1. 2-Ketobutanoate
2. 2-Ketobutanoic acid
3. 2-Oxo-Butanoate
4. 2-Oxo-Butanoic acid
5. 2-Oxo-n-butyrate
6. 2-Oxo-n-butyric acid
7. 2-Oxobutanoate
8. 2-Oxobutanoic acid
9. 2-Oxobutyrate
10. 2-Oxobutyric acid
11. 2-oxo-Butyrate
12. 2-oxo-Butyric acid
13. 3-Methylpyruvate
14. 3-Methylpyruvic acid
15. alpha-Keto-n-butyrate
16. alpha-Keto-n-butyric acid
17. alpha-Ketobutyrate
18. alpha-Ketobutric acid
19. alpha-Ketobutyric acid
20. alpha-Oxo-n-butyrate
21. alpha-Oxo-n-butyric acid
22. alpha-Oxobutyrate
23. a-Ketobutyrate
24. a-Ketobutyric acid
25. a-Oxo-n-butyrate
26. a-Oxo-n-butyric acid
27. a-Oxobutyrate
28. a-Oxobutyric acid
29. a-keto-n-Butyrate
30. a-keto-n-Butyric acid
31. methyl-Pyruvate
32. methyl-Pyruvic acid
33. propionyl-formate
34. propionyl-formic acid
35. alpha-Oxobutyric acid

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• Cytoplasm

• Blood
• Cerebrospinal Fluid
• Urine

1. Sprague CL, Elfarra AA: Detection of carboxylic acids and inhibition of hippuric acid formation in rats treated with 3-butene-1,2-diol, a major metabolite of 1,3-butadiene. Drug Metab Dispos. 2003 Aug;31(8):986-92. [PubMed ]
2. Yaegaki K, Sanada K: Biochemical and clinical factors influencing oral malodor in periodontal patients. J Periodontol. 1992 Sep;63(9):783-9. [PubMed ]
3. Yaegaki K, Sanada K: Effects of a two-phase oil-water mouthwash on halitosis. Clin Prev Dent. 1992 Jan-Feb;14(1):5-9. [PubMed ]
4. Yang W, Roth KS: Defect in alpha-ketobutyrate metabolism: a new inborn error. Clin Chim Acta. 1985 Jan 30;145(2):173-82. [PubMed ]
5. Wikipedia

1. Pyruvate dehydrogenase E1 component subunit beta, mitochondrial precursor
2. Pyruvate dehydrogenase E1 component alpha subunit, somatic form, mitochondrial precursor
3. Pyruvate dehydrogenase E1 component alpha subunit, testis-specific form, mitochondrial precursor
4. 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial precursor
5. 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial precursor
6. 2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor
7. Cystathionine gamma-lyase
8. L-lactate dehydrogenase B chain
9. L-lactate dehydrogenase C chain
10. L-lactate dehydrogenase A-like 6B
11. L-lactate dehydrogenase A-like 6A
12. Probable urocanate hydratase
13. [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial precursor
14. Trimethyllysine dioxygenase, mitochondrial precursor
15. Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2
16. Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
17. 2-oxoglutarate dehydrogenase E1 component-like, mitochondrial precursor
18. 2-oxoglutarate receptor 1
19. cDNA FLJ54086, moderately similar to L-lactate dehydrogenase A chain (EC 1.1.1.27)

1. PDHE1-B

MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEV
AQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAI
DQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS
EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVV
SHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFG
VGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI

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

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

• Transket_pyr (PF02779 )
• Transketolase_C (PF02780 )

• None

• None

ATGGCGGCGGTGTCTGGCTTGGTGCGGAGACCCCTTCGGGAGGTCTCCGGGCTGCTGAAG
AGGCGCTTTCACTGGACCGCGCCGGCTGCGCTGCAGGTGACAGTTCGTGATGCTATAAAT
CAGGGTATGGATGAGGAGCTGGAAAGAGATGAGAAGGTATTTCTGCTTGGAGAAGAAGTT
GCCCAGTATGATGGGGCATACAAGGTTAGTCGAGGGCTGTGGAAGAAATATGGAGACAAG
AGGATTATTGACACTCCCATATCAGAGATGGGCTTTGCTGGAATTGCTGTAGGTGCAGCT
ATGGCTGGGTTGCGGCCCATTTGTGAATTTATGACCTTCAATTTCTCCATGCAAGCCATT
GACCAGGTTATAAACTCAGCTGCCAAGACCTACTACATGTCTGGTGGCCTTCAGCCTGTG
CCTATAGTCTTCAGGGGACCCAATGGTGCCTCAGCAGGTGTAGCTGCCCAGCACTCACAG
TGCTTTGCTGCCTGGTATGGGCACTGCCCAGGCTTAAAGGTGGTCAGTCCCTGGAATTCA
GAGGATGCTAAAGGACTTATTAAATCAGCCATTCGGGATAACAATCCAGTGGTGGTGCTA
GAGAATGAATTGATGTATGGGGTTCCTTTTGAATTTCCTCCGGAAGCTCAGTCAAAAGAT
TTTCTGATTCCTATTGGAAAAGCCAAAATAGAAAGGCAAGGAACACATATAACTGTGGTT
TCCCATTCAAGACCTGTGGGCCACTGCTTAGAAGCTGCAGCAGTGCTATCTAAAGAAGGA
GTTGAATGTGAGGTGATAAATATGCGTACCATTAGACCAATGGACATGGAAACCATAGAA
GCCAGTGTCATGAAGACAAATCATCTTGTAACTGTGGAAGGAGGCTGGCCACAGTTTGGA
GTAGGAGCTGAAATCTGTGCCAGGATCATGGAAGGTCCTGCGTTCAATTTCCTGGATGCT
CCTGCTGTTCGTGTCACTGGTGCTGATGTCCCTATGCCTTATGCAAAGATTCTAGAGGAC
AACTCTATACCTCAGGTCAAAGACATCATATTTGCAATAAAGAAAACATTAAATATTTAG

