KASA_MYCLE
ID KASA_MYCLE Reviewed; 416 AA.
AC Q9CBS7; O69474;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=ML1655; ORFNames=MLCB1243.20c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; 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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19201.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL023635; CAA19201.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583922; CAC30606.1; -; Genomic_DNA.
DR PIR; A87116; A87116.
DR PIR; T44711; T44711.
DR RefSeq; NP_302136.1; NC_002677.1.
DR RefSeq; WP_010908457.1; NC_002677.1.
DR AlphaFoldDB; Q9CBS7; -.
DR SMR; Q9CBS7; -.
DR STRING; 272631.ML1655; -.
DR EnsemblBacteria; CAC30606; CAC30606; CAC30606.
DR KEGG; mle:ML1655; -.
DR PATRIC; fig|272631.5.peg.3122; -.
DR Leproma; ML1655; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_11; -.
DR OMA; YAYLSMQ; -.
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; 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; Reference proteome; Transferase.
FT CHAIN 1..416
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000180331"
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; 43470 MW; F90F8210F022F4FC CRC64;
MTMPSTANGG FPSVVVTAVT ATTSISPDIE STWKGLLAGE SGIHVLEDEY ITKWDLPVKI
GGHLKEPVDS HMSRLDLRRM SYVQRMSKLL SGRLWESTGS PEVDPDRFTV VVGTGLGGAE
RIVESYDLMN AGGPRKVSPL AVQMIMPNGA AATVGLQLGA CAGVMTPVSA CSSGSEAIAH
AWRQIIMGDA DVAVCGGVEG PIEALPIAAF SMMRAMSTRN DDPEGASRPF DKNRDGFVFG
EAGALMLIET EEHAKARGAK PLARLLGAGI TSDAFHMVAP AADGVRAGRA MTRSLELAGL
SAKDVDHVNA HGTATPIGDS AEANAIRVAG CEQAAVYAPK SALGHSIGAV GALESVLTVL
ALRDGVIPPT LNYQTPDPEI DLDIVAGEPR YGDYRYAINN SFGFGGHNVA LAFGRY
