ID   BIOF2_MYCTO             Reviewed;         771 AA.
AC   P9WQ84; L0T270; P71602; Q7DAK0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Putative 8-amino-7-oxononanoate synthase 2;
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=bioF2; OrderedLocusNames=MT0037;
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   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK44260.1; -; Genomic_DNA.
DR   PIR; F70701; F70701.
DR   RefSeq; WP_003905217.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ84; -.
DR   SMR; P9WQ84; -.
DR   EnsemblBacteria; AAK44260; AAK44260; MT0037.
DR   KEGG; mtc:MT0037; -.
DR   PATRIC; fig|83331.31.peg.37; -.
DR   HOGENOM; CLU_024741_1_0_11; -.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR038740; BioF2-like_GNAT_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF13480; Acetyltransf_6; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..771
FT                   /note="Putative 8-amino-7-oxononanoate synthase 2"
FT                   /id="PRO_0000426820"
FT   REGION          1..418
FT                   /note="Unknown"
FT   REGION          419..771
FT                   /note="KAPA synthase"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         485..486
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         510
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         556
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         581..584
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         615
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   771 AA;  86243 MW;  8FC1D0FED27E43C6 CRC64;
     MPTGLGYDFL RPVEDSGIND LKHYYFMADL ADGQPLGRAN LYSVCFDLAT TDRKLTPAWR
     TTIKRWFPGF MTFRFLECGL LTMVSNPLAL RSDTDLERVL PVLAGQMDQL AHDDGSDFLM
     IRDVDPEHYQ RYLDILRPLG FRPALGFSRV DTTISWSSVE EALGCLSHKR RLPLKTSLEF
     RERFGIEVEE LDEYAEHAPV LARLWRNVKT EAKDYQREDL NPEFFAACSR HLHGRSRLWL
     FRYQGTPIAF FLNVWGADEN YILLEWGIDR DFEHYRKANL YRAALMLSLK DAISRDKRRM
     EMGITNYFTK LRIPGARVIP TIYFLRHSTD PVHTATLARM MMHNIQRPTL PDDMSEEFCR
     WEERIRLDQD GLPEHDIFRK IDRQHKYTGL KLGGVYGFYP RFTGPQRSTV KAAELGEIVL
     LGTNSYLGLA THPEVVEASA EATRRYGTGC SGSPLLNGTL DLHVSLEQEL ACFLGKPAAV
     LCSTGYQSNL AAISALCESG DMIIQDALNH RSLFDAARLS GADFTLYRHN DMDHLARVLR
     RTEGRRRIIV VDAVFSMEGT VADLATIAEL ADRHGCRVYV DESHALGVLG PDGRGASAAL
     GVLARMDVVM GTFSKSFASV GGFIAGDRPV VDYIRHNGSG HVFSASLPPA AAAATHAALR
     VSRREPDRRA RVLAAAEYMA TGLARQGYQA EYHGTAIVPV ILGNPTVAHA GYLRLMRSGV
     YVNPVAPPAV PEERSGFRTS YLADHRQSDL DRALHVFAGL AEDLTPQGAA L