1. Ho L, Patel MS: Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex. Gene. 1990 Feb 14;86(2):297-302. [PubMed ]
2. Chun K, Mackay N, Willard HF, Robinson BH: Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex. Eur J Biochem. 1990 Dec 12;194(2):587-92. [PubMed ]
3. Huh TL, Casazza JP, Huh JW, Chi YT, Song BJ: Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast. J Biol Chem. 1990 Aug 5;265(22):13320-6. [PubMed ]
4. Koike K, Urata Y, Koike M: Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene. Proc Natl Acad Sci U S A. 1990 Aug;87(15):5594-7. [PubMed ]
5. 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 ]
6. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]
7. Ho L, Javed AA, Pepin RA, Thekkumkara TJ, Raefsky C, Mole JE, Caliendo AM, Kwon MS, Kerr DS, Patel MS: Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex. Biochem Biophys Res Commun. 1988 Feb 15;150(3):904-8. [PubMed ]
8. Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65. [PubMed ]
9. Muno D, Kominami E, Ishii H, Usui K, Saifuku K, Sakakibara Y, Namihisa T: Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis. Hepatology. 1990 Jan;11(1):16-23. [PubMed ]
10. 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 ]

1. Paxton R, Scislowski PW, Davis EJ, Harris RA: Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism. Biochem J. 1986 Mar 1;234(2):295-303. [PubMed ]

1. PDHE1-A type I

MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS

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

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

• E1_dh (PF00676 )

• 1-16

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

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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]
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 ]

1. Paxton R, Scislowski PW, Davis EJ, Harris RA: Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism. Biochem J. 1986 Mar 1;234(2):295-303. [PubMed ]

1. PDHE1-A type II

MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGL
KYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHG
VCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACK
YKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDY
YKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYR
TREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLE
ELGHHIYSSDSSFEVRGANPWIKFKSVS

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

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

• E1_dh (PF00676 )

• 1-15

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

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 ]

1. Paxton R, Scislowski PW, Davis EJ, Harris RA: Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism. Biochem J. 1986 Mar 1;234(2):295-303. [PubMed ]

1. Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
2. BCKDH E1-beta

MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDP
EPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVF
NTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSL
TIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEP
KILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCE
VIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRV
CGYDTPFPHIFEPFYIPDKWKCYDALRKMINY

• Valine, Leucine and Isoleucine Degradation (map00280 )

• 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2

• Transket_pyr (PF02779 )
• Transketolase_C (PF02780 )

• 1-19

ATGGCGGTTGTAGCGGCGGCTGCCGGCTGGCTACTCAGGCTCAGGGCGGCAGGGGCTGAG
GGGCACTGGCGTCGGCTTCCTGGCGCGGGGCTGGCGCGGGGCTTTTTGCACCCCGCCGCG
ACTGTCGAGGATGCGGCCCAGAGGCGGCAGGTGGCTCATTTTACTTTCCAGCCAGATCCG
GAGCCCCGGGAGTACGGGCAAACTCAGAAAATGAATCTTTTCCAGTCTGTAACAAGTGCC
TTGGATAACTCATTGGCCAAAGATCCTACTGCAGTAATATTTGGTGAAGATGTTGCCTTT
GGTGGAGTCTTTAGATGCACTGTTGGCTTGCGAGACAAATATGGAAAAGATAGAGTTTTT
AATACCCCATTGTGTGAACAAGGAATTGTTGGATTTGGAATCGGAATTGCGGTCACTGGA
GCTACTGCCATTGCGGAAATTCAGTTTGCAGATTATATTTTCCCTGCATTTGATCAGATT
GTTAATGAAGCTGCCAAGTATCGCTATCGCTCTGGGGATCTTTTTAACTGTGGAAGCCTC
ACTATCCGGTCCCCTTGGGGCTGTGTTGGTCATGGGGCTCTCTATCATTCTCAGAGTCCT
GAAGCATTTTTTGCCCATTGCCCAGGAATCAAGGTGGTTATACCCAGAAGCCCTTTCCAG
GCCAAAGGACTTCTTTTGTCATGCATAGAGGATAAAAATCCTTGTATATTTTTTGAACCT
AAAATACTTTACAGGGCAGCAGCGGAAGAAGTCCCTATAGAACCATACAACATCCCACTG
TCCCAGGCCGAAGTCATACAGGAAGGGAGTGATGTTACTCTAGTTGCCTGGGGCACTCAG
GTTCATGTGATCCGAGAGGTAGCTTCCATGGCAAAAGAAAAGCTTGGAGTGTCTTGTGAA
GTCATTGATCTGAGGACTATAATACCTTGGGATGTGGACACAATTTGTAAGTCTGTGATC
AAAACAGGGCGACTGCTAATCAGTCACGAGGCTCCCTTGACAGGCGGCTTTGCATCGGAA
ATCAGCTCTACAGTTCAGGAGGAATGTTTCTTGAACCTAGAGGCTCCTATATCAAGAGTA
TGTGGTTATGACACACCATTTCCTCACATTTTTGAACCATTCTACATCCCAGACAAATGG
AAGTGTTATGATGCCCTTCGAAAAATGATCAACTATTGA

1. Nobukuni Y, Mitsubuchi H, Endo F, Akaboshi I, Asaka J, Matsuda I: Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease. J Clin Invest. 1990 Jul;86(1):242-7. [PubMed ]
2. Chuang JL, Cox RP, Chuang DT: Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am J Hum Genet. 1996 Jun;58(6):1373-7. [PubMed ]
3. Chuang JL, Cox RP, Chuang DT: Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1990 Mar 26;262(2):305-9. [PubMed ]
4. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed ]
5. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed ]

1. Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
2. BCKDH E1-alpha
3. BCKDE1A

MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAE
FIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILY
ESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYG
NISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGA
ASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDG
NDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRSVDEVNYWDKQDHP
ISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQL
RKQQESLARHLQTYGEHYPLDHFDK

• Valine, Leucine and Isoleucine Degradation (map00280 )

• 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2

• E1_dh (PF00676 )

