We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for 2-(a-Hydroxyethyl)thiamine diphosphate (HMDB03904)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 08:01:57
Update Date 2009-05-05 20:59:54
Accession Number HMDB03904
Secondary Accession Numbers Not Available
Common Name 2-(a-Hydroxyethyl)thiamine diphosphate
Description 2-Hydroxyethyl-ThPP is involved in Glycolysis, Gluconeogenesis, Alanine and aspartate matabolism, Valine, Leucine and isoleucine biosynthesis, Pyruvate metabolism, and Butanoate metabolism [Kegg: c05125]
Synonyms
  1. 2-Hydroxyethyl-ThPP
  2. 2-(alpha-Hydroxyethyl)thiamine diphosphic acid
  3. Thiazolium
  4. 3-[(4-amino-2-methyl-5-pyrimidinyl)methyl]-2-(1-hydroxyethyl)-4-methyl-5-(4,6,6-trihydroxy-3,5-dioxa-4,6-diphosphahex-1-yl)- P,P'-dioxide
  5. 3-[(4-amino-2-methyl-5-pyrimidinyl)methyl]-2-(1-hydroxyethyl)-5-(2-hydroxyethyl)-4-methyl- 5-(trihydrogen pyrophosphate) (8CI)
  6. 2-(alpha-Hydroxyethyl)thiamine diphosphate
Chemical IUPAC Name 2-[3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-hydroxyethyl)-4-methyl-1,3-thiazol-3-ium-5-yl]ethyl phosphono hydrogen phosphate
Chemical Formula C14H23N4O8P2S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellanous
Class
  • Miscellaneous
Sub Class
  • Miscellaneous heterocyclic compounds
Family
  • Mammalian Metabolite
Species
  • cation
  • secondary alcohol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 469.367
Monoisotopic Molecular Weight 469.071198
Isomeric SMILES CC(O)C1=[N+](CC2=CN=C(C)N=C2N)C(C)=C(CCOP(O)(=O)OP(O)(O)=O)S1
Canonical SMILES CC(O)C1=[N+](CC2=CN=C(C)N=C2N)C(C)=C(CCOP(O)(=O)OP(O)(O)=O)S1
KEGG Compound ID C05125 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB03904 Link Image
Metagene Link HMDB03904 Link Image
METLIN ID Not Available
PubChem Compound 440568 Link Image
PubChem Substance 11110188 Link Image
ChEBI ID 978 Link Image
CAS Registry Number 10055-47-7
InChI Identifier InChI=1/C14H22N4O8P2S/c1-8-12(4-5-25-28(23,24)26-27(20,21)22)29-14(9(2)19)18(8)7-11-6-16-10(3)17-13(11)15/h6,9,19H,4-5,7H2,1-3H3,(H4-,15,16,17,20,21,22,23,24)/p+1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.09 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity 0.401 Source: PhysProp
Predicted LogP/Hydrophobicity -0.67 [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 Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyruvate Metabolism SMP00060 Link Image map00620 Link Image
General References Not Available
Metabolic Enzymes
  1. Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
  2. Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
  3. 2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
  4. ILVBL protein
  5. cDNA, FLJ93492, highly similar to Homo sapiens pyruvate dehydrogenase (lipoamide) beta (PDHB), mRNA (Pyruvate dehydrogenase (Lipoamide) beta, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5275
Enzyme 1 Name Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
Enzyme 1 Synonyms
  1. PDHE1-A type I
Enzyme 1 Gene Name PDHA1
Enzyme 1 Protein Sequence >Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor 
MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS
Enzyme 1 Number of Residues 390
Enzyme 1 Molecular Weight 43296
Enzyme 1 Theoretical pI 8.14
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-16
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 387009 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P08559 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ODPA_HUMAN Link Image
Enzyme 1 PDB ID 1NI4 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1173 bp 
ATGAGGAAGATGCTCGCCGCCGTCTCCCGCGTGCTGTCTGGCGCTTCTCAGAAGCCGGCA
AGCAGAGTGCTGGTAGCATCCCGTAATTTTGCAAATGATGCTACATTTGAAATTAAGAAA
TGTGACCTTCACCGGCTGGAAGAAGGCCCTCCTGTCACAACAGTGCTCACCAGGGAGGAT
