ID   BIOF_BACAH              Reviewed;         395 AA.
AC   A0RIB9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BALH_3733;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(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; CP000485; ABK86962.1; -; Genomic_DNA.
DR   RefSeq; WP_001075625.1; NC_008600.1.
DR   AlphaFoldDB; A0RIB9; -.
DR   SMR; A0RIB9; -.
DR   EnsemblBacteria; ABK86962; ABK86962; BALH_3733.
DR   KEGG; btl:BALH_3733; -.
DR   HOGENOM; CLU_015846_11_2_9; -.
DR   OMA; HYHASGI; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000761; 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; Transferase.
FT   CHAIN           1..395
FT                   /note="Putative 8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000380905"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..111
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..210
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         239..242
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         242
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  44126 MW;  09A0262EC8BFABD7 CRC64;
     MNQPWRTHLQ TKLQQLHEQG QYRNLHVTEQ AEETWLIRDE KRMLNLASNN YLGLAGDERL
     KEAAIVCTRK YGTGATASRL VVGNYSLYEE VERSICNWKG TEKALVVNSG FTANVGAISS
     LACRHDIVFS DKLNHASIVD GIILSGAEHK RYRHNDLNHL EVLLKTASPE KRKLIVTDTV
     FSMDGDTAYL RELVQLKEKY GAIIIVDEAH ASGIYGIGGA GLSHIEKDLA QKIDIHMGTF
     SKALGCYGAY LTGDAIYIEY LQNMMRSFIF TTALPPSTLG AVQKAIEIVQ EDHKRRENLI
     ANGEYFRSKL REAGFNIGNS STHIVPIVVG SNENTLRFSK RLQEAGIAAI AIRPPTVPVH
     SSRIRFAVTS QHTIADLKWA IDRITHIAKE EELFV