ID   KASB_MYCLE              Reviewed;         420 AA.
AC   O69473;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   24-JAN-2024, entry version 120.
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=ML1656; ORFNames=MLCB1243.19c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC30607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL023635; CAA19200.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL583922; CAC30607.1; ALT_INIT; Genomic_DNA.
DR   PIR; T44710; T44710.
DR   AlphaFoldDB; O69473; -.
DR   SMR; O69473; -.
DR   STRING; 272631.gene:17575499; -.
DR   KEGG; mle:ML1656; -.
DR   Leproma; ML1656; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_11; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000000806; 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:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..420
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT                   /id="PRO_0000180332"
FT   DOMAIN          13..419
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        173
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        314
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        349
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
SQ   SEQUENCE   420 AA;  44497 MW;  C015CF9CC5DC7E72 CRC64;
     MTTSPELVTG KAFPNVVVTG IAMTTALATD AETTWKLLLD NQSGIRMLDD PFIEEFNLPV
     RIGGHLLEEF DHQLTRVELR RMGYLQRMST VLSRRLWENA GSPEVDTNRL MVSIGTGLGS
     AEELVFSYDD MRARGMKAVS PLAVQKYMPN GAAAAVGLEH HAKAGVMTPV SACASGSEAI
     AHAWQQIVLG EADSAICGGV ETKIEAVPIA GFSQMRIVMS TKNDNPAGAC RPFDRDRDGF
     VFGEAGALML IETEDSAKAR SANILARIMG ASITSDGFHM VAPDPNGERA GHAIARAVHL
     AGLSPSDIDH VNAHATGTQV GDLAEAKAIN KALCNNRPAV YAPKSALGHS VGAVGAVESI
     LTVLALRDQV IPPTLNLVNL DPDIDLDVVA GKPRPGDYRY AVNNSFGFGG HNVAIAFGCY
//