BIOF_MYCBO
ID BIOF_MYCBO Reviewed; 386 AA.
AC P0A4X5; A0A1R3XYP3; O06621; X2BI87;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BQ2027_MB1596;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCG / Pasteur;
RA Yu S., Jacobs W.R. Jr.;
RT "Cloning, sequencing, and identification of Mycobacterium bovis BCG biotin
RT biosynthetic genes by complementing two Mycobacterium smegmatis biotin
RT mutants.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; AF041819; AAB96957.1; -; Genomic_DNA.
DR EMBL; LT708304; SIU00199.1; -; Genomic_DNA.
DR RefSeq; NP_855248.1; NC_002945.3.
DR RefSeq; WP_003407805.1; NC_002945.4.
DR AlphaFoldDB; P0A4X5; -.
DR SMR; P0A4X5; -.
DR EnsemblBacteria; SIU00199; SIU00199; BQ2027_MB1596.
DR PATRIC; fig|233413.5.peg.1743; -.
DR OMA; MDTHGFG; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001419; 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..386
FT /note="8-amino-7-oxononanoate synthase"
FT /id="PRO_0000163816"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 205..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 236..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 40028 MW; DE2C7D9B3300104F CRC64;
MKAATQARID DSPLAWLDAV QRQRHEAGLR RCLRPRPAVA TELDLASNDY LGLSRHPAVI
DGGVQALRIW GAGATGSRLV TGDTKLHQQF EAELAEFVGA AAGLLFSSGY TANLGAVVGL
SGPGSLLVSD ARSHASLVDA CRLSRARVVV TPHRDVDAVD AALRSRDEQR AVVVTDSVFS
ADGSLAPVRE LLEVCRRHGA LLLVDEAHGL GVRGGGRGLL YELGLAGAPD VVMTTTLSKA
LGSQGGVVLG PTPVRAHLID AARPFIFDTG LAPAAVGAAR AALRVLQAEP WRPQAVLNHA
GELARMCGVA AVPDSAMVSV ILGEPESAVA AAAACLDAGV KVGCFRPPTV PAGTSRLRLT
ARASLNAGEL ELARRVLTDV LAVARR
