ID   BIOF_GRABC              Reviewed;         382 AA.
AC   Q0BUV6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=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            Short=KAPA synthase;
DE   AltName: Full=8-amino-7-ketopelargonate synthase;
DE   AltName: Full=Alpha-oxoamine synthase;
GN   OrderedLocusNames=GbCGDNIH1_0498;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI61396.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000394; ABI61396.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043453557.1; NC_008343.2.
DR   AlphaFoldDB; Q0BUV6; -.
DR   SMR; Q0BUV6; -.
DR   STRING; 391165.GbCGDNIH1_0498; -.
DR   EnsemblBacteria; ABI61396; ABI61396; GbCGDNIH1_0498.
DR   KEGG; gbe:GbCGDNIH1_0498; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_0_5; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001963; 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; 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   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..382
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381002"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109..110
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
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         233..236
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  40394 MW;  FA6016C0A58FF4AD CRC64;
     MQTLDDFAAR RLSALEKRQL SRVLHETGRD SSPWVMRGER RMLSLSCNDY LNLSTHPATI
     RAAIDATAQF GVGAGGSRLV TGNHPLYTAL EVRLAALKGT EAAIVFGSGF LANIGIIPAL
     IAPNDLILVD ELAHACIHAG AALAHARTIR FPHNDMQALA GLLEQERPQH DHVLIVTDGV
     FSMDGDLAPM SALVELSARY NAWLMTDDAH GIGVLNEGHG SAYGHDVPLQ MGTLSKAVGA
     YGGYLCASAP VVALIRNRAR SFIYTTGLPP GTLAAAITAL DLIAADPALT MQPLEKAKLF
     TRLTSLPDAQ SPIVPILLGS AEAALSASAM LAEHDYLAAA IRPPTVPAGT ARLRLTFTAL
     TPDSDIMRLA ELIRPLLSDT AG