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 28-JUN-2023, entry version 48. 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; Actinomycetota; Actinomycetes; Mycobacteriales; 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}. 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; 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: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 2: Evidence at transcript level; 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_0000422686" 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; 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 //