• 1-32

ATGGCGGTAGCGATCGCTGCAGCGAGGGTCTGGCGGCTAAACCGTGGTTTGAGCCAGGCT
GCCCTCCTGCTGCTGCGGCAGCCTGGGGCTCGGGGACTGGCTAGATCTCACCCCCCCAGG
CAGCAGCAGCAGTTTTCATCTCTGGATGACAAGCCCCAGTTCCCAGGGGCCTCGGCGGAG
TTTATAGATAAGTTGGAATTCATCCAGCCCAACGTCATCTCTGGAATCCCCATCTACCGC
GTCATGGACCGGCAAGGCCAGATCATCAACCCCAGCGAGGACCCCCACCTGCCGAAGGAG
AAGGTGCTGAAGCTCTACAAGAGCATGACACTGCTTAACACCATGGACCGCATCCTCTAT
GAGTCTCAGCGGCAGGGCCGGATCTCCTTCTACATGACCAACTATGGTGAGGAGGGCACG
CACGTGGGGAGTGCCGCCGCCCTGGACAACACGGACCTGGTGTTTGGCCAGTACCGGGAG
GCAGGTGTGCTGATGTATCGGGACTACCCCCTGGAACTATTCATGGCCCAGTGCTATGGC
AACATCAGTGACTTGGGCAAGGGGCGCCAGATGCCTGTCCACTACGGCTGCAAGGAACGC
CACTTCGTCACTATCTCCTCTCCACTGGCCACGCAGATCCCTCAGGCGGTGGGGGCGGCG
TACGCAGCCAAGCGGGCCAATGCCAACAGGGTCGTCATCTGTTACTTCGGCGAGGGGGCA
GCCAGTGAGGGGGACGCCCATGCCGGCTTCAACTTCGCTGCCACACTTGAGTGCCCCATC
ATCTTCTTCTGCCGGAACAATGGCTACGCCATCTCCACGCCCACCTCTGAGCAGTATCGC
GGCGATGGCATTGCAGCACGAGGCCCCGGGTATGGCATCATGTCAATCCGCGTGGATGGT
AATGATGTGTTTGCCGTATACAACGCCACAAAGGAGGCCCGACGGCGGGCTGTGGCAGAG
AACCAGCCCTTTCTCATCGAGGCCATGACCTACAGGATCGGGCACCACAGCACCAGTGAC
GACAGTTCAGCGTACCGCTCGGTGGATGAGGTCAATTACTGGGATAAACAGGACCACCCC
ATCTCCCGGCTGCGGCACTATCTGCTGAGCCAAGGCTGGTGGGATGAGGAGCAGGAGAAG
GCCTGGAGGAAGCAGTCCCGCAGGAAGGTGATGGAGGCCTTTGAGCAGGCCGAGCGGAAG
CCCAAACCCAACCCCAACCTGCTCTTCTCAGACGTGTATCAGGAGATGCCCGCCCAGCTC
CGCAAGCAGCAGGAGTCTCTGGCCCGCCACCTGCAGACCTACGGGGAGCACTACCCACTG
GATCACTTCGATAAGTGA

1. McKean MC, Winkeler KA, Danner DJ: Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex. Biochim Biophys Acta. 1992 Nov 15;1171(1):109-12. [PubMed ]
2. Fisher CW, Chuang JL, Griffin TA, Lau KS, Cox RP, Chuang DT: Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex. J Biol Chem. 1989 Feb 25;264(6):3448-53. [PubMed ]
3. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex. FEBS Lett. 1991 Jun 17;284(1):34-8. [PubMed ]
4. Dariush N, Fisher CW, Cox RP, Chuang DT: Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex (1991) FEBS Letters 284, 34-38. FEBS Lett. 1991 Oct 21;291(2):376-7. [PubMed ]
5. Zhang B, Crabb DW, Harris RA: Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase. Gene. 1988 Sep 15;69(1):159-64. [PubMed ]
6. Wynn RM, Kochi H, Cox RP, Chuang DT: Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence. Biochim Biophys Acta. 1994 Sep 28;1201(1):125-8. [PubMed ]
7. AEvarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WG: Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure. 2000 Mar 15;8(3):277-91. [PubMed ]
8. Chuang JL, Fisher CR, Cox RP, Chuang DT: Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex. Am J Hum Genet. 1994 Aug;55(2):297-304. [PubMed ]
9. Zhang B, Edenberg HJ, Crabb DW, Harris RA: Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease. J Clin Invest. 1989 Apr;83(4):1425-9. [PubMed ]
10. Matsuda I, Nobukuni Y, Mitsubuchi H, Indo Y, Endo F, Asaka J, Harada A: A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients. Biochem Biophys Res Commun. 1990 Oct 30;172(2):646-51. [PubMed ]
11. Fisher CR, Fisher CW, Chuang DT, Cox RP: Occurrence of a Tyr393----Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population. Am J Hum Genet. 1991 Aug;49(2):429-34. [PubMed ]
12. Fisher CR, Chuang JL, Cox RP, Fisher CW, Star RA, Chuang DT: Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex. J Clin Invest. 1991 Sep;88(3):1034-7. [PubMed ]
13. Nobukuni Y, Mitsubuchi H, Hayashida Y, Ohta K, Indo Y, Ichiba Y, Endo F, Matsuda I: Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex. Biochim Biophys Acta. 1993 Nov 25;1225(1):64-70. [PubMed ]
14. Chuang JL, Davie JR, Chinsky JM, Wynn RM, Cox RP, Chuang DT: Molecular and biochemical basis of intermediate maple syrup urine disease. Occurrence of homozygous G245R and F364C mutations at the E1 alpha locus of Hispanic-Mexican patients. J Clin Invest. 1995 Mar;95(3):954-63. [PubMed ]

1. Alpha-ketoglutarate dehydrogenase

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

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

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

• E1_dh (PF00676 )
• Transket_pyr (PF02779 )

• None

• None

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

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 ]
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 ]

1. Gamma-cystathionase

MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS

• Cysteine Metabolism (map00272 )
• Glycine, Serine and Threonine Metabolism (map00260 )
• Methionine Metabolism (map00271 )
• Nitrogen Metabolism (map00910 )
• Selenoamino Acid Metabolism (map00450 )

• L-cystathionine + H2O = L-cysteine + ammonia + 2-oxobutanoate

• Cys_Met_Meta_PP (PF01053 )

• None

• None

ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCGGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG

1. Lu Y, O'Dowd BF, Orrego H, Israel Y: Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun. 1992 Dec 15;189(2):749-58. [PubMed ]
2. Wang J, Hegele RA: Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH). Hum Genet. 2003 Apr;112(4):404-8. Epub 2003 Feb 6. [PubMed ]

1. LDH-B
2. LDH heart subunit
3. LDH-H
4. Renal carcinoma antigen NY-REN-46

MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLK
GEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKF
IIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLG
IHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAY
EVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARG
LTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL

• Cysteine Metabolism (map00272 )
• Gluconeogenesis (map00010 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )

• (S)-lactate + NAD+ = pyruvate + NADH + H+

• Ldh_1_C (PF02866 )
• Ldh_1_N (PF00056 )

• None

• None

ATGGCAACTCTTAAGGAAAAACTCATTGCACCAGTTGCGGAAGAAGAGGCAACAGTTCCA
AACAATAAGATCACTGTAGTGGGTGTTGGACAAGTTGGTATGGCGTGTGCTATCAGCATT
CTGGGAAAG

