Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (P12995)

Identification
Name:Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
Synonyms:
  • 7,8-diamino-pelargonic acid aminotransferase
  • DAPA AT
  • DAPA aminotransferase
  • Diaminopelargonic acid synthase
Gene Name:bioA
Enzyme Class:
Biological Properties
General Function:Involved in transaminase activity
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
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.08-Amino-7-oxononanoate + 1.0S-Adenosylmethionine ↔ 1.0S-Adenosyl-4-methylthio-2-oxobutanoate + 1.07,8-Diaminononanoate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0S-adenosyl-L-methionine → 1.0Thumb+1.07,8-Diaminononanoate+1.0Thumb
1.08-Amino-7-oxononanoate + 1.0S-adenosyl-L-methionine → 1.0a sulfurated [sulfur carrier] + 1.07,8-Diaminononanoate + 1.07,8-Diaminononanoate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.08-Amino-7-oxononanoate + 1.0S-Adenosylmethionine ↔ 1.0S-Adenosyl-4-methylthio-2-oxobutanoate + 1.07,8-Diaminononanoate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB201097,8-DiaminononanoateMetaboCard
ECMDB201118-Amino-7-oxononanoateMetaboCard
ECMDB24186a sulfurated [sulfur carrier]MetaboCard
ECMDB21282S-Adenosyl-4-methylthio-2-oxobutanoateMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
GO Classification:
Function
adenosylmethionine-8-amino-7-oxononanoate transaminase activity
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
transaminase activity
transferase activity
transferase activity, transferring nitrogenous groups
Process
biotin biosynthetic process
biotin metabolic process
metabolic process
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b0774
Gene OrientationCounterclockwise
Centisome Percentage:17.40
Left Sequence End807191
Right Sequence End808480
Gene Sequence:
>1290 bp
ATGACAACGGACGATCTTGCCTTTGACCAACGCCATATCTGGCACCCATACACATCCATG
ACCTCCCCTCTGCCGGTTTATCCGGTGGTGAGCGCCGAAGGTTGCGAGCTGATTTTGTCT
GACGGCAGACGCCTGGTTGACGGTATGTCGTCCTGGTGGGCGGCGATCCACGGCTACAAT
CACCCGCAGCTTAATGCGGCGATGAAGTCGCAAATTGATGCCATGTCGCATGTGATGTTT
GGCGGTATCACCCATGCGCCAGCCATTGAGCTGTGCCGCAAACTGGTGGCGATGACGCCG
CAACCGCTGGAGTGCGTTTTTCTCGCGGACTCCGGTTCCGTAGCGGTGGAAGTGGCGATG
AAAATGGCGTTGCAGTACTGGCAAGCCAAAGGCGAAGCGCGCCAGCGTTTTCTGACCTTC
CGCAATGGTTATCATGGCGATACCTTTGGCGCGATGTCGGTGTGCGATCCGGATAACTCA
ATGCACAGTCTGTGGAAAGGCTACCTGCCAGAAAACCTGTTTGCTCCCGCCCCGCAAAGC
CGCATGGATGGCGAATGGGATGAGCGCGATATGGTGGGCTTTGCCCGCCTGATGGCGGCG
CATCGTCATGAAATCGCGGCGGTGATCATTGAGCCGATTGTCCAGGGCGCAGGCGGGATG
CGCATGTACCATCCGGAATGGTTAAAACGAATCCGCAAAATATGCGATCGCGAAGGTATC
TTGCTGATTGCCGACGAGATCGCCACTGGATTTGGTCGTACCGGGAAACTGTTTGCCTGT
GAACATGCAGAAATCGCGCCGGACATTTTGTGCCTCGGTAAAGCCTTAACCGGCGGCACA
ATGACCCTTTCCGCCACACTCACCACGCGCGAGGTTGCAGAAACCATCAGTAACGGTGAA
GCCGGTTGCTTTATGCATGGGCCAACTTTTATGGGCAATCCGCTGGCCTGCGCGGCAGCA
AACGCCAGCCTGGCGATTCTCGAATCTGGCGACTGGCAGCAACAGGTGGCGGATATTGAA
GTACAGCTGCGCGAGCAACTTGCCCCCGCCCGTGATGCCGAAATGGTTGCCGATGTGCGC
GTACTGGGGGCCATTGGCGTGGTCGAAACCACTCATCCGGTGAATATGGCGGCGCTGCAA
AAATTCTTTGTCGAACAGGGTGTCTGGATCCGGCCTTTTGGCAAACTGATTTACCTGATG
CCGCCCTATATTATTCTCCCGCAACAGTTGCAGCGTCTGACCGCAGCGGTTAACCGCGCG
GTACAGGATGAAACATTTTTTTGCCAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:429
Protein Molecular Weight:47335
Protein Theoretical pI:6
PDB File:1QJ5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYN
HPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM
KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQS
RMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI
LLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGE
AGCFMHGPTFMGNPLACAAANASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR
VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMPPYIILPQQLQRLTAAVNRA
VQDETFFCQ
References
External Links:
ResourceLink
Uniprot ID:P12995
Uniprot Name:BIOA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674757
PDB ID:1QJ5
Ecogene ID:EG10117
Ecocyc:EG10117
ColiBase:b0774
Kegg Gene:b0774
EchoBASE ID:EB0115
CCDB:BIOA_ECOLI
BacMap:16128742
General Reference:
  • Barker, D. F., Campbell, A. M. (1981). "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 146:469-492. Pubmed: 6456358
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Eliot, A. C., Sandmark, J., Schneider, G., Kirsch, J. F. (2002). "The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation." Biochemistry 41:12582-12589. Pubmed: 12379100
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kack, H., Sandmark, J., Gibson, K., Schneider, G., Lindqvist, Y. (1999). "Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes." J Mol Biol 291:857-876. Pubmed: 10452893
  • Mann, S., Marquet, A., Ploux, O. (2005). "Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues." Biochem Soc Trans 33:802-805. Pubmed: 16042602
  • Otsuka, A. J., Buoncristiani, M. R., Howard, P. K., Flamm, J., Johnson, C., Yamamoto, R., Uchida, K., Cook, C., Ruppert, J., Matsuzaki, J. (1988). "The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon." J Biol Chem 263:19577-19585. Pubmed: 3058702
  • Sandmark, J., Eliot, A. C., Famm, K., Schneider, G., Kirsch, J. F. (2004). "Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis." Biochemistry 43:1213-1222. Pubmed: 14756557
  • Sandmark, J., Mann, S., Marquet, A., Schneider, G. (2002). "Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin." J Biol Chem 277:43352-43358. Pubmed: 12218056
  • Stoner, G. L., Eisenberg, M. A. (1975). "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 250:4037-4043. Pubmed: 1092682
  • Stoner, G. L., Eisenberg, M. A. (1975). "Purification and properties of 7, 8-diaminopelargonic acid aminotransferase." J Biol Chem 250:4029-4036. Pubmed: 1092681