GGGCTCAAATACTACAGGATGATGCAGACTGTACGCCGAATGGAGTTGAAAGCAGATCAG
CTGTATAAACAGAAAATTATTCGTGGTTTCTGTCACTTGTGTGATGGTCAGGAAGCTTGC
TGTGTGGGCCTGGAGGCCGGCATCAACCCCACAGACCATCTCATCACAGCCTACCGGGCT
CACGGCTTTACTTTCACCCGGGGCCTTTCCGTCCGAGAAATTCTCGCAGAGCTTACAGGA
CGAAAAGGAGGTTGTGCTAAAGGGAAAGGAGGATCGATGCACATGTATGCCAAGAACTTC
TACGGGGGCAATGGCATCGTGGGAGCGCAGGTGCCCCTGGGCGCTGGGATTGCTCTAGCC
TGTAAGTATAATGGAAAAGATGAGGTCTGCCTGACTTTATATGGCGATGGTGCTGCTAAC
CAGGGCCAGATATTCGAAGCTTACAACATGGCAGCTTTGTGGAAATTACCTTGTATTTTC
ATCTGTGAGAATAATCGCTATGGAATGGGAACGTCTGTTGAGAGAGCGGCAGCCAGCACT
GATTACTACAAGAGAGGCGATTTCATTCCTGGGCTGAGAGTGGATGGAATGGATATCCTG
TGCGTCCGAGAGGCAACAAGGTTTGCTGCTGCCTATTGTAGATCTGGGAAGGGGCCCATC
CTGATGGAGCTGCAGACTTACCGTTACCACGGACACAGTATGAGTGACCCTGGAGTCAGT
TACCGTACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGTGACCCTATTATGCTTCTC
AAGGACAGGATGGTGAACAGCAATCTTGCCAGTGTGGAAGAACTAAAGGAAATTGATGTG
GAAGTGAGGAAGGAGATTGAGGATGCTGCCCAGTTTGCCACGGCCGATCCTGAGCCACCT
TTGGAAGAGCTGGGCTACCACATCTACTCCAGCGACCCACCTTTTGAAGTTCGTGGTGCC
AATCAGTGGATCAAGTTTAAGTCAGTCAGTTAA
Enzyme 1 GenBank Gene ID M27257 Link Image
Enzyme 1 GeneCard ID PDHA1 Link Image
Enzyme 1 GenAtlas ID PDHA1 Link Image
Enzyme 1 HGNC ID HGNC:8806 Link Image
Enzyme 1 Chromosome Location X
Enzyme 1 Locus Xp22.2-p22.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Koike K, Urata Y, Matsuo S, Koike M: Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit. Gene. 1990 Sep 14;93(2):307-11. [PubMed Link Image]
  2. Ho L, Wexler ID, Liu TC, Thekkumkara TJ, Patel MS: Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5330-4. [PubMed Link Image]
  3. Dahl HH, Hunt SM, Hutchison WM, Brown GK: The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. 1987 May 25;262(15):7398-403. [PubMed Link Image]
  4. Maragos C, Hutchison WM, Hayasaka K, Brown GK, Dahl HH: Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex. J Biol Chem. 1989 Jul 25;264(21):12294-8. [PubMed Link Image]
  5. De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH: Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. 1988 Feb 5;263(4):1991-5. [PubMed Link Image]
  6. Koike K, Ohta S, Urata Y, Kagawa Y, Koike M: Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):41-5. [PubMed Link Image]
  7. Harris EE, Hey J: X chromosome evidence for ancient human histories. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3320-4. [PubMed Link Image]
  8. Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS: Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. [PubMed Link Image]
  9. Dahl HH, Brown GK, Brown RM, Hansen LL, Kerr DS, Wexler ID, Patel MS, De Meirleir L, Lissens W, Chun K, et al.: Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene. Hum Mutat. 1992;1(2):97-102. [PubMed Link Image]
  10. Hansen LL, Brown GK, Kirby DM, Dahl HH: Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis. 1991;14(2):140-51. [PubMed Link Image]
  11. De Meirleir L, Lissens W, Vamos E, Liebaers I: Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit. Hum Genet. 1992 Mar;88(6):649-52. [PubMed Link Image]
  12. Dahl HH, Hansen LL, Brown RM, Danks DM, Rogers JG, Brown GK: X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation. J Inherit Metab Dis. 1992;15(6):835-47. [PubMed Link Image]
  13. Matthews PM, Marchington DR, Squier M, Land J, Brown RM, Brown GK: Molecular genetic characterization of an X-linked form of Leigh's syndrome. Ann Neurol. 1993 Jun;33(6):652-5. [PubMed Link Image]
  14. Chun K, MacKay N, Petrova-Benedict R, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex. Hum Mol Genet. 1993 Apr;2(4):449-54. [PubMed Link Image]
  15. Matthews PM, Brown RM, Otero LJ, Marchington DR, LeGris M, Howes R, Meadows LS, Shevell M, Scriver CR, Brown GK: Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients. Brain. 1994 Jun;117 ( Pt 3):435-43. [PubMed Link Image]
