ID   BIOF_PASMU              Reviewed;         387 AA.
AC   Q9CJU0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=PM1901;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03985.1; -; Genomic_DNA.
DR   RefSeq; WP_005724990.1; NC_002663.1.
DR   AlphaFoldDB; Q9CJU0; -.
DR   SMR; Q9CJU0; -.
DR   STRING; 747.DR93_33; -.
DR   EnsemblBacteria; AAK03985; AAK03985; PM1901.
DR   KEGG; pmu:PM1901; -.
DR   PATRIC; fig|272843.6.peg.1923; -.
DR   HOGENOM; CLU_015846_11_2_6; -.
DR   OMA; YPYFRPI; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000000809; 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..387
FT                   /note="Putative 8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381060"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..108
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
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         206..209
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         237..240
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   387 AA;  43837 MW;  692F648BB785F5AF CRC64;
     MIRYYQQQLA DLKAQNQFRQ LPQLIHRGRF IQREDNTMLN MSSNDYLGLA NNEALRQAFF
     TQYQDQLPAL TSSSSRLLTG SFPIYDELES LMAQAFGRET ALLFNSGYHA NIGILPALAD
     KKTLIVADKL VHASMIDGIR LAQCEFVRFR HHDYAHLEQI LQKNDRTFER IIVVTESVFS
     MDGDCADLTQ LVALKQRYPQ VMLYVDEAHA IGVLGEKGLG LAEQQGCINQ IDILVGTFGK
     ALGSMGAYVI CDQVIRDYLV NKMRPLIFST ALPPFNVAWT HFVFQQLPHL QAERAHLAQL
     SQHLRQAIVD IFQVPMPSES CIVPYILGDN ELTVRTAQRL QQQGYYCLPI RPPTVPKGTS
     RIRFSLTADM QVAEVEQFIA CLQELAE