ID FAB1_MYCTE Reviewed; 416 AA. AC H8ESN0; DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2013, sequence version 2. DT 08-JUN-2016, entry version 24. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1; DE EC=2.3.1.41; 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; Actinobacteria; Corynebacteriales; 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 RT 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 RT through three anti-sigma factor substrates."; RL Mol. Microbiol. 77:605-617(2010). CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl- CC carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + CC [acyl-carrier-protein]. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- INDUCTION: Repressed by Rip1 and independently by the metal CC chelator phenanthroline. {ECO:0000269|PubMed:20545848}. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. CC {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 ProteinModelPortal; H8ESN0; -. DR SMR; H8ESN0; 2-416. DR EnsemblBacteria; BAL66261; BAL66261; ERDMAN_2470. DR KEGG; mtn:ERDMAN_2470; -. DR KO; K11609; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000007568; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.47.10; -; 2. 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 Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. PE 2: Evidence at transcript level; KW Acyltransferase; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Transferase. FT CHAIN 1 416 3-oxoacyl-[acyl-carrier-protein] synthase FT 1. FT /FTId=PRO_0000422686. FT ACT_SITE 171 171 {ECO:0000250}. 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 //