1. Takeno T, Li SS: Structure of the human lactate dehydrogenase B gene. Biochem J. 1989 Feb 1;257(3):921-4. [PubMed ]
2. Sakai I, Sharief FS, Pan YC, Li SS: The cDNA and protein sequences of human lactate dehydrogenase B. Biochem J. 1987 Dec 15;248(3):933-6. [PubMed ]
3. 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 ]
4. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit. Hum Genet. 1993 Jun;91(5):423-6. [PubMed ]
5. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Detection and characterization of new genetic mutations in individuals heterozygous for lactate dehydrogenase-B(H) deficiency using DNA conformation polymorphism analysis and silver staining. Hum Genet. 1993 Mar;91(2):163-8. [PubMed ]
6. Sudo K, Maekawa M, Tomonaga A, Tsukada T, Nakayama T, Kitamura M, Li SS, Kanno T, Toriumi J: Molecular characterization of genetic mutations in human lactate dehydrogenase (LDH) B (H) variant. Hum Genet. 1992 May;89(2):158-62. [PubMed ]
7. Sudo K, Maekawa M, Ikawa S, Machida K, Kitamura M, Li SS: A missense mutation found in human lactate dehydrogenase-B (H) variant gene. Biochem Biophys Res Commun. 1990 Apr 30;168(2):672-6. [PubMed ]
8. Shonnard GC, Hud NV, Mohrenweiser HW: Arginine to tryptophan substitution in the active site of a human lactate dehydrogenase variant--LDHB GUA1: postulated effects on subunit structure and catalysis. Biochim Biophys Acta. 1996 Jan 17;1315(1):9-14. [PubMed ]
9. Sudo K, Maekawa M, Houki N, Okuda T, Akizuki S, Magara T, Kawano K: A novel in-frame deletion mutation in a case of lactate dehydrogenase (LD) H subunit deficiency showing an atypical LD isoenzyme pattern in serum and erythrocytes. Clin Biochem. 1999 Mar;32(2):137-41. [PubMed ]
10. Hidaka K, Ueda N, Hirata I, Watanabe Y, Minatogawa Y, Iuchi I: First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate dehydrogenase gene detected in a Japanese patient. J Hum Genet. 1999;44(1):69-72. [PubMed ]
11. Takatani T, Takaoka N, Tatsumi M, Kawamoto H, Okuno Y, Morita K, Masutani T, Murakawa K, Okamoto Y: A novel missense mutation in human lactate dehydrogenase B-subunit gene. Mol Genet Metab. 2001 Aug;73(4):344-8. [PubMed ]

1. LDH-C
2. LDH testis subunit
3. LDH-X

MSTVKEQLIEKLIEDDENSQCKITIVGTGAVGMACAISILLKDLADELALVDVALDKLKG
EMMDLQHGSLFFSTSKITSGKDYSVSANSRIVIVTAGARQQEGETRLALVQRNVAIMKSI
IPAIVHYSPDCKILVVSNPVDILTYIVWKISGLPVTRVIGSGCNLDSARFRYLIGEKLGV
HPTSCHGWIIGEHGDSSVPLWSGVNVAGVALKTLDPKLGTDSDKEHWKNIHKQVIQSAYE
IIKLKGYTSWAIGLSVMDLVGSILKNLRRVHPVSTMVKGLYGIKEELFLSIPCVLGRNGV
SDVVKINLNSEEEALFKKSAETLWNIQKDLIF

• Cysteine Metabolism (map00272 )
• Gluconeogenesis (map00010 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )

• (S)-lactate + NAD+ = pyruvate + NADH + H+

• Ldh_1_C (PF02866 )
• Ldh_1_N (PF00056 )

• None

• None

ATGTCAACTGTCAAGGAGCAGCTAATTGAGAAGCTAATTGAGGATGATGAAAACTCCCAG
TGTAAAATTACTATTGTTGGAACTGGTGCCGTAGGCATGGCTTGTGCTATTAGTATCTTA
CTGAAGGATTTGGCTGATGAACTTGCCCTTGTTGATGTTGCATTGGACAAACTGAAGGGA
GAAATGATGGATCTTCAGCATGGCAGTCTTTTCTTTAGTACTTCAAAGGTTACTTCTGGA
AAAGATTACAGTGTATCTGCAAACTCCAGAATAGTTATTGTCACAGCAGGTGCAAGGCAG
CAGGAGGGAGAAACTCGCCTTGCCCTGGTCCAACGTAATGTGGCTATAATGAAAATAATC
ATTCCTGCCATAGTCCATTATAGTCCTGATTGTAAAATTCTTGTTGTTTCAAATCCAGTG
GATATTTTGACATATATAGTCTGGAAGATAAGTGGCTTACCTGTAACTCGTGTAATTGGA
AGTGGTTGTAATCTAGACTCTGCCCGTTTCCGTTACCTAATTGGAGAAAAGTTGGGTGTC
CACCCCACAAGCTGCCATGGTTGGATTATTGGAGAACATGGTGATTCTAGTGTGCCCTTA
TGGAGTGGGGTGAATGTTGCTGGTGTTGCTCTGAAGACTCTGGACCCTAAATTAGGAACG
GATTCAGATAAGGAACACTGGAAAAATATCCATAAACAAGTTATTCAAAGTGCCTATGAA
ATTATCAAGCTGAAGGGGTATACCTCTTGGGCTATTGGACTGTCTGTGATGGATCTGGTA
GGATCCATTTTGAAAAATCTTAGGAGAGTGCACCCAGTTTCCACCATGGTTAAGGGATTA
TATGGAATAAAAGAAGAACTCTTTCTCAGTATCCCTTGTGTCTTGGGGCGGAATGGTGTC
TCAGATGTTGTGAAAATTAACTTGAATTCTGAGGAGGAGGCCCTTTTCAAGAAGAGTGCA
GAAACACTTTGGAATATTCAAAAGGATCTAATATTTTAA

1. Millan JL, Driscoll CE, LeVan KM, Goldberg E: Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5311-5. [PubMed ]
2. Takano T, Li SS: Human testicular lactate dehydrogenase-C gene is interrupted by six introns at positions homologous to those of LDH-A (muscle) and LDH-B (heart) genes. Biochem Biophys Res Commun. 1989 Mar 15;159(2):579-83. [PubMed ]

MSWTVPVVRASQRVSSVGANFLCLGMALCPRQATRIPLNGTWLFTPVSKMATVKSELIER
FTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPF
TKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHC
KLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILG
EHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWA
IGLSVADLTESILKNLRRIHPVSTIIKGLYGIDEEVFLSIPCILGENGITNLIKIKLTPE
EEAHLKKSAKTLWEIQNKLKL

