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 02-SEP-2026, entry version 129. 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; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; 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] + CC malonyl-[ACP] + H(+) = a 3-oxo-ultra-long-chain mono-unsaturated CC fatty acyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:65312, Rhea:RHEA- CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:16765, Rhea:RHEA- CC COMP:16775, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; WP_010908457.1; NC_002677.1. DR AlphaFoldDB; Q9CBS7; -. DR SMR; Q9CBS7; -. DR STRING; 272631.gene:17575498; -. 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 OrthoDB; 9808669at2; -. DR UniPathway; UPA00915; -. DR Proteomes; UP000000806; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:TreeGrafter. DR GO; GO:0030497; P:fatty acid elongation; IEA:UniProtKB-ARBA. DR CDD; cd00834; KAS_I_II; 1. DR FunFam; 3.40.47.10:FF:000029; 3-oxoacyl-[acyl-carrier-protein] synthase 1; 1. DR FunFam; 3.40.47.10:FF:000018; 3-oxoacyl-[acyl-carrier-protein] synthase 2; 1. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR000794; Beta-ketoacyl_synthase. DR InterPro; IPR014031; KAS_C. DR InterPro; IPR014030; KAS_N. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; NF005589; PRK07314.1; 1. DR NCBIfam; NF005916; PRK07910.1; 1. 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..416 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1" FT /id="PRO_0000180331" FT DOMAIN 11..415 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 171 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 311 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 345 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" 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 //