ID   BIOF_EXIS2              Reviewed;         390 AA.
AC   B1YMC6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Exig_1033;
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-2008) 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; CP001022; ACB60513.1; -; Genomic_DNA.
DR   RefSeq; WP_012369936.1; NC_010556.1.
DR   AlphaFoldDB; B1YMC6; -.
DR   SMR; B1YMC6; -.
DR   STRING; 262543.Exig_1033; -.
DR   EnsemblBacteria; ACB60513; ACB60513; Exig_1033.
DR   KEGG; esi:Exig_1033; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001681; Chromosome.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; ISS:UniProtKB.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0009102; P:biotin biosynthetic process; ISS:UniProtKB.
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; IPR010962; AONS_Archaea/Firmicutes.
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   TIGRFAMs; TIGR01825; gly_Cac_T_rel; 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..390
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000380991"
FT   BINDING         20
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         179
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..207
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..238
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         238
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  42602 MW;  8A2AE52FAFB53382 CRC64;
     MGFEHLRTEL EEMKQAGTFR ELVALESAQH NRVTVDGKEL IQLSSNNYLG LAAHPRLAKR
     AADAALEFGA GTGSVRTIAG TLEMHQAFER ELATFKHTEA ALVFQSGFAT NLGVLSALLG
     PEDVVISDAL NHASIIDGIR LTKAKRRIYN HVDLADLEAA LQETQDARTR LVVTDGVFSM
     DGNIAPLPEI VELAEKYDAL VMVDDAHASG VLGKSGRGTV NHFGLDGRVA LQVGTLSKAI
     GVLGGYVACE QHVKDYLIHK GRPFLFSTSH PPAVVEANRE ALRVMEEETE LFDRLWENTE
     FFKHGLRELG FNIGTSTTPI TPVIVGDEAL CHQLSDRLRQ HGVFAQGIAF PTVAKGKARV
     RTIVTAEHTR EDLEQALEAF KQVGQELELI