• Cysteine Metabolism (map00272 )
• Gluconeogenesis (map00010 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )

• (S)-lactate + NAD+ = pyruvate + NADH + H+

• Ldh_1_C (PF02866 )
• Ldh_1_N (PF00056 )

• None

• None

ATGAGTTGGACTGTGCCTGTTGTGCGGGCCAGCCAGAGAGTGAGCTCGGTGGGAGCGAAT
TTCCTATGCCTGGGGATGGCCCTGTGTCCGCGTCAAGCAACGCGCATCCCGCTCAACGGC
ACCTGGCTCTTCACCCCCGTGAGCAAGATGGCGACTGTGAAGAGTGAGCTTATTGAGCGT
TTCACTTCCGAGAAGCCCGTTCATCACAGTAAGGTCTCCATCATAGGAACTGGATCGGTG
GGCATGGCCTGCGCTATCAGCATCTTATTAAAAGGCTTGAGTGATGAACTTGCCCTTGTG
GATCTTGATGAAGACAAACTGAAGGGTGAGACGATGGATCTTCAACATGGCAGCCCTTTC
ACGAAAATGCCAAATATTGTTTGTAGCAAAGATTACTTTGTCACAGCAAACTCCAACCTA
GTGATTATCACAGCAGGTGCACGCCAAGAAAAGGGAGAAACGCGCCTTAATTTAGTCCAG
CGAAATGTGGCCATCTTCAAGTTAATGATTTCCAGTATTGTCCAGTACAGCCCCCACTGC
AAACTGATTATTGTTTCCAATCCAGTGGATATCTTAACTTATGTAGCTTGGAAGTTGAGT
GCATTTCCCAAAAACCGTATTATTGGAAGCGGCTGTAATCTGGATACTGCTCGTTTTCGT
TTCTTGATTGGACAAAAGCTTGGTATCCATTCTGAAAGCTGCCATGGATGGATCCTCGGA
GAGCATGGAGACTCAAGTGTTCCTGTGTGGAGTGGAGTGAACATAGCTGGTGTCCCTTTG
AAGGATCTGAACTCTGATATAGGAACTGATAAAGATCCTGAGCAATGGAAAAATGTCCAC
AAAGAAGTGACTGCAACTGCCTATGAGATTATTAAAATGAAAGGTTATACTTCTTGGGCC
ATTGGCCTATCTGTGGCCGATTTAACAGAAAGTATTTTGAAGAATCTTAGGAGAATACAT
CCAGTTTCCACCATAATTAAGGGCCTCTATGGAATAGATGAAGAAGTATTCCTCAGTATT
CCTTGTATCCTGGGAGAGAACGGTATTACCAACCTTATAAAGATAAAGCTGACCCCTGAA
GAAGAGGCCCATCTGAAAAAAAGTGCAAAAACACTCTGGGAAATTCAGAATAAGCTTAAG
CTTTAA

MATIKSELIKNFAEEEAIHHNKISIVGTGSVGVACAISILLKGLSDELVLVDVDEGKLKG
ETMDLQHGSPFMKMPNIVSSKDYLVTANSNLVIITAGARQKKGETRLDLVQRNVSIFKLM
IPNITQYSPHCKLLIVTNPVDILTYVAWKLSGFPKNRVIGSGCNLDSARFRYFIGQRLGI
HSESCHGLILGEHGDSSVPVWSGVNIAGVPLKDLNPDIGTDKDPEQWENVHKKVISSGYE
MVKMKGYTSWGISLSVADLTESILKNLRRVHPVSTLSKGLYGINEDIFLSVPCILGENGI
TDLIKVKLTLEEEACLQKSAETLWEIQKELKL

• Cysteine Metabolism (map00272 )
• Gluconeogenesis (map00010 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )

• (S)-lactate + NAD+ = pyruvate + NADH + H+

• Ldh_1_C (PF02866 )
• Ldh_1_N (PF00056 )

• None

• None

ATGGCAACTATCAAGAGTGAACTTATTAAGAATTTCGCGGAAGAGGAGGCCATTCATCAC
AATAAGATCTCCATTGTAGGAACTGGATCGGTTGGTGTGGCTTGTGCTATCAGCATCTTA
TTAAAAGGTTTGAGTGATGAACTTGTCCTTGTGGATGTTGATGAAGGCAAACTGAAGGGT
GAGACAATGGATCTTCAACATGGCAGCCCTTTTATGAAAATGCCAAATATTGTCTCCAGC
AAAGATTACCTGGTCACTGCAAACTCCAATCTAGTGATTATCACAGCAGGTGCACGCCAG
AAAAAAGGAGAAACACGCCTTGATTTAGTCCAGCGAAATGTATCCATCTTTAAATTAATG
ATTCCCAATATTACCCAGTACAGTCCTCACTGCAAACTGCTTATTGTTACTAATCCAGTG
GATATCTTAACTTATGTAGCCTGGAAGTTGAGTGGATTTCCCAAAAACCGTGTTATTGGA
AGTGGTTGTAATCTGGACTCTGCTCGTTTTCGTTACTTTATTGGGCAAAGGCTTGGCATC
CACTCTGAAAGCTGTCATGGGCTGATCCTTGGAGAGCATGGCGACTCAAGTGTTCCTGTG
TGGAGTGGTGTGAACATTGCTGGCGTCCCTCTGAAGGATCTGAACCCAGATATAGGAACT
GATAAAGATCCTGAGCAGTGGGAAAATGTCCACAAAAAAGTGATTTCCAGTGGCTATGAG
ATGGTCAAAATGAAAGGTTATACTTCTTGGGGCATTAGCCTATCTGTAGCTGATTTAACA
GAAAGTATTTTGAAGAATCTTAGGAGAGTGCATCCAGTTTCTACCCTAAGTAAGGGCCTC
TATGGAATAAATGAAGACATATTCCTTAGTGTCCCATGTATCCTGGGAGAGAATGGTATC
ACAGACCTCATAAAAGTAAAACTGACTCTTGAAGAGGAGGCCTGCTTGCAAAAGAGTGCA
GAAACACTTTGGGAAATTCAGAAGGAGCTCAAGCTTTAA