  16. Hansen LL, Horn N, Dahl HH, Kruse TA: Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit. Hum Mol Genet. 1994 Jun;3(6):1021-2. [PubMed Link Image]
  17. Dahl HH, Brown GK: Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit. Hum Mutat. 1994;3(2):152-5. [PubMed Link Image]
  18. Awata H, Endo F, Tanoue A, Kitano A, Matsuda I: Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia. J Inherit Metab Dis. 1994;17(2):189-95. [PubMed Link Image]
  19. Chun K, MacKay N, Petrova-Benedict R, Federico A, Fois A, Cole DE, Robertson E, Robinson BH: Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex. Am J Hum Genet. 1995 Mar;56(3):558-69. [PubMed Link Image]
  20. Takakubo F, Cartwright P, Hoogenraad N, Thorburn DR, Collins F, Lithgow T, Dahl HH: An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein. Am J Hum Genet. 1995 Oct;57(4):772-80. [PubMed Link Image]
  21. Hemalatha SG, Kerr DS, Wexler ID, Lusk MM, Kaung M, Du Y, Kolli M, Schelper RL, Patel MS: Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit. Hum Mol Genet. 1995 Feb;4(2):315-8. [PubMed Link Image]
  22. Lissens W, De Meirleir L, Seneca S, Benelli C, Marsac C, Poll-The BT, Briones P, Ruitenbeek W, van Diggelen O, Chaigne D, Ramaekers V, Liebaers I: Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency. Hum Mutat. 1996;7(1):46-51. [PubMed Link Image]
  23. Tripatara A, Kerr DS, Lusk MM, Kolli M, Tan J, Patel MS: Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS). Hum Mutat. 1996;8(2):180-2. [PubMed Link Image]
  24. Otero LJ, Brown RM, Brown GK: Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity. Hum Mutat. 1998;12(2):114-21. [PubMed Link Image]
  25. Ito M, Huq AH, Naito E, Saijo T, Takeda E, Kuroda Y: Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein. J Inherit Metab Dis. 1992;15(6):848-56. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5279
Enzyme 2 Name Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
Enzyme 2 Synonyms
  1. PDHE1-A type II
Enzyme 2 Gene Name PDHA2
Enzyme 2 Protein Sequence >Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor 
MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS
Enzyme 2 Number of Residues 388
Enzyme 2 Molecular Weight 42934
Enzyme 2 Theoretical pI 8.56
Enzyme 2 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components:pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-15
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 190790 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P29803 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ODPAT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1167 bp 
ATGCTGGCCGCCTTCATCTCCCGCGTGTTGAGGCGAGTTGCCCAGAAATCAGCTCGCAGA
GTGCTGGTGGCATCCCGTAACTCCTCAAATGACGCTACATTTGAAATTAAGAAATGTGAT
CTTTATCTGTTGGAAGAGGGTCCCCCTGTCACTACAGTGCTCACTAGGGCGGAGGGGCTT
AAATACTACAGGATGATGCTGACTGTTCGCCGCATGGAATTGAAGGCAGATCAGCTGTAC
AAACAGAAATTCATTCGCGGTTTCTGTCACCTGTGCGATGGTCAGGAAGCTTGTTGCGTG
GGCCTTGAGGCCGGCATAAACCCCTCGGATCACGTCATTACATCCTATAGGGCTCATGGT
GTGTGCTATACTCGGGGACTTTCTGTCCGATCCATTCTCGCAGAGCTGACGGGAAGAAGA
GGAGGTTGTGCTAAAGGAAAAGGAGGATCGATGCATATGTATACCAAGAACTTCTATGGG
GGCAATGGCATCGTCGGTGCACAGGGCCCCCTGGGCGCTGGCATTGCTCTGGCCTGTAAA
TATAAAGGAAACGATGAGATCTGTTTGACTTTATATGGGGATGGCGCTGCGAATCAGGGG
CAGATAGCCGAAGCTTTCAATATGGCAGCTTTATGGAAATTACCTTGTGTTTTCATCTGT
GAGAATAACCTATATGGAATGGGAACATCTACTGAGAGAGCAGCAGCCAGCCCTGATTAC
TACAAGAGGGGCAATTTTATCCCTGGGCTAAAGGTCGATGGAATGGATGTTCTGTGTGTT
CGTGAGGCAACAAAATTTGCAGCTAACTACTGTAGATCTGGAAAGGGGCCCATACTGATG
GAGCTGCAAACCTACCGTTATCATGGACACAGTATGAGTGATCCTGGAGTCAGTTATCGT
ACACGAGAAGAAATTCAGGAAGTAAGAAGTAAGAGGGATCCTATAATAATTCTCCAAGAT
AGAATGGTAAACAGCAAGCTCGCCACTGTGGAAGAATTAAAGGAAATTGGGGCTGAGGTG
AGGAAAGAAATTGATGATGCTGCCCAGTTTGCTACCACTGATCCTGAGCCACATTTGGAA
GAATTAGGCCATCACATCTACAGCAGTGATTCATCTTTTGAAGTTCGTGGTGCAAATCCA
