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14. Gene. 1995 Jul 4;159(2):261-6. [PubMed ]

Enzyme 5 Metabolite References

Not Available

Enzyme 6 [top]

Enzyme 6 ID

5985

Enzyme 6 Name

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor

Enzyme 6 Synonyms

Somatic-type succinyl CoA:3-oxoacid CoA- transferase
Scot-S

Enzyme 6 Gene Name

OXCT1

Enzyme 6 Protein Sequence

>Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial precursor

MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVL
VGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENA
EFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSV
AIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAET
TVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDD
VRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEAD
ADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMV
KGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDK
KKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN

Enzyme 6 Number of Residues

520

Enzyme 6 Molecular Weight

56158

Enzyme 6 Theoretical pI

7.52

Enzyme 6 GO Classification

Function
CoA-transferase activity catalytic activity transferase activity transferase activity, transferring sulfur-containing groups
Process
metabolism physiological process
Component
—

Enzyme 6 General Function

Lipid transport and metabolism

Enzyme 6 Specific Function

Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate

Enzyme 6 Pathways

Butyrate Metabolism (map00650 )
Synthesis and Degradation of Ketone Bodies (map00072 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 6 Reactions

succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA

Enzyme 6 Pfam Domain Function

CoA_trans (PF01144 )

Enzyme 6 Signals

1-22

Enzyme 6 Transmembrane Regions

Not Available

Enzyme 6 Essentiality

Not Available

Enzyme 6 GenBank ID Protein

1519052

Enzyme 6 UniProtKB/Swiss-Prot ID

P55809

Enzyme 6 UniProtKB/Swiss-Prot Entry Name

SCOT_HUMAN Link Image

Enzyme 6 PDB ID

1OOY

Enzyme 6 PDB File

Show

Enzyme 6 3D Structure

Enzyme 6 Cellular Location

Not Available

Enzyme 6 Gene Sequence

>1563 bp

ATGGCGGCTCTCAAACTCCTCTCCTCCGGGCTTCGGCTCTGCGCCTCTGCCCGCGGATCT
GGGGCAACCTGGTACAAGGGATGTGTTTGTTCCTTTTCCACCAGTGCTCATCGCCATACC
AAGTTTTATACAGATCCAGTAGAAGCTGTAAAAGACATCCCTGATGGTGCCACGGTTTTG
GTTGGTGGTTTTGGGCTATGTGGAATTCCAGAGAATCTTATAGATGCTTTACTGAAAACT
GGAGTAAAAGGACTAACTGCAGTCAGCAACAATGCAGGGGTTGACAATTTTGGTTTGGGG
CTTTTGCTTCGGTCGAAGCAGATAAAACGCATGGTCTCTTCATATGTGGGAGAAAATGCA
GAATTTGAACGACAGTACTTATCTGGTGAATTAGAAGTGGAGCTGACACCACAGGGCACA
CTTGCAGAGAGGATCCGTGCAGGCGGGGCTGGAGTTCCTGCATTTTACACCCCAACAGGG
TATGGGACCCTGGTACAAGAAGGAGGATCGCCCATCAAATACAACAAAGATGGCAGTGTT
GCCATTGCCAGTAAGCCAAGAGAGGTGAGGGAGTTCAATGGTCAGCACTTTATTTTGGAG
GAAGCAATTACAGGGGATTTTGCTTTGGTGAAAGCCTGGAAGGCGGACCGAGCAGGAAAC
GTGATTTTCAGGAAAAGTGCAAGGAATTTCAACTTGCCAATGTGCAAAGCTGCAGAAACC
ACAGTGGTAGAGGTTGAAGAAATTGTGGATATTGGAGCATTTGCTCCAGAAGACATCCAT
ATTCCTCAGATTTATGTACATCGCCTTATAAAGGGAGAAAAATATGAGAAAAGAATTGAG
CGTTTATCAATCCGGAAAGAGGGAGATGGGGAAGCCAAATCTGCTAAACCTGGAGATGAC
GTAAGGGAACGAATCATCAAGAGGGCCGCTCTTGAGTTTGAGGATGGCATGTATGCTAAT
TTGGGCATAGGAATCCCTCTCCTGGCCAGCAATTTTATCAGCCCAAATATAACTGTTCAT
CTTCAAAGTGAAAATGGAGTTCTGGGTTTGGGTCCATATCCACGACAACATGAAGCTGAT
GCAGATCTCATCAATGCAGGCAAGGAAACAGTTACTATTCTTCCAGGAGCCTCTTTTTTC
TCCAGCGATGAATCATTTGCAATGATTAGAGGTGGACACGTCGATCTGACAATGCTAGGA
GCGATGCAGGTTTCCAAATATGGTGACCTGGCTAACTGGATGATACCTGGGAAGATGGTG
AAAGGAATGGGAGGTGCTATGGATTTAGTGTCCAGTGCGAAAACCAAAGTGGTGGTCACC
ATGGAGCATTCTGCAAAGGGAAATGCACATAAAATCATGGAGAAATGTACATTACCATTG
ACTGGAAAGCAATGTGTCAACCGCATTATTACTGAAAAGGCTGTGTTTGATGTGGACAAG
AAGAAAGGGTTGACTCTGATTGAGCTCTGGGAAGGCCTGACAGTGGATGACGTACAAAAG
AGTACTGGGTGTGATTTTGCAGTTTCACCAAAACTCATGCCAATGCAGCAGATCGCAAAT
TGA

Enzyme 6 GenBank Gene ID

Enzyme 6 GeneCard ID

Enzyme 6 GenAtlas ID

Enzyme 6 HGNC ID

Enzyme 6 Chromosome Location

Enzyme 6 Locus

5p13.1

Enzyme 6 SNPs

SNPJam Report Link Image

Enzyme 6 General References

Kassovska-Bratinova S, Fukao T, Song XQ, Duncan AM, Chen HS, Robert MF, Perez-Cerda C, Ugarte M, Chartrand C, Vobecky S, Kondo N, Mitchell GA: Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient. Am J Hum Genet. 1996 Sep;59(3):519-28. [PubMed ]
Fukao T, Mitchell GA, Song XQ, Nakamura H, Kassovska-Bratinova S, Orii KE, Wraith JE, Besley G, Wanders RJ, Niezen-Koning KE, Berry GT, Palmieri M, Kondo N: Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. Genomics. 2000 Sep 1;68(2):144-51. [PubMed ]
Song XQ, Fukao T, Watanabe H, Shintaku H, Hirayama K, Kassovska-Bratinova S, Kondo N, Mitchell GA: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings. Hum Mutat. 1998;12(2):83-8. [PubMed ]

