ID   PKS11_MYCBO             Reviewed;         353 AA.
AC   Q7VEU7; A0A1R3XZB9; X2BIL5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Methyl-branched alkylpyrone synthesis polyketide synthase-like Pks11 {ECO:0000250|UniProtKB:P9WPF3};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P9WPF3};
DE   AltName: Full=Methyl-branched alkylpyrone synthesis polyketide synthase type III Pks11 {ECO:0000250|UniProtKB:P9WPF3};
GN   Name=pks11; OrderedLocusNames=BQ2027_MB1693;
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 methyl-branched alkylpyrones.
CC       Pks11 catalyzes the extension of medium- and long-chain aliphatic acyl-
CC       CoA substrates by using malonyl-CoA and methylmalonyl-CoA as extender
CC       molecules to synthesize polyketide products. Palmitoyl-CoA or a similar
CC       long chain fatty acid derivative is the likely substrate in vivo.
CC       {ECO:0000250|UniProtKB:P9WPF3}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WPF3}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WPF3}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00296.1; -; Genomic_DNA.
DR   RefSeq; NP_855345.1; NC_002945.3.
DR   RefSeq; WP_003408248.1; NC_002945.4.
DR   AlphaFoldDB; Q7VEU7; -.
DR   SMR; Q7VEU7; -.
DR   EnsemblBacteria; SIU00296; SIU00296; BQ2027_MB1693.
DR   GeneID; 45425634; -.
DR   PATRIC; fig|233413.5.peg.1846; -.
DR   OMA; NFMGCYA; -.
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..353
FT                   /note="Methyl-branched alkylpyrone synthesis polyketide
FT                   synthase-like Pks11"
FT                   /id="PRO_0000407319"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPF3"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPF3"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPF3"
FT   BINDING         277..282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPF3"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPF3"
SQ   SEQUENCE   353 AA;  37639 MW;  1F2225FC7D41AA17 CRC64;
     MSVIAGVFGA LPPHRYSQSE ITDSFVEFPG LKEHEEIIRR LHAAAKVNGR HLVLPLQQYP
     SLTDFGDANE IFIEKAVDLG VEALLGALDD ANLRPSDIDM IATATVTGVA VPSLDARIAG
     RLGLRPDVRR MPLFGLGCVA GAAGVARLRD YLRGAPDDVA VLVSVELCSL TYPAVKPTVS
     SLVGTALFGD GAAAVVAVGD RRAEQVRAGG PDILDSRSSL YPDSLHIMGW DVGSHGLRLR
     LSPDLTNLIE RYLANDVTTF LDAHRLTKDD IGAWVSHPGG PKVIDAVATS LALPPEALEL
     TWRSLGEIGN LSSASILHIL RDTIEKRPPS GSAGLMLAMG PGFCTELVLL RWR