ID   PKS18_MYCBO             Reviewed;         393 AA.
AC   Q7U064; A0A1R3XY69; X2BHP7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BQ2027_MB1406;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
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; LT708304; SIU00010.1; -; Genomic_DNA.
DR   RefSeq; NP_855059.1; NC_002945.3.
DR   RefSeq; WP_003407185.1; NC_002945.4.
DR   AlphaFoldDB; Q7U064; -.
DR   SMR; Q7U064; -.
DR   EnsemblBacteria; SIU00010; SIU00010; BQ2027_MB1406.
DR   PATRIC; fig|233413.5.peg.1541; -.
DR   OMA; PIWGLGC; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001419; 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   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; PTHR11877; 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; SSF53901; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism; Transferase.
FT   CHAIN           1..393
FT                   /note="Alpha-pyrone synthesis polyketide synthase-like
FT                   Pks18"
FT                   /id="PRO_0000407321"
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