8-amino-7-oxononanoate synthase (P12998)

Identification
Name:8-amino-7-oxononanoate synthase
Synonyms:
  • AONS
  • 7-keto-8-amino-pelargonic acid synthase
  • 7-KAP synthase
  • KAPA synthase
  • 8-amino-7-ketopelargonate synthase
  • L-alanine--pimeloyl-CoA ligase
Gene Name:bioF
Enzyme Class:
Biological Properties
General Function:Involved in 8-amino-7-oxononanoate synthase activity
Specific Function:Catalyzes the decarboxylative condensation of pimeloyl- CoA and L-alanine to produce 8-amino-7-oxononanoate (AON), coenzyme A, and carbon dioxide
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.06-Carboxyhexanoyl-CoA+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Acyl-carrier protein
1.06-Carboxyhexanoyl-CoA + 1.0L-Alanine + 1.0Pimeloyl-[acyl-carrier protein] ↔ 1.08-Amino-7-oxononanoate + 1.0Coenzyme A + 1.0Carbon dioxide + 1.0Acyl-carrier protein
ReactionCard
SMPDB Reactions:
1.0a pimeloyl-[acp]+1.0L-Alanine+1.0Thumb → 1.0Thumb+1.0a holo-[acyl-carrier protein]+1.0Thumb
1.0a pimeloyl-[acp] + 1.0L-Alanine + 1.0L-Alanine → 1.0Carbon dioxide + 1.0a holo-[acyl-carrier protein] + 1.08-Amino-7-oxononanoate
ReactionCard
1.0Thumb+1.0L-Alanine+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0a sulfurated [sulfur carrier] + 1.0L-Alanine + 1.0L-Alanine → 1.08-Amino-7-oxononanoate + 1.0Coenzyme A + 1.0Carbon dioxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Pimeloyl-[acyl-carrier protein] → 1.0Thumb+1.0acyl carrier protein+1.0Thumb
1.0L-Alanine + 1.0Pimeloyl-[acyl-carrier protein] → 1.08-Amino-7-oxononanoate + 1.0acyl carrier protein + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB201118-Amino-7-oxononanoateMetaboCard
ECMDB24186a sulfurated [sulfur carrier]MetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB23803Pimeloyl-[acyl-carrier protein]MetaboCard
GO Classification:
Function
8-amino-7-oxononanoate synthase activity
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
transferase activity, transferring nitrogenous groups
Process
biosynthetic process
biotin biosynthetic process
biotin metabolic process
metabolic process
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b0776
Gene OrientationClockwise
Centisome Percentage:17.45
Left Sequence End809604
Right Sequence End810758
Gene Sequence:
>1155 bp
ATGCTGCTGGTACTGGTGCTGATTGGTCTTAATATGCGACCACTGCTCACCTCCGTCGGG
CCACTGCTACCGCAATTGCGCCAGGCGAGCGGAATGAGCTTTAGCGTGGCTGCCCTGTTG
ACCGCTCTGCCGGTGGTTACCATGGGCGGGCTGGCGCTGGCCGGAAGCTGGCTTCATCAG
CATGTCAGCGAACGTCGCAGTGTCGCCATCAGTCTGTTGCTGATTGCCGTCGGTGCATTG
ATGCGTGAGCTTTACCCGCAAAGTGCGCTGCTGCTTAGCAGCGCACTGCTTGGTGGGGTG
GGGATCGGCATCATTCAGGCGGTGATGCCTTCGGTGATTAAACGGCGGTTTCAGCAGCGC
ACGCCACTGGTGATGGGGCTGTGGTCCGCGGCTCTGATGGGCGGCGGTGGGCTTGGTGCC
GCCATAACGCCCTGGTTAGTTCAACATAGCGAAACCTGGTATCAAACACTCGCCTGGTGG
GCGCTGCCTGCCGTTGTTGCGCTCTTTGCCTGGTGGTGGCAAAGCGCCCGCGAGGTCGCC
TCTTCCCACAAGACAACAACCACTCCGGTTCGCGTGGTATTCACTCCCCGCGCGTGGACG
CTGGGTGTTTACTTCGGTCTGATTAACGGCGGTTACGCCAGCCTGATTGCCTGGTTACCC
GCTTTCTATATTGAGATTGGTGCCAGCGCGCAGTACAGCGGTTCCTTACTGGCATTGATG
ACGCTTGGGCAAGCCGCAGGAGCTTTGCTGATGCCTGCTATGGCTCGCCATCAGGATCGG
CGCAAACTGTTAATGCTGGCGCTGGTGTTACAACTGGTGGGGTTCTGCGGCTTTATCTGG
CTGCCGATGCAATTGCCGGTATTGTGGGCGATGGTGTGTGGGTTAGGTCTGGGCGGCGCG
TTTCCGCTCTGTTTGCTGCTGGCGCTCGATCACTCTGTGCAACCGGCTATTGCTGGCAAG
CTGGTGGCGTTTATGCAGGGAATCGGTTTTATCATCGCCGGGCTTGCCCCGTGGTTTTCT
GGCGTGCTGCGTAGTATCAGCGGCAATTACCTGATGGACTGGGCATTTCATGCGCTGTGC
GTCGTTGGGCTGATGATCATAACCCTGCGTTTTGCACCAGTACGTTTTCCGCAGCTGTGG
GTCAAAGAGGCATGA
Protein Properties
Pfam Domain Function:
Protein Residues:384
Protein Molecular Weight:41594
Protein Theoretical pI:7
PDB File:1BS0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>8-amino-7-oxononanoate synthase
MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIR
AWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMM
AKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSM
DGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGV
SGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALIT
RFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARL
RLTLTAAHEMQDIDRLLEVLHGNG
References
External Links:
ResourceLink
Uniprot ID:P12998
Uniprot Name:BIOF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674483
PDB ID:1BS0
Ecogene ID:EG10121
Ecocyc:EG10121
ColiBase:b0776
Kegg Gene:b0776
EchoBASE ID:EB0119
CCDB:BIOF_ECOLI
BacMap:16128744
General Reference:
  • Alexeev, D., Alexeeva, M., Baxter, R. L., Campopiano, D. J., Webster, S. P., Sawyer, L. (1998). "The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme." J Mol Biol 284:401-419. Pubmed: 9813126
  • Alexeev, D., Baxter, R. L., Campopiano, D. J., Kerbarh, O., Sawyer, L., Tomczyk, N., Watt, R., Webster, S. P. (2006). "Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine." Org Biomol Chem 4:1209-1212. Pubmed: 16557306
  • 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
  • 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
  • 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
  • Ploux, O., Breyne, O., Carillon, S., Marquet, A. (1999). "Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies." Eur J Biochem 259:63-70. Pubmed: 9914476
  • Webster, S. P., Alexeev, D., Campopiano, D. J., Watt, R. M., Alexeeva, M., Sawyer, L., Baxter, R. L. (2000). "Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies." Biochemistry 39:516-528. Pubmed: 10642176