ID   BIOF_ANOFW              Reviewed;         390 AA.
AC   B7GHW7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Aflv_1163;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ33539.1; -; Genomic_DNA.
DR   RefSeq; WP_012574791.1; NC_011567.1.
DR   AlphaFoldDB; B7GHW7; -.
DR   SMR; B7GHW7; -.
DR   STRING; 491915.Aflv_1163; -.
DR   EnsemblBacteria; ACJ33539; ACJ33539; Aflv_1163.
DR   KEGG; afl:Aflv_1163; -.
DR   PATRIC; fig|491915.6.peg.1186; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_9; -.
DR   OMA; HYHASGI; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000742; 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..390
FT                   /note="Putative 8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000380900"
FT   BINDING         20
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         178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..206
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         234..237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43195 MW;  FAA85B3CBEDC5F7E CRC64;
     MLWEELHAHI EQLAEKAQKR TLIQAESDGC FIHIDGRHLL NFSSNNYLGF AHDERLIHAS
     MEATRRYGVG ATASRLVVGN HPLYEQAEDA LVRWKGCEAA LIVNSGYTAN VGILSSLAGR
     DAVIFSDKWN HASIVDGAML SRAEVKRYRH ADVEHLETLL KKAERHKRKI IVTDTIFSMD
     GDVAPLRELV VLKETYGAML VVDEAHASGI YGEKGQGMAH ELQLAQHIDV HMGTFSKALG
     AYGAYVAGKR VVIDYFINTM RPFIFTTALP PSVLGTICTA IEIVQQERSL RHHLHALSDY
     FRTHLQQAGF DIGQSTTHIV PIIVGDNERA LAFSARLRER GIVAVAIRPP TVPDGTARLR
     FSLMATMTKE QLDWAIAEIT AVGKEMGLIA