Enzyme 6 Metabolite References

Not Available

Enzyme 7 [top]

Enzyme 7 ID

5988

Enzyme 7 Name

Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor

Enzyme 7 Synonyms

Testis-specific succinyl CoA:3-oxoacid CoA- transferase
SCOT-t

Enzyme 7 Gene Name

OXCT2

Enzyme 7 Protein Sequence

>Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial precursor

MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVM
IGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENT
LCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHL
ALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADV
TAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDART
RIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADL
INAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGM
GGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKE
LTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP

Enzyme 7 Number of Residues

517

Enzyme 7 Molecular Weight

56141

Enzyme 7 Theoretical pI

7.15

Enzyme 7 GO Classification

Function
CoA-transferase activity catalytic activity transferase activity transferase activity, transferring sulfur-containing groups
Process
metabolism physiological process
Component
—

Enzyme 7 General Function

Lipid transport and metabolism

Enzyme 7 Specific Function

Enzyme 7 Pathways

Butyrate Metabolism (map00650 )
Synthesis and Degradation of Ketone Bodies (map00072 )
Valine, Leucine and Isoleucine Degradation (map00280 )

Enzyme 7 Reactions

succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA

Enzyme 7 Pfam Domain Function

CoA_trans (PF01144 )

Enzyme 7 Signals

1-21

Enzyme 7 Transmembrane Regions

Not Available

Enzyme 7 Essentiality

Not Available

Enzyme 7 GenBank ID Protein

118026874

Enzyme 7 UniProtKB/Swiss-Prot ID

Q9BYC2

Enzyme 7 UniProtKB/Swiss-Prot Entry Name

SCOT2_HUMAN Link Image

Enzyme 7 PDB ID

Not Available

Enzyme 7 Cellular Location

Not Available

Enzyme 7 Gene Sequence

>1554 bp

ATGGCGGCGCTGCGGCTCCTGGCGTCAGTGCTCGGGCGCGGGGTCCCCGCCGGCGGCTCA
GGGCTCGCGCTGTCCCAGGGCTGCGCCCGCTGCTTTGCCACCAGTCCCCGGCTCCGTGCC
AAGTTCTACGCGGACCCGGTGGAGATGGTGAAGGACATCTCTGACGGGGCGACCGTCATG
ATCGGGGGCTTCGGGCTCTGCGGGATCCCCGAGAACCTGATCGCCGCGCTGCTCAGGACC
CGCGTGAAAGACCTGCAGGTGGTCAGCAGCAACGTGGGCGTGGAGGACTTCGGCCTGGGC
CTCCTGCTGGCCGCCAGGCAGGTCCGTCGCATCGTCTGTTCCTACGTGGGCGAGAACACC
CTGTGCGAGAGCCAGTACCTGGCAGGAGAGCTGGAGCTGGAGCTCACGCCCCAGGGCACC
CTGGCCGAGCGCATCCGCGCGGGGGGCGCCGGGGTGCCCGCCTTCTACACCCCCACGGGC
TACGGGACCCTGGTCCAGGAAGGGGGCGCCCCCATCCGCTACACCCCGGACGGCCACCTG
GCGCTCATGAGCCAGCCCCGAGAGGTGAGGGAGTTCAACGGCGACCACTTCCTTTTGGAG
CGCGCCATCCGGGCAGACTTCGCCCTGGTGAAAGGGTGGAAGGCCGACCGGGCAGGAAAC
GTGGTCTTCAGGAGAAGCGCCCGCAATTTCAACGTGCCCATGTGCAAAGCTGCAGACGTC
ACGGCGGTGGAGGTGGAAGAGATCGTGGAGGTGGGGGCTTTCCCCCCAGAAGACATCCAC
GTTCCTAACATTTATGTAGATCGCGTGATAAAGGGGCAGAAATACGAGAAACGAATTGAG
CGCTTAACGATCCTGAAAGAGGAAGATGGAGACGCTGGAAAGGAAGAGGACGCCAGGACG
CGCATCATCAGACGCGCAGCTCTGGAATTTGAGGACGGCATGTACGCCAATCTGGGCATA
GGCATCCCCCTGCTGGCCAGCAACTTCATCAGTCCCAGCATGACTGTCCATCTTCACAGT
GAGAACGGGATCCTGGGCCTGGGCCCGTTTCCCACGGAAGATGAGGTGGATGCCGACCTC
ATCAATGCAGGCAAGCAGACGGTCACGGTGCTTCCCGGGGGCTGCTTCTTCGCCAGCGAC
GACTCCTTCGCCATGATCCGAGGGGGACACATCCAACTAACCATGCTTGGAGCCATGCAG
GTTTCCAAATACGGCGACCTGGCGAACTGGATGATCCCTGGCAAGAAGGTGAAAGGCATG
GGCGGTGCCATGGACTTGGTGTCCAGTCAGAAGACCAGAGTGGTGGTCACCATGCAGCAC
TGCACAAAGGACAACACCCCCAAGATCATGGAGAAATGCACCATGCCGCTGACCGGGAAG
CGGTGCGTGGACCGCATCATCACCGAGAAGGCCGTGTTTGACGTGCACAGGAAGAAAGAG
CTGACGCTGAGGGAGCTCTGGGAGGGCCTGACGGTGGACGACATCAAAAAGAGCACGGGG
TGTGCCTTTGCTGTGTCCCCGAACCTCAGGCCCATGCAGCAGGTGGCACCCTGA

Enzyme 7 GenBank Gene ID

AB050193

Enzyme 7 GeneCard ID

OXCT2

Enzyme 7 GenAtlas ID

OXCT2

Enzyme 7 HGNC ID

HGNC:18606 Link Image

Enzyme 7 Chromosome Location

Enzyme 7 Locus

1p34

Enzyme 7 SNPs

SNPJam Report Link Image

Enzyme 7 General References

Not Available

Enzyme 7 Metabolite References

Not Available

Enzyme 8 [top]

Enzyme 8 ID

6171

Enzyme 8 Name

Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor

Enzyme 8 Synonyms

Succinyl-CoA synthetase subunit alpha
SCS- alpha

Enzyme 8 Gene Name

SUCLG1

Enzyme 8 Protein Sequence

>Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor

MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML

Enzyme 8 Number of Residues

333

Enzyme 8 Molecular Weight

35048

Enzyme 8 Theoretical pI

9.24

Enzyme 8 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 8 General Function

