ID   KASA_MYCTE              Reviewed;         416 AA.
AC   H8ESN0;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 2.
DT   03-AUG-2022, entry version 44.
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=ERDMAN_2470;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA   Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT   "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT   three anti-sigma factor substrates.";
RL   Mol. Microbiol. 77:605-617(2010).
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   -!- INDUCTION: Repressed by Rip1 and independently by the metal chelator
CC       phenanthroline. {ECO:0000269|PubMed:20545848}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AP012340; BAL66261.1; -; Genomic_DNA.
DR   RefSeq; WP_003411571.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8ESN0; -.
DR   SMR; H8ESN0; -.
DR   EnsemblBacteria; BAL66261; BAL66261; ERDMAN_2470.
DR   GeneID; 45426225; -.
DR   KEGG; mtn:ERDMAN_2470; -.
DR   PATRIC; fig|652616.3.peg.2513; -.
DR   HOGENOM; CLU_000022_69_2_11; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000007568; 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   2: Evidence at transcript level;
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_0000422686"
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