ID   BIOF_CHLP8              Reviewed;         392 AA.
AC   B3QLR6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 69.
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=Cpar_2015;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACF12402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001099; ACF12402.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041466197.1; NC_011027.1.
DR   AlphaFoldDB; B3QLR6; -.
DR   SMR; B3QLR6; -.
DR   STRING; 517417.Cpar_2015; -.
DR   EnsemblBacteria; ACF12402; ACF12402; Cpar_2015.
DR   KEGG; cpc:Cpar_2015; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_10; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000008811; 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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase; Biotin biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..392
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000380952"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..115
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         212..215
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         243..246
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  42903 MW;  1CECC6D34E3A9E44 CRC64;
     MPIEEHIARE QERLRAKQRY RTLPETGARR GPYITVGGRE LLNLSSNDYL GLGSEPKLLA
     SWMAQVECGG ADGRFAMTSS SSRLLTGNFP VGGELESAIA KAYGSEAALV FNSGYHANTG
     ILPSLSTRHD LILSDRLNHA SIIDGLRIAE AEYRRYRHAD YDHLEELLAS AAGKYRQVFI
     VTESVFSMDG DLADLRRLVD LKKRYGAMLI VDEAHGVGVY GQRGLGLCEA LGVLENIDIL
     IGTFGKALAS TGAYAVMSGL FREYLVNTMR TLIFTTALPP MMLSWSLATF TRQLEMRRER
     EHLLGLAARL RETLGDAGFE TPGESHIVPV VLGEDRAAVA MAAALREAGY HALPVRPPTV
     PENSARLRLS LRADLAVEQI DALASTMQSL RS