Energy production and conversion

Enzyme 8 Specific Function

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA

Enzyme 8 Pathways

Citrate Cycle (map00020 )
Propanoate Metabolism (map00640 )

Enzyme 8 Reactions

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA

Enzyme 8 Pfam Domain Function

CoA_binding (PF02629 )
Ligase_CoA (PF00549 )

Enzyme 8 Signals

1-19

Enzyme 8 Transmembrane Regions

Not Available

Enzyme 8 Essentiality

Not Available

Enzyme 8 GenBank ID Protein

9409794

Enzyme 8 UniProtKB/Swiss-Prot ID

P53597

Enzyme 8 UniProtKB/Swiss-Prot Entry Name

SUCA_HUMAN Link Image

Enzyme 8 PDB ID

1EUC

Enzyme 8 PDB File

Show

Enzyme 8 3D Structure

Enzyme 8 Cellular Location

Not Available

Enzyme 8 Gene Sequence

>1002 bp

ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA

Enzyme 8 GenBank Gene ID

AF104921

Enzyme 8 GeneCard ID

SUCLG1

Enzyme 8 GenAtlas ID

SUCLG1

Enzyme 8 HGNC ID

HGNC:11449 Link Image

Enzyme 8 Chromosome Location

Enzyme 8 Locus

2p11.2

Enzyme 8 SNPs

SNPJam Report Link Image

Enzyme 8 General References

James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed ]

Enzyme 8 Metabolite References

Not Available

Enzyme 9 [top]

Enzyme 9 ID

6173

Enzyme 9 Name

Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor

Enzyme 9 Synonyms

Succinyl-CoA synthetase, betaG chain
SCS-betaG
GTP- specific succinyl-CoA synthetase subunit beta

Enzyme 9 Gene Name

SUCLG2

Enzyme 9 Protein Sequence

>Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor

MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK

Enzyme 9 Number of Residues

432

Enzyme 9 Molecular Weight

46511

Enzyme 9 Theoretical pI

6.18

Enzyme 9 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 9 General Function

Energy production and conversion

Enzyme 9 Specific Function

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA

Enzyme 9 Pathways

Citrate Cycle (map00020 )
Propanoate Metabolism (map00640 )

Enzyme 9 Reactions

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA

Enzyme 9 Pfam Domain Function

ATP-grasp_2 (PF08442 )
Ligase_CoA (PF00549 )

Enzyme 9 Signals

1-29

Enzyme 9 Transmembrane Regions

Not Available

Enzyme 9 Essentiality

Not Available

Enzyme 9 GenBank ID Protein

133777003

Enzyme 9 UniProtKB/Swiss-Prot ID

Q96I99

Enzyme 9 UniProtKB/Swiss-Prot Entry Name

SUCB2_HUMAN Link Image

Enzyme 9 PDB ID

1EUC

Enzyme 9 PDB File

Show

Enzyme 9 3D Structure

Enzyme 9 Cellular Location

Not Available

Enzyme 9 Gene Sequence

>1155 bp

ATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTTGTAGCAGACACTGCAAATGAAGCT
CTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATTGTTTTAAAAGCCCAGATCTTAGCT
GGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTGAAAGGAGGTGTTCATTTAACAAAA
GACCCTAATGTTGTGGGACAGCTGGCTAAACAGATGATTGGGTACAATCTAGCGACAAAA
CAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTGATGGTTGCTGAAGCCTTGGATATT
TCCAGAGAAACCTACCTGGCAATTCTGATGGACCGGTCCTGCAATGGCCCCGTGCTGGTG
GGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTGGCTGCTTCAAACCCGGAGCTCATT
TTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAGGACAGCCAAGCTCAGCGGATGGCC
GAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAGGCTGCAGATCAAATTACGAAGCTG
TATAATCTCTTCCTGAAAATTGATGCTACTCAGGTGGAAGTGAATCCCTTTGGTGAAACT
CCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATAAACTTTGATGACAACGCAGAATTC
CGACAAAAAGACATATTTGCTATGGACGACAAATCAGAGAATGAGCCCATTGAAAATGAA
GCTGCCAAATATGATCTAAAATACATAGGACTAGATGGGAACATTGCCTGCTTTGTGAAT
GGTGCTGGGCTCGCCATGGCTACTTGTGATATCATTTTCCTTAATGGTGGGAAGCCAGCC
AACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCTCAAGTATATCAAGCATTCAAATTG
CTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTCAATATATTTGGTGGTATCGTCAAC
TGTGCCATCATTGCCAATGGGATCACCAAAGCCTGCCGGGAGCTAGAACTCAAGGTGCCC
CTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAGGCCCAGAAGATACTCAACAACAGC
GGACTCCCCATTACTTCAGCCATTGACCTGGAGGATGCAGCCAAGAAGGCTGTGGCCAGT
GTGGCCAAGAAGTGA

Enzyme 9 GenBank Gene ID

BC007716

Enzyme 9 GeneCard ID

SUCLG2

Enzyme 9 GenAtlas ID

SUCLG2

Enzyme 9 HGNC ID

HGNC:11450 Link Image

Enzyme 9 Chromosome Location

Enzyme 9 Locus

3p14.1

Enzyme 9 SNPs

SNPJam Report Link Image

Enzyme 9 General References

Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed ]

Enzyme 9 Metabolite References

Not Available

Enzyme 10 [top]

Enzyme 10 ID

6227

Enzyme 10 Name

Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex, mitochondrial precursor

Enzyme 10 Synonyms

Dihydrolipoamide succinyltransferase component of 2- oxoglutarate dehydrogenase complex
E2
E2K

Enzyme 10 Gene Name

DLST

Enzyme 10 Protein Sequence

>Dihydrolipoyllysine-residue succinyltransferase component of 2- oxoglutarate dehydrogenase complex, mitochondrial precursor

MLSRSRCVSRAFSAPLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFF
RTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAN
GVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPI
PTQMPPVPSPSQPPSGKPVSAVKPTVAPPLADAGAGKGLRSEHREKMNRMRQRIAQRLKE
AQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNA
VIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA
IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVAL
TYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL

