ID   KASB_MYCTO              Reviewed;         417 AA.
AC   P9WQD6; L0TBY1; P63456; Q10525;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE            EC=2.3.1.294 {ECO:0000250|UniProtKB:P9WQD7};
DE   AltName: Full=Beta-ketoacyl-ACP synthase 2;
DE            Short=KAS 2;
GN   Name=kasB; OrderedLocusNames=MT2306;
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: 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 extension of
CC       the mycolate chains to full lengths and produces longer chain
CC       multiunsaturated hydrocarbons averaging 54 carbons in length.
CC       {ECO:0000250|UniProtKB:P9WQD7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an ultra-long-chain di-unsaturated fatty acyl-[ACP] + H(+) +
CC         malonyl-[ACP] = a 3-oxo-ultra-long-chain di-unsaturated fatty acyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:65308, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16767, Rhea:RHEA-COMP:16774,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:156401, ChEBI:CHEBI:156402;
CC         EC=2.3.1.294; Evidence={ECO:0000250|UniProtKB:P9WQD7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65309;
CC         Evidence={ECO:0000250|UniProtKB:P9WQD7};
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQD7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WQD7}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK46590.1; -; Genomic_DNA.
DR   PIR; B70779; B70779.
DR   RefSeq; WP_003411576.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQD6; -.
DR   SMR; P9WQD6; -.
DR   EnsemblBacteria; AAK46590; AAK46590; MT2306.
DR   GeneID; 45426226; -.
DR   KEGG; mtc:MT2306; -.
DR   HOGENOM; CLU_000022_69_2_11; -.
DR   UniPathway; UPA00915; -.
DR   PHI-base; PHI:4196; -.
DR   Proteomes; UP000001020; 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..417
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT                   /id="PRO_0000426794"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000250|UniProtKB:P9WQD9"
SQ   SEQUENCE   417 AA;  44277 MW;  239F7D19A6380F66 CRC64;
     MTELVTGKAF PYVVVTGIAM TTALATDAET TWKLLLDRQS GIRTLDDPFV EEFDLPVRIG
     GHLLEEFDHQ LTRIELRRMG YLQRMSTVLS RRLWENAGSP EVDTNRLMVS IGTGLGSAEE
     LVFSYDDMRA RGMKAVSPLT VQKYMPNGAA AAVGLERHAK AGVMTPVSAC ASGAEAIARA
     WQQIVLGEAD AAICGGVETR IEAVPIAGFA QMRIVMSTNN DDPAGACRPF DRDRDGFVFG
     EGGALLLIET EEHAKARGAN ILARIMGASI TSDGFHMVAP DPNGERAGHA ITRAIQLAGL
     APGDIDHVNA HATGTQVGDL AEGRAINNAL GGNRPAVYAP KSALGHSVGA VGAVESILTV
     LALRDQVIPP TLNLVNLDPE IDLDVVAGEP RPGNYRYAIN NSFGFGGHNV AIAFGRY