ID   BIOF1_MYCTO             Reviewed;         386 AA.
AC   P9WQ86; L0TA03; O06621; P0A4X4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=8-amino-7-oxononanoate synthase 1;
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;
GN   Name=bioF1; OrderedLocusNames=MT1620;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45887.1; -; Genomic_DNA.
DR   PIR; C70540; C70540.
DR   RefSeq; WP_003407805.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ86; -.
DR   SMR; P9WQ86; -.
DR   EnsemblBacteria; AAK45887; AAK45887; MT1620.
DR   KEGG; mtc:MT1620; -.
DR   PATRIC; fig|83331.31.peg.1742; -.
DR   HOGENOM; CLU_015846_11_2_11; -.
DR   UniPathway; UPA00078; -.
DR   Proteomes; UP000001020; 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 1"
FT                   /id="PRO_0000426819"
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