1. Urocanase
2. Imidazolonepropionate hydrolase

MSSLQALCSGLPLRPLPENRGRQAGVPHAPVRTPSLSPVEKQLALRNALRYFPPDVQELL
APEFAQELQLYGHIYMYRFCPDIEMRAYPIEQYPCQTKVAAAIMHMIMNNLDPAVAQFPQ
ELVTYGGNGQVFSNWAQFWLTMFYLSKMTEEQTLVMYSGHPLGLFPSSRSAPRLVITNGM
VIPNYSSRTEYEKLFALGVTMYGQMTAGSYCYIGPQGIVHGTVLTVLNAARRYLGIEDLA
GKVFVTSGLGGMSGAQAKAAVIVGCIGVIAEVDKAALEKRHRQGWLMEVTDSLDRCIQRL
REARKKKEVLSLGYHGNVVALWERLVHELDTTGECLVDLGSDQTSCHNPFNGGYYPVQLS
FTEAQSLMASNPAVFKDLVQESLRRQVSAINRLAEEKFFFWDYGNAFLLEAQRAGADVEK
KGAGRTEFRYPSYVQHIMGDIFSQGFGPFRWVCTSGDPQDLAVTDELATSVLEEAIADGV
KVSVKLQYMDNIRWIREAARHRLVVGSQARILYSDQKGRVAIAVAINQAIACRRIKAPVV
LSRDHHDVSGTDSPFRETSNIYDGSAFCADMAVQNFVGDACRGATWVALHNGGGVGWGEV
INGGFGLVLDGTPEAEGRARLMLSWDVSNGVARRCWSGNQKAYEIICQTMQENSTLVVTL
PHKVEDERVLQQALQL

• Histidine Metabolism (map00340 )

• 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O

• Urocanase (PF01175 )

• None

• None

ATGTCTAGCCTCCAGGCGCTGTGCTCTGGCCTGCCCCTGCGGCCCCTCCCAGAGAACCGG
GGACGCCAGGCTGGGGTGCCCCATGCCCCTGTCAGGACCCCCAGCCTCAGCCCTGTGGAG
AAACAGCTGGCGCTGAGGAACGCCCTGCGCTACTTCCCCCCGGATGTCCAGGAGCTGCTG
GCCCCAGAGTTTGCCCAGGAGCTGCAACTGTACGGACACATCTACATGTACCGGTTTTGC
CCCGACATTGAAATGAGGGCCTACCCGATTGAGCAGTACCCCTGCCAGACGAAAGTGGCT
GCCGCCATCATGCACATGATTATGAACAACCTGGATCCTGCCGTGGCCCAGTTTCCCCAG
GAGCTGGTGACCTATGGAGGAAATGGGCAGGTGTTCAGCAACTGGGCTCAGTTCTGGCTG
ACCATGTTCTACTTGTCGAAGATGACAGAGGAGCAGACTTTGGTCATGTACAGTGGGCAC
CCACTTGGCCTCTTTCCCAGCAGCCGCAGTGCCCCACGGCTCGTCATCACCAATGGGATG
GTCATTCCCAACTACTCCTCCCGGACGGAGTATGAGAAGCTCTTTGCCTTGGGGGTTACA
ATGTACGGCCAGATGACAGCAGGTAGCTACTGCTACATCGGTCCCCAGGGAATCGTTCAT
GGCACTGTGCTCACCGTGTTGAATGCTGCACGTCGGTACCTGGGCATCGAGGACTTGGCT
GGGAAGGTCTTTGTCACCTCTGGGCTCGGCGGAATGAGTGGGGCTCAGGCCAAGGCCGCA
GTCATCGTGGGGTGCATCGGTGTGATAGCAGAGGTGGATAAAGCAGCCCTTGAGAAACGC
CACAGGCAGGGCTGGCTGATGGAAGTGACTGACAGCTTGGACCGCTGCATCCAGAGGCTC
AGGGAAGCAAGGAAAAAAAAGGAGGTGCTCAGCCTTGGTTACCATGGCAACGTGGTGGCT
CTTTGGGAGCGCCTGGTCCACGAATTGGACACGACGGGGGAGTGCTTGGTGGACCTGGGG
TCAGATCAGACATCCTGCCACAACCCGTTCAATGGCGGCTACTACCCTGTGCAGCTCAGC
TTCACGGAGGCCCAGAGCCTCATGGCCTCCAACCCTGCTGTGTTCAAGGACCTGGTCCAG
GAAAGCCTGAGGAGGCAAGTCTCAGCCATCAACAGGTTGGCCGAGGAGAAGTTCTTCTTC
TGGGACTACGGCAATGCCTTCCTCTTGGAGGCCCAGAGAGCAGGAGCGGATGTGGAGAAG
AAAGGTGCTGGCAGGACAGAGTTCCGCTACCCTTCCTATGTGCAGCACATCATGGGGGAC
ATATTCTCCCAGGGATTTGGGCCTTTCCGCTGGGTGTGCACATCGGGGGACCCCCAGGAC
CTGGCGGTCACAGACGAACTGGCCACATCTGTGCTGGAGGAAGCCATTGCTGATGGAGTG
AAGGTGTCTGTGAAGCTGCAGTACATGGACAACATCCGCTGGATCCGGGAGGCCGCCAGG
CACCGGCTGGTGGTGGGCTCCCAGGCAAGGATCTTGTACTCAGACCAGAAGGGCCGCGTG
GCCATCGCTGTGGCCATTAACCAGGCCATCGCCTGCAGGAGGATCAAGGCGCCGGTGGTC
CTGAGCCGAGATCACCATGACGTGAGCGGCACCGACAGCCCCTTTAGGGAGACCTCCAAC
ATTTACGACGGCTCTGCCTTCTGTGCAGACATGGCTGTGCAGAACTTCGTGGGAGATGCC
TGTCGCGGAGCCACCTGGGTCGCCCTTCACAACGGAGGGGGCGTGGGCTGGGGTGAGGTG
ATCAACGGGGGATTCGGCCTCGTGCTGGACGGTACCCCGGAGGCCGAGGGGAGAGCCAGG
CTGATGCTCAGCTGGGATGTCTCCAATGGTGTGGCCCGGCGCTGCTGGTCAGGGAACCAG
AAGGCCTATGAGATCATCTGCCAGACCATGCAGGAGAACAGCACCTTGGTGGTGACACTG
CCTCACAAGGTGGAGGACGAGCGGGTGCTCCAGCAGGCCCTGCAGCTCTGA

1. Branched-chain alpha-ketoacid dehydrogenase kinase
2. BCKDHKIN
3. BCKD-kinase

MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAID
AAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNP
TILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHI
EDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARR
LCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVI
TIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQS
GPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI

• HATPase_c (PF02518 )