Enzyme 10 Number of Residues

453

Enzyme 10 Molecular Weight

48641

Enzyme 10 Theoretical pI

9.20

Enzyme 10 GO Classification

Function
S-acyltransferase activity S-succinyltransferase activity acyltransferase activity catalytic activity dihydrolipoyllysine-residue succinyltransferase activity transferase activity transferase activity, transferring acyl groups transferase activity, transferring groups other than amino-acyl groups
Process
cellular metabolism energy derivation by oxidation of organic compounds generation of precursor metabolites and energy main pathways of carbohydrate metabolism metabolism physiological process tricarboxylic acid cycle
Component
oxoglutarate dehydrogenase complex protein complex

Enzyme 10 General Function

Energy production and conversion

Enzyme 10 Specific Function

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components:2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3)

Enzyme 10 Pathways

Citrate Cycle (map00020 )
Lysine Degradation (map00310 )

Enzyme 10 Reactions

succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine

Enzyme 10 Pfam Domain Function

2-oxoacid_dh (PF00198 )
Biotin_lipoyl (PF00364 )

Enzyme 10 Signals

None

Enzyme 10 Transmembrane Regions

None

Enzyme 10 Essentiality

Not Available

Enzyme 10 GenBank ID Protein

499719

Enzyme 10 UniProtKB/Swiss-Prot ID

P36957

Enzyme 10 UniProtKB/Swiss-Prot Entry Name

ODO2_HUMAN Link Image

Enzyme 10 PDB ID

Not Available

Enzyme 10 Cellular Location

Not Available

Enzyme 10 Gene Sequence

>1362 bp

ATGCTGTCCCGATCCCGCTGTGTGTCTCGGGCGTTCAGCGCTCCGCTCTCCGCCTTCCAG
AAGGGGAACTGCCCTCTAGGGAGACGTTCCCTGCCTGGGGTCTCCTTATGCCAGGGACCA
GGTTACCCTAACAGCAGGAAGGTTGTCATTAACAACAGTGTCTTCAGTGTTCGCTTTTTC
AGAACTACAGCTGTATGCAAGGATGACTTGGTTACAGTCAAAACCCCAGCGTTTGCAGAA
TCTGTCACAGAGGGAGATGTCAGGTGGGAGAAAGCTGTTGGAGACACAGTTGCAGAAGAT
GAAGTGGTTTGTGAGATTGAAACTGACAAGACATCTGTGCAGGTTCCATCACCAGCAAAT
GGCGTGATTGAAGCTCTTTTGGTACCTGATGGGACAAAAGTCGAAGGAGGCACTCCACTT
TTCACACTCAGGAAAACTGGTGCTGCTCCTGCTAAGGCCAAGCCGGCTGAAGCTCCTGCT
GCTGCAGCCCCAAAAGCAGAACCTACAGCAGCGGCAGTTCCTCCCCCTGCAGCACCCATA
CCCACTCAGATGCCACCGGTGCCCTCGCCCTCACAGCCTCCTTCTGGCAAACCTGTGTCT
GCAGTAAAACCCACTGTTGCCCCACCACTAGCTGACGCAGGAGCTGGCAAAGGTCTGCGT
TCAGAACATCGGGAGAAAATGAACAGGATGCGGCAACGCATTGCTCAGCGTCTGAAGGAG
GCCCAGAATACATGTGCAATGCTGACAACTTTTAATGAGATTGACATGAGTAACATCCAG
GAGATGAGGGCTCGGCACAAAGAGGCTTTTTTGAAGAAACATAACCTCAAACTAGGCTTC
ATGTCGGCATTTGTGAAGGCCTCAGCCTTTGCCTTGCAGGAACAGCCTGTTGTAAATGCA
GTGATTGACGACACAACCAAAGAGGTGGTGTATAGGGATTATATTGACATCAGTGTTGCA
GTGGCCACCCCAAGGGGTCTGGTGGTTCCAGTCATCAGGAATGTGGAAGCTATGAATTTT
GCAGATATTGAACGGACCATCACTGAACTGGGAGAGAAGGCCCGAAAGAATGAACTTGCC
ATTGAAGATATGGATGGCGGTACCTTCACCATTAGCAATGGAGGCGTTTTTGGCTCGCTC
TTTGGAACAACCATTATCAACCCCCCTCAGTCTGCCATCCTGGGGATGCATGGCATCTTT
GACAGGCCAGTGGCTATAGGAGGCAAGGTAGAGGTGCGGCCCATGATGTACGTGGCACTG
ACCTATGATCACCGGCTGATTGATGGCAGAGAGGCTGTGACTTTCCTCCGCAAAATCAAG
GCAGCGGTAGAGGATCCCAGAGTCCTCCTCCTGGATCTTTAG

Enzyme 10 GenBank Gene ID

D16373

Enzyme 10 GeneCard ID

DLST

Enzyme 10 GenAtlas ID

DLST

Enzyme 10 HGNC ID

HGNC:2911

Enzyme 10 Chromosome Location

Enzyme 10 Locus

14q24.3

Enzyme 10 SNPs

SNPJam Report Link Image

Enzyme 10 General References

Nakano K, Matuda S, Sakamoto T, Takase C, Nakagawa S, Ohta S, Ariyama T, Inazawa J, Abe T, Miyata T: Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. Biochim Biophys Acta. 1993 Dec 14;1216(3):360-8. [PubMed ]
Nakano K, Takase C, Sakamoto T, Nakagawa S, Inazawa J, Ohta S, Matuda S: Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur J Biochem. 1994 Aug 15;224(1):179-89. [PubMed ]

Enzyme 10 Metabolite References

Not Available

Enzyme 11 [top]

Enzyme 11 ID

6259

Enzyme 11 Name

Succinyl-CoA ligase [ADP-forming] beta-chain, mitochondrial precursor

Enzyme 11 Synonyms

Succinyl-CoA synthetase, betaA chain
SCS-betaA
ATP- specific succinyl-CoA synthetase subunit beta
Renal carcinoma antigen NY-REN-39

Enzyme 11 Gene Name

SUCLA2

Enzyme 11 Protein Sequence

>Succinyl-CoA ligase [ADP-forming] beta-chain, mitochondrial precursor

MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI

Enzyme 11 Number of Residues

463

Enzyme 11 Molecular Weight

50318

Enzyme 11 Theoretical pI

7.50

Enzyme 11 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 11 General Function

