ID   BIOF_METC4              Reviewed;         383 AA.
AC   B7L0L2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Mchl_0816;
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688;
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., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-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; CP001298; ACK81735.1; -; Genomic_DNA.
DR   RefSeq; WP_012605834.1; NC_011757.1.
DR   AlphaFoldDB; B7L0L2; -.
DR   SMR; B7L0L2; -.
DR   EnsemblBacteria; ACK81735; ACK81735; Mchl_0816.
DR   KEGG; mch:Mchl_0816; -.
DR   HOGENOM; CLU_015846_11_2_5; -.
DR   OMA; HYHASGI; -.
DR   BioCyc; MEXT440085:MCHL_RS03935-MON; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000002385; 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..383
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381021"
FT   BINDING         27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
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         232..235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  39617 MW;  6588FF5E89226553 CRC64;
     MSPNPSNSLD AFAGEKLAGL EASALRRRLA VTARGPEAAA ERGGRSLVSF SCNDYLGLAH
     DPRVIAAATE ALARYGAGAG ASRLVTGNSP PLAALEERLA RHKGKEAALV FGSGYLANLG
     IAPALVGAGD LILIDELGHS CLFAGAAMSR AQTVRFAHND VAQLRALLAE HRGTARRALI
     LTERVFSMDG DRAPLPEILA LAGEYDAWTL VDDAHGLGVV EPGQRAPLEM GTLSKTLGSY
     GGYLCASQPV IDLLTSRARS LVYTTGLPPA SAAAALKALD IVETEPERAA RPLALARRFT
     ARLGLPEAMS PIVPVLIGAA EAALALSTAL EARGFLVVAI RPPTVAPGTA RLRVAFSAAH
     DEGQVDALAE ALIELAPESV RAG