ID   BIOF_NEIG1              Reviewed;         380 AA.
AC   Q5F6R6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative 8-amino-7-oxononanoate synthase;
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   AltName: Full=8-amino-7-ketopelargonate synthase;
GN   Name=bioF; OrderedLocusNames=NGO1483;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW90121.1; -; Genomic_DNA.
DR   RefSeq; WP_010951279.1; NC_002946.2.
DR   RefSeq; YP_208533.1; NC_002946.2.
DR   AlphaFoldDB; Q5F6R6; -.
DR   SMR; Q5F6R6; -.
DR   STRING; 242231.NGO_1483; -.
DR   EnsemblBacteria; AAW90121; AAW90121; NGO_1483.
DR   KEGG; ngo:NGO_1483; -.
DR   PATRIC; fig|242231.10.peg.1755; -.
DR   HOGENOM; CLU_015846_11_2_4; -.
DR   OMA; HYHASGI; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000535; Chromosome.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..380
FT                   /note="Putative 8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381048"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
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         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  43100 MW;  671FD34280960094 CRC64;
     MKVFRQQLEQ LGAQNQYRSI PDLIHQGRYI TRENRKMLNM SSNDYLGLAS DENLRRSFLQ
     QYGGNFPSFT SSSSRLLTGN FPIYTDLEEL VAQRFQRESA LLFNSGYHAN LGILPALTTT
     KSLILADKFV HASMIDGIRL SRCAFFRYRH NDYEHLKNLL EKNVGKFDRT FIVTESVFSM
     DGDVADLKQL VQLKKQFPNT YLYVDEAHAI GVYGQNGLGI AERDNLIAEI DLLVGTFGKA
     LASVGAYAVC NQVLKECLIN QMRPLIFSTA LPPFNVAWTY FIFERLPQFS KERSHLEQLS
     AFLRREVAHR TQIMPSETCI VPYILGGNEA TLAKAEYLQG QGYYCLPIGP PTVPKNTSRI
     RLSLTADMTT DEVRQFAACL