Energy production and conversion

Enzyme 11 Specific Function

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA

Enzyme 11 Pathways

C5-Branched Dibasic Acid Metabolism (map00660 )
Citrate Cycle (map00020 )
Propanoate Metabolism (map00640 )

Enzyme 11 Reactions

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA

Enzyme 11 Pfam Domain Function

ATP-grasp_2 (PF08442 )
Ligase_CoA (PF00549 )

Enzyme 11 Signals

None

Enzyme 11 Transmembrane Regions

None

Enzyme 11 Essentiality

Not Available

Enzyme 11 GenBank ID Protein

7328935

Enzyme 11 UniProtKB/Swiss-Prot ID

Q9P2R7

Enzyme 11 UniProtKB/Swiss-Prot Entry Name

SUCB1_HUMAN Link Image

Enzyme 11 PDB ID

Not Available

Enzyme 11 Cellular Location

Not Available

Enzyme 11 Gene Sequence

>1392 bp

ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA

Enzyme 11 GenBank Gene ID

AB035863

Enzyme 11 GeneCard ID

SUCLA2

Enzyme 11 GenAtlas ID

SUCLA2

Enzyme 11 HGNC ID

HGNC:11448 Link Image

Enzyme 11 Chromosome Location

Enzyme 11 Locus

13q12.2-q13.3

Enzyme 11 SNPs

SNPJam Report Link Image

Enzyme 11 General References

Furuyama K, Sassa S: Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000 Mar;105(6):757-64. [PubMed ]
Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed ]
Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed ]

Enzyme 11 Metabolite References

Not Available

Enzyme 12 [top]

Enzyme 12 ID

8557

Enzyme 12 Name

Succinate-CoA ligase, ADP-forming, beta subunit

Enzyme 12 Synonyms

Not Available

Enzyme 12 Gene Name

SUCLA2

Enzyme 12 Protein Sequence

>Succinate-CoA ligase, ADP-forming, beta subunit

MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI

Enzyme 12 Number of Residues

463

Enzyme 12 Molecular Weight

50318

Enzyme 12 Theoretical pI

7.50

Enzyme 12 GO Classification

Function
catalytic activity
Process
metabolism physiological process
Component
—

Enzyme 12 General Function

Energy production and conversion

Enzyme 12 Specific Function

Not Available

Enzyme 12 Pathways

Not Available

Enzyme 12 Reactions

Not Available

Enzyme 12 Pfam Domain Function

ATP-grasp_2 (PF08442 )
Ligase_CoA (PF00549 )

Enzyme 12 Signals

Not Available

Enzyme 12 Transmembrane Regions

Not Available

Enzyme 12 Essentiality

Not Available

Enzyme 12 GenBank ID Protein

55957259

Enzyme 12 UniProtKB/Swiss-Prot ID

Q5T9Q4

Enzyme 12 UniProtKB/Swiss-Prot Entry Name

Q5T9Q4_HUMAN Link Image

Enzyme 12 PDB ID

Not Available

Enzyme 12 Cellular Location

Not Available

Enzyme 12 Gene Sequence

>1326 bp

ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGTATGGAA
TTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCAGATGAA
GCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAGGTTTTA
GCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAGATAGTT
TTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTGTTTACC
AAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGAAAATAT
CCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCTGTATTA
ATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCTGAAGCA
ATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTCCAGCTT
GCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATGGTCAAG
CTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATGGTGGAA
GATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAATTCAGCC
TATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGGGACAAA
GATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGCCTAGTA
AATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGGACTCCA
GCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCATTTAAG
CTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGAATCATG
CGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATTAAAATA
CCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATAGCGGAC
AGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTTGTAAAG
CTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAGTTGCCA
ATATGA

Enzyme 12 GenBank Gene ID

AL157369

Enzyme 12 GeneCard ID

SUCLA2

Enzyme 12 GenAtlas ID

SUCLA2

Enzyme 12 HGNC ID

HGNC:11448 Link Image

Enzyme 12 Chromosome Location

Enzyme 12 Locus

13q12.2-q13.3

Enzyme 12 SNPs

SNPJam Report Link Image

Enzyme 12 General References

Not Available

Enzyme 12 Metabolite References

Not Available

Enzyme 13 [top]

Enzyme 13 ID

13017

Enzyme 13 Name

Alpha-KG-E2

Enzyme 13 Synonyms

Dihydrolipoamide S-succinyltransferase
E2 component of 2-oxo-glutarate complex, isoform CRA_a
cDNA FLJ75101, highly similar to Homo sapiens dihydrolipoamide S-succinyltransferase
E2 component of 2-oxo-glutarate complex
DLST, mRNA

Enzyme 13 Gene Name

alpha=KG-E2

Enzyme 13 Protein Sequence

>Alpha-KG-E2

MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFF
RTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPAN
GVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPI
PTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKE
AQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNA
VIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELA
IEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVAL
TYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL

Enzyme 13 Number of Residues

453

Enzyme 13 Molecular Weight

48756

Enzyme 13 Theoretical pI

9.39

Enzyme 13 GO Classification

Function
S-acyltransferase activity S-succinyltransferase activity acyltransferase activity catalytic activity dihydrolipoyllysine-residue succinyltransferase activity transferase activity transferase activity, transferring acyl groups transferase activity, transferring groups other than amino-acyl groups
Process
cellular metabolism energy derivation by oxidation of organic compounds generation of precursor metabolites and energy main pathways of carbohydrate metabolism metabolism physiological process tricarboxylic acid cycle
Component
oxoglutarate dehydrogenase complex protein complex

Enzyme 13 General Function

Energy production and conversion

Enzyme 13 Specific Function

Not Available

Enzyme 13 Pathways

Not Available

Enzyme 13 Reactions

Not Available

Enzyme 13 Pfam Domain Function

2-oxoacid_dh (PF00198 )
Biotin_lipoyl (PF00364 )

Enzyme 13 Signals

None

Enzyme 13 Transmembrane Regions

None

Enzyme 13 Essentiality

Not Available

Enzyme 13 GenBank ID Protein

Not Available

Enzyme 13 UniProtKB/Swiss-Prot ID

Q7LDY7

Enzyme 13 UniProtKB/Swiss-Prot Entry Name

Q7LDY7_HUMAN Link Image

Enzyme 13 PDB ID

Not Available

Enzyme 13 Cellular Location

Not Available

Enzyme 13 Gene Sequence

Not Available

Enzyme 13 GenBank Gene ID

AC006530

Enzyme 13 GeneCard ID

Q7LDY7

Enzyme 13 GenAtlas ID

DLST

Enzyme 13 HGNC ID

HGNC:2911

Enzyme 13 Chromosome Location

Not Available

Enzyme 13 Locus

Not Available

Enzyme 13 SNPs

SNPJam Report Link Image

Enzyme 13 General References

Not Available

Enzyme 13 Metabolite References

Not Available

Enzyme 14 [top]