TGGATCAAGTTTAAGTCCGTCAGTTAA
Enzyme 2 GenBank Gene ID M86808 Link Image
Enzyme 2 GeneCard ID PDHA2 Link Image
Enzyme 2 GenAtlas ID PDHA2 Link Image
Enzyme 2 HGNC ID HGNC:8807 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q22-q23
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Dahl HH, Brown RM, Hutchison WM, Maragos C, Brown GK: A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4. Genomics. 1990 Oct;8(2):225-32. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 10320
Enzyme 3 Name 2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
Enzyme 3 Synonyms
  1. Alpha-ketoglutarate dehydrogenase
Enzyme 3 Gene Name OGDH
Enzyme 3 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 3 Number of Residues 1002
Enzyme 3 Molecular Weight 113477
Enzyme 3 Theoretical pI Not Available
Enzyme 3 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 3 General Function Energy production and conversion
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • 2-Oxoadipate + Coenzyme A + Nicotinamide adenine dinucleotide --> CO2 + Glutaryl-CoA + Nicotinamide adenine dinucleotide - reduced
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 531241 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q02218 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ODO1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID D10523 Link Image
Enzyme 3 GeneCard ID OGDH Link Image
Enzyme 3 GenAtlas ID OGDH Link Image
Enzyme 3 HGNC ID HGNC:8124 Link Image
Enzyme 3 Chromosome Location 7
Enzyme 3 Locus 7p14-p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13009
Enzyme 4 Name ILVBL protein
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name ILVBL
Enzyme 4 Protein Sequence >ILVBL protein 
VVTKKLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTR
HEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQN
RGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPY
FMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQLLSN
N
Enzyme 4 Number of Residues 241
Enzyme 4 Molecular Weight 25613
Enzyme 4 Theoretical pI 10.17
Enzyme 4 GO Classification
Function
  • binding
  • thiamin pyrophosphate binding
  • vitamin binding
Process
—
Component
—
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 119850829 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A1L0T0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A1L0T0_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID BC126913 Link Image
Enzyme 4 GeneCard ID A1L0T0 Link Image
Enzyme 4 GenAtlas ID ILVBL Link Image
Enzyme 4 HGNC ID HGNC:6041 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16533
Enzyme 5 Name cDNA, FLJ93492, highly similar to Homo sapiens pyruvate dehydrogenase (lipoamide) beta (PDHB), mRNA (Pyruvate dehydrogenase (Lipoamide) beta, isoform CRA_a)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PDHB
Enzyme 5 Protein Sequence >cDNA, FLJ93492, highly similar to Homo sapiens pyruvate dehydrogenase (lipoamide) beta (PDHB), mRNA (Pyruvate dehydrogenase (Lipoamide) beta, isoform CRA_a) 
MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEV
AQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAI
DQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS
EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVV
SHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFG
VGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
Enzyme 5 Number of Residues 359
Enzyme 5 Molecular Weight 39234
Enzyme 5 Theoretical pI 6.63
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B2R7L0 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B2R7L0_HUMAN Link Image
Enzyme 5 PDB ID 1NI4 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK313022 Link Image
Enzyme 5 GeneCard ID B2R7L0 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available