ID   BIOF1_BACVZ             Reviewed;         391 AA.
AC   A7Z4X1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=8-amino-7-oxononanoate synthase 1;
DE            Short=AONS;
DE            EC=2.3.1.47;
DE   AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE            Short=7-KAP synthase;
DE            Short=KAPA synthase;
DE   AltName: Full=8-amino-7-ketopelargonate synthase;
DE   AltName: Full=Alpha-oxoamine synthase;
GN   OrderedLocusNames=RBAM_016840;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
CC   -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC       carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC       [acyl-carrier protein], and carbon dioxide. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC         oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC         ChEBI:CHEBI:149468; EC=2.3.1.47;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. BioF subfamily. {ECO:0000305}.
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DR   EMBL; CP000560; ABS74047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7Z4X1; -.
DR   SMR; A7Z4X1; -.
DR   STRING; 326423.RBAM_016840; -.
DR   EnsemblBacteria; ABS74047; ABS74047; RBAM_016840.
DR   KEGG; bay:RBAM_016840; -.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001120; Chromosome.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; ISS:UniProtKB.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0009102; P:biotin biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR010962; AONS_Archaea/Firmicutes.
DR   InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00858; bioF; 1.
DR   TIGRFAMs; TIGR01825; gly_Cac_T_rel; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..391
FT                   /note="8-amino-7-oxononanoate synthase 1"
FT                   /id="PRO_0000380903"
FT   BINDING         108..109
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..208
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..239
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  43176 MW;  B0A106263B61C6C0 CRC64;
     MKEFEFLKAE LDKMKENKTW QQMKQIETKQ GPSVEVKGEN VIQLSSNNYL GLTSHPRLVE
     AAKRAAEEFG AGTGSVRTIA GTFTMHNELE KKLANFKKTE AALVFQSGFT TNQGVLSSIL
     TKEDIVISDE LNHASIIDGI RLTKADKKVY RHVDMDDLER VLKKSMNYRM RLIVTDGVFS
     MDGNIAPLPD IVKLAEAYDA FVMVDDAHAS GVLGKNGRGT VNHFGLDGRV HIQVGTLSKA
     IGVLGGYAAG SQVLIDYLRH KGRPFLFSTS HPPAVTAACI EAIDVLLEEP EHMEKLWENT
     AYFKDKLVQM GLTLTKSETP IVPILIGEEE KAQALSDLLL TRGVFAQSIV YPTVAQGKAR
     IRTIITAEHT NEELDRALEV IRSAAKELQL V