Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
Details
- Name
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Synonyms
- 2.6.1.62
- 7,8-diamino-pelargonic acid aminotransferase
- 7,8-diaminononanoate synthase
- DANS
- DAPA aminotransferase
- DAPA AT
- Diaminopelargonic acid synthase
- Gene Name
- bioA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011074|Adenosylmethionine-8-amino-7-oxononanoate aminotransferase MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYN HPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQS RMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGE AGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQRLTAAVNRA VQDETFFCQ
- Number of residues
- 429
- Molecular Weight
- 47335.21
- Theoretical pI
- 5.71
- GO Classification
- Functionsadenosylmethionine-8-amino-7-oxononanoate transaminase activity / identical protein binding / pyridoxal phosphate bindingProcessesbiotin biosynthetic processComponentscytoplasm
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor.
- Pfam Domain Function
- Aminotran_3 (PF00202)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0011075|Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (bioA) ATGACAACGGACGATCTTGCCTTTGACCAACGCCATATCTGGCACCCATACACATCCATG ACCTCCCCTCTGCCGGTTTATCCGGTGGTGAGCGCCGAAGGTTGCGAGCTGATTTTGTCT GACGGCAGACGCCTGGTTGACGGTATGTCGTCCTGGTGGGCGGCGATCCACGGCTACAAT CACCCGCAGCTTAATGCGGCGATGAAGTCGCAAATTGATGCCATGTCGCATGTGATGTTT GGCGGTATCACCCATGCGCCAGCCATTGAGCTGTGCCGCAAACTGGTGGCGATGACGCCG CAACCGCTGGAGTGCGTTTTTCTCGCGGACTCCGGTTCCGTAGCGGTGGAAGTGGCGATG AAAATGGCGTTGCAGTACTGGCAAGCCAAAGGCGAAGCGCGCCAGCGTTTTCTGACCTTC CGCAATGGTTATCATGGCGATACCTTTGGCGCGATGTCGGTGTGCGATCCGGATAACTCA ATGCACAGTCTGTGGAAAGGCTACCTGCCAGAAAACCTGTTTGCTCCCGCCCCGCAAAGC CGCATGGATGGCGAATGGGATGAGCGCGATATGGTGGGCTTTGCCCGCCTGATGGCGGCG CATCGTCATGAAATCGCGGCGGTGATCATTGAGCCGATTGTCCAGGGCGCAGGCGGGATG CGCATGTACCATCCGGAATGGTTAAAACGAATCCGCAAAATATGCGATCGCGAAGGTATC TTGCTGATTGCCGACGAGATCGCCACTGGATTTGGTCGTACCGGGAAACTGTTTGCCTGT GAACATGCAGAAATCGCGCCGGACATTTTGTGCCTCGGTAAAGCCTTAACCGGCGGCACA ATGACCCTTTCCGCCACACTCACCACGCGCGAGGTTGCAGAAACCATCAGTAACGGTGAA GCCGGTTGCTTTATGCATGGGCCAACTTTTATGGGCAATCCGCTGGCCTGCGCGGCAGCA AACGCCAGCCTGGCGATTCTCGAATCTGGCGACTGGCAGCAACAGGTGGCGGATATTGAA GTACAGCTGCGCGAGCAACTTGCCCCCGCCCGTGATGCCGAAATGGTTGCCGATGTGCGC GTACTGGGGGCCATTGGCGTGGTCGAAACCACTCATCCGGTGAATATGGCGGCGCTGCAA AAATTCTTTGTCGAACAGGGTGTCTGGATCCGGCCTTTTGGCAAACTGATTTACCTGATG CCGCCCTATATTATTCTCCCGCAACAGTTGCAGCGTCTGACCGCAGCGGTTAACCGCGCG GTACAGGATGAAACATTTTTTTGCCAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P12995 UniProtKB Entry Name BIOA_ECOLI GenBank Protein ID 457106 GenBank Gene ID J04423 - General References
- Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J: The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon. J Biol Chem. 1988 Dec 25;263(36):19577-85. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Stoner GL, Eisenberg MA: Purification and properties of 7, 8-diaminopelargonic acid aminotransferase. J Biol Chem. 1975 Jun 10;250(11):4029-36. [Article]
- Stoner GL, Eisenberg MA: Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction. J Biol Chem. 1975 Jun 10;250(11):4037-43. [Article]
- Barker DF, Campbell AM: Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli. J Mol Biol. 1981 Mar 15;146(4):469-92. [Article]
- Mann S, Marquet A, Ploux O: Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues. Biochem Soc Trans. 2005 Aug;33(Pt 4):802-5. [Article]
- Lin S, Hanson RE, Cronan JE: Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat Chem Biol. 2010 Sep;6(9):682-8. doi: 10.1038/nchembio.420. Epub 2010 Aug 8. [Article]
- Kack H, Sandmark J, Gibson K, Schneider G, Lindqvist Y: Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes. J Mol Biol. 1999 Aug 27;291(4):857-76. [Article]
- Eliot AC, Sandmark J, Schneider G, Kirsch JF: The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Biochemistry. 2002 Oct 22;41(42):12582-9. [Article]
- Sandmark J, Mann S, Marquet A, Schneider G: Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin. J Biol Chem. 2002 Nov 8;277(45):43352-8. Epub 2002 Sep 5. [Article]
- Sandmark J, Eliot AC, Famm K, Schneider G, Kirsch JF: Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis. Biochemistry. 2004 Feb 10;43(5):1213-22. [Article]