Enzyme 14 ID

14717

Enzyme 14 Name

cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase

Enzyme 14 Synonyms

Aminolevulinate, delta-, synthase 2
Sideroblastic/hypochromic anemia, isoform CRA_c

Enzyme 14 Gene Name

ALAS2

Enzyme 14 Protein Sequence

>cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase

MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA

Enzyme 14 Number of Residues

587

Enzyme 14 Molecular Weight

64634

Enzyme 14 Theoretical pI

8.19

Enzyme 14 GO Classification

Not Available

Enzyme 14 General Function

Coenzyme transport and metabolism

Enzyme 14 Specific Function

Not Available

Enzyme 14 Pathways

Not Available

Enzyme 14 Reactions

Not Available

Enzyme 14 Pfam Domain Function

Not Available

Enzyme 14 Signals

1-15

Enzyme 14 Transmembrane Regions

None

Enzyme 14 Essentiality

Not Available

Enzyme 14 GenBank ID Protein

158254562

Enzyme 14 UniProtKB/Swiss-Prot ID

A8K3F0

Enzyme 14 UniProtKB/Swiss-Prot Entry Name

A8K3F0_HUMAN Link Image

Enzyme 14 PDB ID

Not Available

Enzyme 14 Cellular Location

Not Available

Enzyme 14 Gene Sequence

>1764 bp

ATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGC
CTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATC
CTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGA
GATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGG
AAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAG
ACAGATCTGCCTAGCTCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAG
GAGCAGGAGCAGATCTCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAAC
TATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCAC
ACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACAT
TTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTG
GGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGT
GCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAG
CAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTT
GCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCA
GACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTT
GTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAG
ATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTC
GAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCAT
GCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCAT
AAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATT
GCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACC
ACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGA
GAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTA
CTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTG
GGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTAT
GTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCC
TCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGG
ACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGT
CCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCC
CAGTATGTCACCACCTATGCCTGA

Enzyme 14 GenBank Gene ID

AK290565

Enzyme 14 GeneCard ID

A8K3F0

Enzyme 14 GenAtlas ID

Not Available

Enzyme 14 HGNC ID

Not Available

Enzyme 14 Chromosome Location

Not Available

Enzyme 14 Locus

Not Available

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

14844

Enzyme 15 Name

2-oxoglutarate dehydrogenase E1 component-like, mitochondrial precursor

Enzyme 15 Synonyms

Alpha-ketoglutarate dehydrogenase-like

Enzyme 15 Gene Name

OGDHL

Enzyme 15 Protein Sequence

>2-oxoglutarate dehydrogenase E1 component-like, mitochondrial precursor

MSQLRLLPSRLGVQAARLLAAHDVPVFGWRSRSSGPPATFPSSKGGGGSSYMEEMYFAWL
ENPQSVHKSWDSFFREASEEAFSGSAQPRPPSVVHESRSAVSSRTKTSKLVEDHLAVQSL
IRAYQIRGHHVAQLDPLGILDADLDSFVPSDLITTIDKLAFYDLQEADLDKEFQLPTTTF
IGGSENTLSLREIIRRLENTYCQHIGLEFMFINDVEQCQWIRQKFETPGVMQFSSEEKRT
LLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGIENVILGMPHRG
RLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGMYHERINRVTNRNITLSLVAN
PSHLEAVDPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYT
TNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEW
RNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKYADKLIAEGTVTLQ
EFEEEIAKYDRICEEAYGRSKDKKILHIKHWLDSPWPGFFNVDGEPKSMTCPATGIPEDM
LTHIGSVASSVPLEDFKIHTGLSRILRGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRL
SGQDVERGTFSHRHHVLHDQEVDRRTCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYA
MASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLLPHGMEGMGPEHSSA
RPERFLQMSNDDSDAYPAFTKDFEVSQLYDCNWIVVNCSTPANYFHVLRRQILLPFRKPL
IIFTPKSLLRHPEAKSSFDQMVSGTSFQRVIPEDGAAARAPEQVQRLIFCTGKVYYDLVK
ERSSQDLEEKVAITRLEQISPFPFDLIKQEAEKYPGAELAWCQEEHKNMGYYDYISPRFM
TILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNLQAFEGKTF

Enzyme 15 Number of Residues

1010

Enzyme 15 Molecular Weight

114482

Enzyme 15 Theoretical pI

6.63

Enzyme 15 GO Classification

Function
binding catalytic activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor oxoglutarate dehydrogenase (succinyl-transferring) activity thiamin pyrophosphate binding vitamin binding
Process
alcohol metabolism cellular metabolism glucose catabolism glucose metabolism glycolysis hexose metabolism metabolism monosaccharide metabolism physiological process
Component
—

Enzyme 15 General Function

Energy production and conversion

Enzyme 15 Specific Function

Not Available

Enzyme 15 Pathways

Not Available

Enzyme 15 Reactions

Not Available

Enzyme 15 Pfam Domain Function

E1_dh (PF00676 )
Transket_pyr (PF02779 )

