ID   PKS10_MYCTO             Reviewed;         353 AA.
AC   P9WPF4; L0T8X1; P94995; Q7D876;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Polyketide synthase-like Pks10;
DE            EC=2.3.1.-;
DE   AltName: Full=Chalcone synthase-like protein;
DE            Short=CHS-like;
DE   AltName: Full=Polyketide synthase type III Pks10;
GN   Name=pks10; OrderedLocusNames=MT1698;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; 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: Could catalyze the elongation of hydroxybenzoyl-CoA as well
CC       as elongation of the aliphatic precursor involved in the synthesis of
CC       phthiocerol dimycocerosate (DIM). {ECO:0000250}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45967.1; -; Genomic_DNA.
DR   PIR; G70621; G70621.
DR   RefSeq; WP_003408181.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPF4; -.
DR   SMR; P9WPF4; -.
DR   EnsemblBacteria; AAK45967; AAK45967; MT1698.
DR   GeneID; 45425630; -.
DR   KEGG; mtc:MT1698; -.
DR   PATRIC; fig|83331.31.peg.1825; -.
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   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="Polyketide synthase-like Pks10"
FT                   /id="PRO_0000426961"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  37146 MW;  5B681D1E8D53C2DA CRC64;
     MSVIAGVFGA LPPYRYSQRE LTDSFVSIPD FEGYEDIVRQ LHASAKVNSR HLVLPLEKYP
     KLTDFGEANK IFIEKAVDLG VQALAGALDE SGLRPEDLDV LITATVTGLA VPSLDARIAG
     RLGLRADVRR VPLFGLGCVA GAAGVARLHD YLRGAPDGVA ALVSVELCSL TYPGYKPTLP
     GLVGSALFAD GAAAVVAAGV KRAQDIGADG PDILDSRSHL YPDSLRTMGY DVGSAGFELV
     LSRDLAAVVE QYLGNDVTTF LASHGLSTTD VGAWVTHPGG PKIINAITET LDLSPQALEL
     TWRSLGEIGN LSSASVLHVL RDTIAKPPPS GSPGLMIAMG PGFCSELVLL RWH