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BIOF_MYCGI
ID   BIOF_MYCGI              Reviewed;         380 AA.
AC   A4T9L3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Mflv_3628;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) 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; CP000656; ABP46102.1; -; Genomic_DNA.
DR   RefSeq; WP_011894485.1; NC_009338.1.
DR   AlphaFoldDB; A4T9L3; -.
DR   SMR; A4T9L3; -.
DR   STRING; 350054.Mflv_3628; -.
DR   EnsemblBacteria; ABP46102; ABP46102; Mflv_3628.
DR   KEGG; mgi:Mflv_3628; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_2_11; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; 479874at2; -.
DR   UniPathway; UPA00078; -.
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; Transferase.
FT   CHAIN           1..380
FT                   /note="8-amino-7-oxononanoate synthase"
FT                   /id="PRO_0000381035"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..105
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..203
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         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  39420 MW;  C4C081B31E7BEB25 CRC64;
     MTRAGLSPLA WLDEVETQRR AAGLRRSLRA RPPVGTVLDL ASNDYLGLSQ HPRVIDGGVA
     ALRTWGAGAT GSRLVTGNTE LHEQFEDALA SFVGADSALV FSSGYTANLG AVVALSGPGS
     LLVSDAYTHA SLVDACRLSR ARVVVTPHND VAAVARALAT RDEERAVVVT DSVFSADGDL
     APLRELHDAC RRHGALMIVD EAHGLGVRGD RGRGLLDEVG LAGAPDVVMT TTLSKALGSQ
     GGVVLGPAAV RDHLIDAARP FIFDTGLAPA AVGAAHAALQ VLVEEPWRAQ RVLDHATTLA
     QICGVADVPS SAVVSVILGE PEVALAAAMG CLERGVRVGC FRPPTVPAGT SRLRLTARAS
     LSDDEMALAR EVLTDVLSRA
 
 
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