BIOF_MYCLE
ID BIOF_MYCLE Reviewed; 385 AA.
AC P45487;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=ML1217; ORFNames=B1170_C2_196;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00010; AAA17066.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31598.1; -; Genomic_DNA.
DR PIR; S72702; S72702.
DR RefSeq; NP_301881.1; NC_002677.1.
DR RefSeq; WP_010908202.1; NC_002677.1.
DR AlphaFoldDB; P45487; -.
DR SMR; P45487; -.
DR STRING; 272631.ML1217; -.
DR EnsemblBacteria; CAC31598; CAC31598; CAC31598.
DR KEGG; mle:ML1217; -.
DR PATRIC; fig|272631.5.peg.2236; -.
DR Leproma; ML1217; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_2_11; -.
DR OMA; MDTHGFG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000000806; 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;
KW Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000163817"
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 385 AA; 39831 MW; 0CA37DD1FACC44AA CRC64;
MKVPIETSPL AWLEAVEQQR RGAGLRRSLR PRSAVATELD LASNDYLGLS QHPDVIDGGV
AALRVWGAGA TGSRLVTGDT ILHHELECEL AEFVGACVGL LFSSGYAANL GAVVGLSGPG
SLIVSDAYSH ASLVDACRLS RARVVVTPHC DVDAVDTALR SCHEERAVVV TESVFSADGV
LAPVSELHDV CRRHGALLLV DEAHGLGVRG GGRGLVYEVG LAGAPDVVIT TTMSKALGSQ
GGAVLGSSAV RAHLINTARP FIFDTGLAPA AVGAARAALQ ILKAETWRPE AVLQHARTLA
KICDLSELPQ SAVVSVVLGD PEVALAAAIA CLDAGVRVGC FRPPTVPAGT SRLRLTAHAS
LDSAKLEVAR RVLTDVLGGC CVARR