• 1-26

ATGATCCTGGCGTCGGTGCTGAGGAGCGGTCCCGGGGGCGGGCTTCCGCTCCGGCCCCTC
CTGGGACCCGCACTCGCGCTCCGGGCCCGCTCGACGTCGGCCACCGACACACACCACGTG
GAGATGGCTCGGGAGCGCTCCAAGACCGTCACCTCCTTTTACAACCAGTCGGCCATCGAC
GCGGCAGCGGAGAAGCCCTCAGTCCGCCTAACGCCCACCATGATGCTCTACGCTGGCCGC
TCTCAGGACGGCAGCCACCTTCTGAAAAGTGCTCGGTACCTGCAGCAAGAACTTCCAGTG
AGGATTGCTCACCGCATCAAGGGCTTCCGCTGCCTTCCTTTCATCATTGGCTGCAACCCC
ACCATACTGCACGTGCATGAGCTATATATCCGTGCCTTCCAGAAGCTGACAGACTTCCCT
CCGATCAAGGACCAGGCGGACGAGGCCCAGTACTGCCAGCTGGTGCGACAGCTGCTGGAT
GACCACAAGGATGTGGTGACCCTCTTGGCAGAGGGCCTACGTGAGAGCCGGAAGCACATA
GAGGATGAAAAGCTCGTCCGCTACTTCTTGGACAAGACGCTGACTTCGAGGCTTGGAATC
CGCATGTTGGCCACGCATCACCTGGCGCTGCATGAGGACAAGCCTGACTTTTTCGGCATC
ATCTGTACTCGTCTCTCACCAAAGAAGATTATTGAGAAGTGGGTGGACTTTGCCAGACGC
CTGTGTGAGCACAAGTATGGCAATGCGCCCCGTGTCCGCATCAATGGCCATGTGGCTGCC
CGGTTCCCCTTCATCCCTATGCCACTGGACTACATCCTGCCGGAGCTGCTCAAGAATGCC
ATGAGAGCCACAATGGAGAGTCACCTAGACACTCCCTACAATGTCCCAGATGTGGTCATC
ACCATCGCCAACAATGATGTCGATCTGATCATCAGGATCTCAGACCGTGGTGGAGGAATC
GCTCACAAAGATCTGGACCGGGTCATGGACTACCACTTCACTACTGCTGAGGCCAGCACA
CAGGACCCCCGGATCAGCCCCCTCTTTGGCCATCTGGACATGCATAGTGGCGCCCAGTCA
GGACCCATGCACGGCTTTGGCTTCGGGTTGCCCACGTCACGGGCCTACGCGGAGTACCTC
GGTGGGTCTCTGCAGCTGCAGTCCCTGCAGGGCATTGGCACGGACGTCTACCTGCGGCTC
CGCCACATCGATGGCCGGGAGGAAAGCTTCCGGATCTGA

1. Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
2. TML-alpha- ketoglutarate dioxygenase
3. TML hydroxylase
4. TML dioxygenase
5. TMLD

MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A

• Lysine Degradation (map00310 )

• 2-Oxoglutarate + O2 + N6,N6,N6-Trimethyl-L-lysine --> 3-Hydroxy-N6,N6,N6-trimethyl-L-lysine + CO2 + Succinate

• TauD (PF02668 )

• None

• None

1. Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ: Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. J Biol Chem. 2001 Sep 7;276(36):33512-7. Epub 2001 Jun 28. [PubMed ]

1. Alkylated DNA repair protein alkB homolog 2
2. Oxy DC1

MDRFLVKGAQGGLLRKQEEQEPTGEEPAVLGGDKESTRKRPRREAPGNGGHSAGPSWRHI
RAEGLDCSYTVLFGKAEADEIFQELEKEVEYFTGALARVQVFGKWHSVPRKQATYGDAGL
TYTFSGLTLSPKPWIPVLERIRDHVSGVTGQTFNFVLINRYKDGCDHIGEHRDDERELAP
GSPIASVSFGACRDFVFRHKDSRGKSPSRRVAVVRLPLAHGSLLMMNHPTNTHWYHSLPV
RKKVLAPRVNLTFRKILLTKK

• 2OG-FeII_Oxy (PF03171 )

• None

• None

ATGGACAGATTCCTGGTGAAAGGGGCTCAAGGGGGCCTTTTGAGGAAGCAGGAGGAGCAA
GAGCCAACTGGAGAAGAGCCAGCTGTGTTGGGAGGAGACAAAGAAAGCACAAGGAAGAGG
CCCAGGGGAGAGGCCCCAGGGAATGGAGGCCACTCAGCAGGCCCTAGCTGGCGGCACATT
CGGGCTGAGGGCCTGGACTGCAGTTACACAGTCCTGTTTGGCAAAGCTGAGGCAGATGAG
ATTTTCCAAGAGTTGGAGAAAGAAGTAGAATATTTTACAGGAGCACTGGCCAGAGTCCAG
GTATTCGGGAAGTGGCACAGTGTGCCCAGGAAGCAAGCAACGTATGGCGACGCTGGGCTG
ACCTACACATTTTCAGGCCTCACGCTGTCTCCAAAGCCCTGGATCCCAGTTCTAGAGCGC
ATCCGGGATCACGTCTCTGGGGTGACTGGACAGACCTTCAACTTTGTGCTCATCAACAGG
TATAAAGATGGCTGTGACCACATCGGGGAGCACCGAGATGATGAAAGAGAACTGGCCCCT
GGGAGCCCCATTGCCTCTGTCTCCTTCGGTGCCTGCAGAGACTTTGTCTTCCGGCATAAG
GATTCCCGTGGGAAAAGCCCCTCCAGGAGGGTGGCGGTGGTCAGGCTGCCGCTGGCCCAC
GGGAGCTTACTAATGATGAACCACCCGACCAACACGCACTGGTACCACAGTCTTCCCGTG
AGAAAGAAGGTTCTGGCTCCACGGGTGAATCTGACTTTTCGTAAAATTTTGCTTACTAAA
AAATAA

1. Alkylated DNA repair protein alkB homolog 3
2. Prostate cancer antigen 1
3. DEPC-1

MEEKRRRARVQGAWAAPVKSQAIAQPATTAKSHLHQKPGQTWKNKEHHLSDREFVFKEPQ
QVVRRAPEPRVIDREGVYEISLSPTGVSRVCLYPGFVDVKEADWILEQLCQDVPWKQRTG
IREDITYQQPRLTAWYGELPYTYSRITMEPNPHWHPVLRTLKNRIEENTGHTFNSLLCNL
YRNEKDSVDWHSDDEPSLGRCPIIASLSFGATRTFEMRKKPPPEENGDYTYVERVKIPLD
HGTLLIMEGATQADWQHRVPKEYHSREPRVNLTFRTVYPDPRGAPW