Enzyme 15 Signals

1-15

Enzyme 15 Transmembrane Regions

None

Enzyme 15 Essentiality

Not Available

Enzyme 15 GenBank ID Protein

29421218

Enzyme 15 UniProtKB/Swiss-Prot ID

Q9ULD0

Enzyme 15 UniProtKB/Swiss-Prot Entry Name

OGDHL_HUMAN Link Image

Enzyme 15 PDB ID

Not Available

Enzyme 15 Cellular Location

Not Available

Enzyme 15 Gene Sequence

>3038 bp

CCCGAATGAGTCAGCTGAGGCTGCTGCCGTCCCGTCTTGGGGTACAGGCTGCGAGGCTCC
TGGCTGCACATGACGTCCCGGTGTTTGGCTGGCGCAGCAGGTCCTCCGGGCCACCGGCCA
CCTTCCCAAGCAGCAAAGGTGGAGGCGGCTCCAGTTACATGGAGGAGATGTACTTCGCCT
GGTTGGAAAACCCCCAGAGTGTCCACAAGTCCTGGGACAGCTTCTTCAGGGAAGCCAGCG
AGGAAGCCTTTTCTGGCTCTGCTCAGCCACGGCCCCCTTCTGTTGTCCATGAGAGCAGGT
CTGCAGTCTCAAGTCGGACCAAGACCAGCAAATTGGTGGAGGACCACCTGGCTGTGCAGT
CCCTGATCCGGGCCTACCAGATCCGGGGTCACCATGTGGCCCAGCTGGACCCCCTGGGCA
TTCTGGATGCAGACCTGGACTCCTTTGTGCCCTCAGACTTGATCACAACCATTGATAAAC
TGGCCTTCTATGACCTTCAGGAGGCTGACCTTGATAAGGAGTTCCAGCTGCCGACAACCA
CCTTCATTGGGGGCTCTGAAAACACCCTTTCTCTGCGGGAGATCATTCGGCGCCTGGAGA
ACACCTACTGCCAGCACATTGGCCTGGAGTTCATGTTCATCAACGATGTGGAGCAGTGCC
AGTGGATCCGGCAGAAGTTTGAGACCCCTGGTGTGATGCAGTTCTCCAGCGAGGAGAAGC
GGACCCTGCTGGCCCGGCTAGTGCGCTCCATGAGGTTTGAAGACTTCCTGGCCCGGAAAT
GGTCCTCAGAGAAGCGGTTTGGCCTGGAGGGCTGTGAAGTGATGATTCCTGCCCTCAAGA
CCATCATCGACAAATCCAGCGAGATGGGGATTGAGAATGTCATCTTGGGGATGCCACACA
GGGGAAGGCTGAACGTGCTGGCCAACGTGATCCGCAAGGACCTGGAGCAGATCTTCTGCC
AGTTTGACCCCAAGCTGGAGGCGGCGGACGAGGGCTCCGGGGATGTCAAGTACCACCTGG
GCATGTACCATGAGAGGATCAACCGCGTCACCAACCGGAACATCACTCTGTCGCTGGTTG
CCAACCCCTCCCACCTGGAGGCAGTGGACCCTGTGGTGCAGGGGAAGACAAAGGCAGAGC
AGTTCTACCGTGGAGATGCCCAGGGCAAGAAGGTCATGTCCATCCTGGTTCATGGGGACG
CCGCCTTTGCTGGCCAGGGCGTGGTATATGAGACCTTCCACCTGAGCGACCTGCCCTCCT
ACACGACCAATGGTACCGTGCACGTCGTCGTCAACAACCAGATTGGATTCACCACAGACC
CCCGAATGGCCCGCTCCTCACCATACCCGACCGACGTGGCCCGGGTGGTCAATGCGCCTA
TCTTCCATGTGAATGCCGATGACCCAGAGGCTGTGATATATGTGTGCAGTGTGGCAGCCG
AATGGAGAAACACTTTCAACAAAGATGTTGTCGTGGACCTGGTCTGTTACCGCCGGCGTG
GCCACAATGAGATGGACGAGCCCATGTTCACCCAGCCGCTCATGTACAAGCAGATCCACA
GACAGGTGCCTGTGCTGAAGAAGTACGCAGACAAGCTGATTGCCGAGGGCACAGTCACCC
TGCAGGAGTTTGAGGAAGAAATTGCCAAATACGACCGGATCTGTGAGGAGGCTTATGGCA
GGTCCAAGGATAAAAAGATTCTGCATATAAAGCACTGGTTGGACTCCCCCTGGCCTGGCT
TCTTCAACGTAGATGGGGAGCCCAAGAGCATGACATGCCCAGCCACGGGGATCCCTGAGG
ACATGCTCACCCACATCGGCAGTGTGGCCAGCTCTGTGCCCCTGGAGGACTTTAAGATCC
ACACTGGCCTCTCTCGCATTCTGCGGGGCCGTGCGGACATGACCAAGAACCGGACGGTGG
ACTGGGCGTTGGCAGAGTACATGGCCTTTGGCTCCCTGCTGAAGGAAGGCATCCACGTGC
GGCTCAGCGGGCAGGATGTGGAGAGGGGCACATTCAGTCACCGGCACCATGTTCTCCATG
ACCAGGAGGTTGACCGCAGGACGTGTGTGCCTATGAATCATCTCTGGCCTGACCAGGCCC
CGTACACCGTGTGCAACAGCTCCCTCTCGGAGTACGGAGTCCTGGGCTTTGAGCTGGGCT
ATGCCATGGCCAGCCCCAATGCCCTGGTCCTCTGGGAGGCCCAGTTTGGGGACTTCCACA
ACACGGCCCAGTGCATCATCGACCAGTTCATCAGCACCGGCCAGGCCAAGTGGGTGCGGC
ATAATGGCATTGTGCTGCTGCTGCCCCATGGCATGGAAGGCATGGGCCCAGAGCACTCGT
CAGCGAGGCCCGAAAGGTTCCTGCAGATGAGCAATGATGACTCGGATGCCTACCCTGCAT
TCACCAAGGACTTCGAGGTGAGCCAGCTCTATGACTGCAACTGGATCGTGGTCAACTGCT
CCACACCGGCCAACTACTTCCACGTGCTGCGCCGGCAGATCCTGCTGCCCTTCCGCAAGC
CGCTGATTATCTTCACACCTAAATCTCTGCTGAGGCACCCAGAGGCCAAGTCCAGCTTTG
ACCAAATGGTATCCGGGACCAGCTTCCAGCGGGTGATTCCTGAAGATGGGGCCGCAGCAC
GGGCCCCTGAGCAGGTGCAGCGGCTCATCTTCTGCACGGGAAAGGTGTACTATGACCTGG
TGAAGGAGCGGAGCAGCCAGGACCTGGAGGAGAAAGTGGCCATCACGCGCCTGGAGCAGA
TCTCTCCATTCCCCTTCGACCTGATCAAGCAGGAGGCAGAGAAGTACCCAGGTGCGGAGC
TGGCCTGGTGTCAGGAGGAGCACAAGAACATGGGCTACTATGACTACATCAGCCCACGCT
TCATGACCATCCTGAGGCGCGCACGGCCCATATGGTATGTTGGCCGGGACCCAGCGGCTG
CACCAGCCACAGGAAACAGGAACACTCACCTGGTGTCACTGAAGAAGTTTCTGGATACTG
CCTTCAATCTCCAGGCCTTTGAGGGCAAGACATTTTAG

