ID PKS18_MYCTO Reviewed; 393 AA.
AC P9WPF0; L0T6G2; Q79FQ0; Q7D8I1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Alpha-pyrone synthesis polyketide synthase-like Pks18 {ECO:0000250|UniProtKB:P9WPF1};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P9WPF1};
DE AltName: Full=Alpha-pyrone synthesis polyketide synthase type III Pks18 {ECO:0000250|UniProtKB:P9WPF1};
DE AltName: Full=Chalcone synthase-like protein {ECO:0000250|UniProtKB:P9WPF1};
DE Short=CHS-like {ECO:0000250|UniProtKB:P9WPF1};
GN Name=pks18; OrderedLocusNames=MT1417;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Involved in the biosynthesis of tri- and tetraketide alpha-
CC pyrones. Pks18 catalyzes the extension of medium- and long-chain
CC aliphatic acyl-CoA substrates by using malonyl-CoA as an extender
CC molecule to synthesize polyketide products.
CC {ECO:0000250|UniProtKB:P9WPF1}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WPF1}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WPF1}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45681.1; -; Genomic_DNA.
DR PIR; A70958; A70958.
DR RefSeq; WP_003407185.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPF0; -.
DR SMR; P9WPF0; -.
DR KEGG; mtc:MT1417; -.
DR PATRIC; fig|83331.31.peg.1524; -.
DR HOGENOM; CLU_034992_0_1_11; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00831; CHS_like; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR PANTHER; PTHR11877:SF46; TYPE III POLYKETIDE SYNTHASE A; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Alpha-pyrone synthesis polyketide synthase-like
FT Pks18"
FT /id="PRO_0000426963"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P9WPF1"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WPF1"
SQ SEQUENCE 393 AA; 42032 MW; 317D24C33B9CFD42 CRC64;
MNVSAESGAP RRAGQRHEVG LAQLPPAPPT TVAVIEGLAT GTPRRVVNQS DAADRVAELF
LDPGQRERIP RVYQKSRITT RRMAVDPLDA KFDVFRREPA TIRDRMHLFY EHAVPLAVDV
SKRALAGLPY RAAEIGLLVL ATSTGFIAPG VDVAIVKELG LSPSISRVVV NFMGCAAAMN
ALGTATNYVR AHPAMKALVV CIELCSVNAV FADDINDVVI HSLFGDGCAA LVIGASQVQE
KLEPGKVVVR SSFSQLLDNT EDGIVLGVNH NGITCELSEN LPGYIFSGVA PVVTEMLWDN
GLQISDIDLW AIHPGGPKII EQSVRSLGIS AELAAQSWDV LARFGNMLSV SLIFVLETMV
QQAESAKAIS TGVAFAFGPG VTVEGMLFDI IRR
//
