8-amino-7-oxononanoate synthase
Details
- Name
- 8-amino-7-oxononanoate synthase
- Synonyms
- 2.3.1.47
- 7-KAP synthase
- 7-keto-8-amino-pelargonic acid synthase
- 8-amino-7-ketopelargonate synthase
- AONS
- KAPA synthase
- Gene Name
- bioF
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016558|8-amino-7-oxononanoate synthase MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIR AWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMM AKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSM DGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGV SGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALIT RFRAGVQDLPFTLADSCSAIQPLIVGDNSRALQLAEKLRQQGCWVTAIRPPTVPAGTARL RLTLTAAHEMQDIDRLLEVLHGNG
- Number of residues
- 384
- Molecular Weight
- 41593.855
- Theoretical pI
- 7.14
- GO Classification
- Functions8-amino-7-oxononanoate synthase activity / pyridoxal phosphate bindingProcessesbiotin biosynthetic process
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl-ACP rather than pimeloyl-CoA is the physiological substrate of BioF.
- Pfam Domain Function
- Aminotran_1_2 (PF00155)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016559|8-amino-7-oxononanoate synthase (bioF) ATGAGCTGGCAGGAGAAAATCAACGCGGCGCTCGATGCGCGGCGTGCTGCCGATGCCCTG CGTCGCCGTTATCCGGTGGCGCAAGGAGCCGGACGCTGGCTGGTGGCGGATGATCGCCAG TATCTGAACTTTTCCAGTAACGATTATTTAGGTTTAAGCCATCATCCGCAAATTATCCGT GCCTGGCAGCAGGGGGCGGAGCAATTTGGCATCGGTAGCGGCGGCTCCGGTCACGTCAGC GGTTATAGCGTGGTGCATCAGGCACTGGAAGAAGAGCTGGCCGAGTGGCTTGGCTATTCG CGGGCACTGCTGTTTATCTCTGGTTTCGCCGCTAATCAGGCAGTTATTGCCGCGATGATG GCGAAAGAGGACCGTATTGCTGCCGACCGGCTTAGCCATGCCTCATTGCTGGAAGCTGCC AGTTTAAGCCCGTCGCAGCTTCGCCGTTTTGCTCATAACGATGTCACTCATTTGGCGCGA TTGCTTGCTTCCCCCTGTCCGGGGCAGCAAATGGTGGTGACAGAAGGCGTGTTCAGCATG GACGGCGATAGTGCGCCACTGGCGGAAATCCAGCAGGTAACGCAACAGCACAATGGCTGG TTGATGGTCGATGATGCCCACGGCACGGGCGTTATCGGGGAGCAGGGGCGCGGCAGCTGC TGGCTGCAAAAGGTAAAACCAGAATTGCTGGTAGTGACTTTTGGCAAAGGATTTGGCGTC AGCGGGGCAGCGGTGCTTTGCTCCAGTACGGTGGCGGATTATCTGCTGCAATTCGCCCGC CACCTTATCTACAGCACCAGTATGCCGCCCGCTCAGGCGCAGGCATTACGTGCGTCGCTG GCGGTCATTCGCAGTGATGAGGGTGATGCACGGCGCGAAAAACTGGCGGCACTCATTACG CGTTTTCGTGCCGGAGTACAGGATTTGCCGTTTACGCTTGCTGATTCATGCAGCGCCATC CAGCCATTGATTGTCGGTGATAACAGCCGTGCGTTACAACTGGCAGAAAAACTGCGTCAG CAAGGCTGCTGGGTCACGGCGATTCGCCCGCCAACCGTACCCGCTGGTACTGCGCGACTG CGCTTAACGCTAACCGCTGCGCATGAAATGCAGGATATCGACCGTCTGCTGGAGGTGCTG CATGGCAACGGTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P12998 UniProtKB Entry Name BIOF_ECOLI 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]
- Webster SP, Alexeev D, Campopiano DJ, Watt RM, Alexeeva M, Sawyer L, Baxter RL: Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry. 2000 Jan 25;39(3):516-28. [Article]
- Ploux O, Breyne O, Carillon S, Marquet A: 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. 1999 Jan;259(1-2):63-70. [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]
- Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L: The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J Mol Biol. 1998 Nov 27;284(2):401-19. [Article]
- Alexeev D, Baxter RL, Campopiano DJ, Kerbarh O, Sawyer L, Tomczyk N, Watt R, Webster SP: Suicide inhibition of alpha-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine. Org Biomol Chem. 2006 Apr 7;4(7):1209-12. Epub 2006 Mar 1. [Article]