BIOF_MYCA1
ID BIOF_MYCA1 Reviewed; 381 AA.
AC A0QHJ9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=MAV_3205;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) 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; CP000479; ABK65140.1; -; Genomic_DNA.
DR RefSeq; WP_011725323.1; NC_008595.1.
DR AlphaFoldDB; A0QHJ9; -.
DR SMR; A0QHJ9; -.
DR EnsemblBacteria; ABK65140; ABK65140; MAV_3205.
DR KEGG; mav:MAV_3205; -.
DR HOGENOM; CLU_015846_11_2_11; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001574; 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; Transferase.
FT CHAIN 1..381
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000381033"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 201..204
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 381 AA; 39376 MW; F615222D4D079E61 CRC64;
MKAPIEVSPL AWLDAVEQQR RAAGLRRSLR PRPPVATELD LASNDYLGLS QHPDVIDGGV
AALRLWGAGA TGSRLVTGDT ELHQQFESEL ADYVGAASGL LFSSGYAANL GAVVGLSGRG
ALVVSDAYSH ASLVDACRLS RARVVVTPHR DVDAVLAALA DRDEERAVVI TESVFSTDGA
LAPLRELHEV CRRHRALLIV DEAHGLGVRG GGRGLVFEAG LAGAPDVVMT TTLSKALGSQ
GGAVLGPAAV RAHLIDAART FIFDTGLAPA AVGAARAALG VLRAEPWRVG AVLRHAGVLA
EVCRVREVPQ SAVVSVILGD PDVAVAAATA CLDAGVRVGC FRPPTVPAGT SRLRLTARAS
LDDAELEVAR RVLTDVLAGL G
