ID   KASA_MYCBO              Reviewed;         416 AA.
AC   P63455; A0A1R3Y0P3; Q10524; X2BKI6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1;
DE            EC=2.3.1.293 {ECO:0000250|UniProtKB:P9WQD9};
DE   AltName: Full=Beta-ketoacyl-ACP synthase 1;
DE            Short=KAS 1;
GN   Name=kasA; OrderedLocusNames=BQ2027_MB2269;
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 [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   [2]
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: Part of the mycobacterial fatty acid elongation system FAS-
CC       II, which is involved in mycolic acid biosynthesis. Catalyzes the
CC       elongation of long chain acyl-ACP substrates by the addition of two
CC       carbons from malonyl-ACP to an acyl acceptor. Involved in the initial
CC       extension of the mycolate chain and forms monounsaturated fatty acids
CC       that averaged 40 carbons in length. {ECO:0000250|UniProtKB:P9WQD9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an ultra-long-chain mono-unsaturated fatty acyl-[ACP] + H(+) +
CC         malonyl-[ACP] = a 3-oxo-ultra-long-chain mono-unsaturated fatty acyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:65312, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16765, Rhea:RHEA-COMP:16775,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:156399, ChEBI:CHEBI:156400;
CC         EC=2.3.1.293; Evidence={ECO:0000250|UniProtKB:P9WQD9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65313;
CC         Evidence={ECO:0000250|UniProtKB:P9WQD9};
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQD9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WQD9}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00880.1; -; Genomic_DNA.
DR   RefSeq; NP_855918.1; NC_002945.3.
DR   RefSeq; WP_003411571.1; NC_002945.4.
DR   AlphaFoldDB; P63455; -.
DR   SMR; P63455; -.
DR   EnsemblBacteria; SIU00880; SIU00880; BQ2027_MB2269.
DR   GeneID; 45426225; -.
DR   PATRIC; fig|233413.5.peg.2490; -.
DR   OMA; YAYLSMQ; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712; PTHR11712; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Transferase.
FT   CHAIN           1..416
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT                   /id="PRO_0000180329"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD9"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD9"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD9"
SQ   SEQUENCE   416 AA;  43316 MW;  D2187BE2F0B56C7F CRC64;
     MSQPSTANGG FPSVVVTAVT ATTSISPDIE STWKGLLAGE SGIHALEDEF VTKWDLAVKI
     GGHLKDPVDS HMGRLDMRRM SYVQRMGKLL GGQLWESAGS PEVDPDRFAV VVGTGLGGAE
     RIVESYDLMN AGGPRKVSPL AVQMIMPNGA AAVIGLQLGA RAGVMTPVSA CSSGSEAIAH
     AWRQIVMGDA DVAVCGGVEG PIEALPIAAF SMMRAMSTRN DEPERASRPF DKDRDGFVFG
     EAGALMLIET EEHAKARGAK PLARLLGAGI TSDAFHMVAP AADGVRAGRA MTRSLELAGL
     SPADIDHVNA HGTATPIGDA AEANAIRVAG CDQAAVYAPK SALGHSIGAV GALESVLTVL
     TLRDGVIPPT LNYETPDPEI DLDVVAGEPR YGDYRYAVNN SFGFGGHNVA LAFGRY