KASA_MYCTE
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 03-AUG-2022, entry version 44.
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; 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 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}.
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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; 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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Transferase.
FT CHAIN 1..416
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000422686"
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; 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