• None

• None

ATGGAGGAAAAAAGACGGCGAGCCCGAGTTCAGGGAGCCTGGGCTGCCCCTGTTAAAAGC
CAGGCCATTGCTCAGCCAGCTACCACTGCTAAGAGCCATCTCCACCAGAAGCCTGGCCAG
ACCTGGAAGAACAAAGAGCATCATCTCTCTGACAGAGAGTTTGTGTTCAAAGAACCTCAG
CAGGTAGTACGTAGAGCTCCTGAGCCACGAGTGATTGACAGAGAGGGTGTGTATGAAATC
AGCCTGTCACCCACAGGTGTATCTAGGGTCTGTTTGTATCCTGGCTTTGTTGACGTGAAA
GAAGCTGACTGGATATTGGAACAGCTTTGTCAAGATGTTCCCTGGAAACAGAGGACCGGC
ATCAGAGAGGATATAACTTATCAGCAACCAAGACTTACAGCATGGTATGGAGAACTTCCT
TACACTTATTCAAGAATCACTATGGAACCAAATCCTCACTGGCACCCTGTGCTGCGCACA
CTAAAGAACCGCATTGAAGAGAACACTGGCCACACCTTCAACTCCTTACTCTGCAATCTT
TATCGCAATGAGAAGGACAGCGTGGACTGGCACAGTGATGATGAACCCTCACTAGGGAGG
TGCCCCATTATTGCTTCACTAAGTTTTGGTGCCACACGCACATTTGAGATGAGAAAGAAG
CCACCACCAGAAGAGAATGGAGACTACACATATGTGGAAAGAGTGAAGATACCCTTGGAT
CATGGGACCTTGTTAATCATGGAAGGAGCGACACAAGCTGACTGGCAGCATCGAGTGCCC
AAAGAATACCACTCTAGAGAACCGAGAGTGAACCTGACCTTTCGGACAGTCTATCCAGAC
CCTCGAGGGGCACCCTGGTGA

1. Alpha-ketoglutarate dehydrogenase-like

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

• E1_dh (PF00676 )
• Transket_pyr (PF02779 )

• 1-15

• None

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

1. 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 ]

1. Alpha-ketoglutarate receptor 1
2. G-protein coupled receptor 80
3. G-protein coupled receptor 99
4. P2Y purinoceptor 15
5. P2Y-like nucleotide receptor
6. P2Y-like GPCR

MNEPLDYLANASDFPDYAAAFGNCTDENIPLKMHYLPVIYGIIFLVGFPGNAVVISTYIF
KMRPWKSSTIIMLNLACTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFSFHFNLYSS
ILFLTCFSIFRYCVIIHPMSCFSIHKTRCAVVACAVVWIISLVAVIPMTFLITSTNRTNR
SACLDLTSSDELNTIKWYNLILTATTFCLPLVIVTLCYTTIIHTLTHGLQTDSCLKQKAR
RLTILLLLAFYVCFLPFHILRVIRIESRLLSISCSIENQIHEAYIVSRPLAALNTFGNLL
LYVVVSDNFQQAVCSTVRCKVSGNLEQAKKISYSNNP

• 7tm_1 (PF00001 )

• None

• 35-55 70-90 117-137 152-172 202-222 243-263 285-305

ATGAATGAGCCACTAGACTATTTAGCAAATGCTTCTGATTTCCCCGATTATGCAGCTGCT
TTTGGAAATTGCACTGATGAAAACATCCCACTCAAGATGCACTACCTCCCTGTTATTTAT
GGCATTATCTTCCTCGTGGGATTTCCAGGCAATGCAGTAGTGATATCCACTTACATTTTC
AAAATGAGACCTTGGAAGAGCAGCACCATCATTATGCTGAACCTGGCCTGCACAGATCTG
CTGTATCTGACCAGCCTCCCCTTCCTGATTCACTACTATGCCAGTGGCGAAAACTGGATC
TTTGGAGATTTCATGTGTAAGTTTATCCGCTTCAGCTTCCATTTCAACCTGTATAGCAGC
ATCCTCTTCCTCACCTGTTTCAGCATCTTCCGCTACTGTGTGATCATTCACCCAATGAGC
TGCTTTTCCATTCACAAAACTCGATGTGCAGTTGTAGCCTGTGCTGTGGTGTGGATCATT
TCACTGGTAGCTGTCATTCCGATGACCTTCTTGATCACATCAACCAACAGGACCAACAGA
TCAGCCTGTCTCGACCTCACCAGTTCGGATGAACTCAATACTATTAAGTGGTACAACCTG
ATTTTGACTGCAACTACTTTCTGCCTCCCCTTGGTGATAGTGACACTTTGCTATACCACG
ATTATCCACACTCTGACCCATGGACTGCAAACTGACAGCTGCCTTAAGCAGAAAGCACGA
AGGCTAACCATTCTGCTACTCCTTGCATTTTACGTATGTTTTTTACCCTTCCATATCTTG
AGGGTCATTCGGATCGAATCTCGCCTGCTTTCAATCAGTTGTTCCATTGAGAATCAGATC
CATGAAGCTTACATCGTTTCTAGACCATTAGCTGCTCTGAACACCTTTGGTAACCTGTTA
CTATATGTGGTGGTCAGCGACAACTTTCAGCAGGCTGTCTGCTCAACAGTGAGATGCAAA
GTAAGCGGGAACCTTGAGCAAGCAAAGAAAATTAGTTACTCAAACAACCCTTGA

1. Lee DK, Nguyen T, Lynch KR, Cheng R, Vanti WB, Arkhitko O, Lewis T, Evans JF, George SR, O'Dowd BF: Discovery and mapping of ten novel G protein-coupled receptor genes. Gene. 2001 Sep 5;275(1):83-91. [PubMed ]
2. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed ]

MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKG
EMMDLQHGSLFLRTPKIVSGKVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERL
GVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESA
YEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQN
GISDLVKVTLTSEEEARLKKSADTLWGIQKELQF

• (S)-lactate + NAD+ = pyruvate + NADH + H+ [RN:R00703] ALL_REAC R00703
• (other) R01000 R03104

• Ldh_1_C (PF02866 )
• Ldh_1_N (PF00056 )

• None

• None