Enzyme 15 GenBank Gene ID

AB033116

Enzyme 15 GeneCard ID

Q9ULD0

Enzyme 15 GenAtlas ID

OGDHL

Enzyme 15 HGNC ID

HGNC:25590 Link Image

Enzyme 15 Chromosome Location

Enzyme 15 Locus

10q11.23

Enzyme 15 SNPs

SNPJam Report Link Image

Enzyme 15 General References

Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed ]

Enzyme 15 Metabolite References

Not Available

Enzyme 16 [top]

Enzyme 16 ID

15876

Enzyme 16 Name

ACAA1 protein

Enzyme 16 Synonyms

Not Available

Enzyme 16 Gene Name

Not Available

Enzyme 16 Protein Sequence

>ACAA1 protein

MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTT
PDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVN
RQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARA
QSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAG
LTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQAITLLNE
LKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN

Enzyme 16 Number of Residues

331

Enzyme 16 Molecular Weight

34637

Enzyme 16 Theoretical pI

8.49

Enzyme 16 GO Classification

Not Available

Enzyme 16 General Function

Lipid transport and metabolism

Enzyme 16 Specific Function

Not Available

Enzyme 16 Pathways

Not Available

Enzyme 16 Reactions

Not Available

Enzyme 16 Pfam Domain Function

Thiolase_N (PF00108 )

Enzyme 16 Signals

None

Enzyme 16 Transmembrane Regions

None

Enzyme 16 Essentiality

Not Available

Enzyme 16 GenBank ID Protein

Not Available

Enzyme 16 UniProtKB/Swiss-Prot ID

Q96CA6

Enzyme 16 UniProtKB/Swiss-Prot Entry Name

Q96CA6_HUMAN Link Image

Enzyme 16 PDB ID

Not Available

Enzyme 16 Cellular Location

Not Available

Enzyme 16 Gene Sequence

Not Available

Enzyme 16 GenBank Gene ID

BC014474

Enzyme 16 GeneCard ID

Q96CA6

Enzyme 16 GenAtlas ID

ACAA1

Enzyme 16 HGNC ID

HGNC:82

Enzyme 16 Chromosome Location

Not Available

Enzyme 16 Locus

Not Available

Enzyme 16 SNPs

Not Available

Enzyme 16 General References

Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed ]

Enzyme 16 Metabolite References

Not Available

Enzyme 17 [top]

Enzyme 17 ID

16512

Enzyme 17 Name

Putative uncharacterized protein

Enzyme 17 Synonyms

Not Available

Enzyme 17 Gene Name

DLD

Enzyme 17 Protein Sequence

>Putative uncharacterized protein

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF

Enzyme 17 Number of Residues

509

Enzyme 17 Molecular Weight

54178

Enzyme 17 Theoretical pI

7.95

Enzyme 17 GO Classification

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

Enzyme 17 General Function

Energy production and conversion

Enzyme 17 Specific Function

Not Available

Enzyme 17 Pathways

Not Available

Enzyme 17 Reactions

Not Available

Enzyme 17 Pfam Domain Function

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

Enzyme 17 Signals

None

Enzyme 17 Transmembrane Regions

None

Enzyme 17 Essentiality

Not Available

Enzyme 17 GenBank ID Protein

Not Available

Enzyme 17 UniProtKB/Swiss-Prot ID

B2R5X0

Enzyme 17 UniProtKB/Swiss-Prot Entry Name

B2R5X0_HUMAN Link Image

Enzyme 17 PDB ID

Not Available

Enzyme 17 Cellular Location

Not Available

Enzyme 17 Gene Sequence

Not Available

Enzyme 17 GenBank Gene ID

AK312346

Enzyme 17 GeneCard ID

B2R5X0

Enzyme 17 GenAtlas ID

Not Available

Enzyme 17 HGNC ID

Not Available

Enzyme 17 Chromosome Location

Not Available

Enzyme 17 Locus

Not Available

Enzyme 17 SNPs

SNPJam Report Link Image

Enzyme 17 General References

Not Available

Enzyme 17 Metabolite References

Not Available

Enzyme 18 [top]

Enzyme 18 ID

16712

Enzyme 18 Name

cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)

Enzyme 18 Synonyms

Not Available

Enzyme 18 Gene Name

Not Available

Enzyme 18 Protein Sequence

>cDNA FLJ30111 fis, clone BNGH42000360, highly similar to 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16)

MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL
QSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTE
SMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECD
KYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK
KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAI
SGALKKAGLSLKDMDLVEANEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSR
ITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA

Enzyme 18 Number of Residues

397

Enzyme 18 Molecular Weight

41897

Enzyme 18 Theoretical pI

8.21

Enzyme 18 GO Classification

Not Available

Enzyme 18 General Function

Lipid transport and metabolism

Enzyme 18 Specific Function

Not Available

Enzyme 18 Pathways

Not Available

Enzyme 18 Reactions

acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA [RN:R00391] ALL_REAC R00391 > R00238 R00829 R00927 R01177 R03778 R03858 R03991 R04742 R04747 R05506 R07937 R07953
(other) R03719 R04546 R04811

Enzyme 18 Pfam Domain Function

Thiolase_C (PF02803 )
Thiolase_N (PF00108 )

Enzyme 18 Signals

None

Enzyme 18 Transmembrane Regions

None

Enzyme 18 Essentiality

Not Available

Enzyme 18 GenBank ID Protein

Not Available

Enzyme 18 UniProtKB/Swiss-Prot ID

B3KNP8

Enzyme 18 UniProtKB/Swiss-Prot Entry Name

B3KNP8_HUMAN Link Image

Enzyme 18 PDB ID

Not Available

Enzyme 18 Cellular Location

Not Available

Enzyme 18 Gene Sequence

Not Available

Enzyme 18 GenBank Gene ID

AK054673

Enzyme 18 GeneCard ID

B3KNP8

Enzyme 18 GenAtlas ID

Not Available

Enzyme 18 HGNC ID

Not Available

Enzyme 18 Chromosome Location

Not Available

Enzyme 18 Locus

Not Available

Enzyme 18 SNPs

Not Available

Enzyme 18 General References

Not Available

Enzyme 18 Metabolite References

Not Available

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Human Metabolome Database Version 2.5

Showing metabocard for Succinyl-CoA (HMDB01022)