ID   PKS10_MYCTU             Reviewed;         353 AA.
AC   P9WPF5; 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 34.
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=Rv1660;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION IN DIM BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12730158; DOI=10.1128/jb.185.10.2999-3008.2003;
RA   Sirakova T.D., Dubey V.S., Cynamon M.H., Kolattukudy P.E.;
RT   "Attenuation of Mycobacterium tuberculosis by disruption of a mas-like gene
RT   or a chalcone synthase-like gene, which causes deficiency in dimycocerosyl
RT   phthiocerol synthesis.";
RL   J. Bacteriol. 185:2999-3008(2003).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000269|PubMed:12730158}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of phthiocerol
CC       dimycocerosate (DIM) on the cell envelope.
CC       {ECO:0000269|PubMed:12730158}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44425.1; -; Genomic_DNA.
DR   PIR; G70621; G70621.
DR   RefSeq; NP_216176.1; NC_000962.3.
DR   RefSeq; WP_003408181.1; NZ_NVQJ01000069.1.
DR   AlphaFoldDB; P9WPF5; -.
DR   SMR; P9WPF5; -.
DR   STRING; 83332.Rv1660; -.
DR   PaxDb; P9WPF5; -.
DR   DNASU; 885112; -.
DR   GeneID; 45425630; -.
DR   GeneID; 885112; -.
DR   KEGG; mtu:Rv1660; -.
DR   TubercuList; Rv1660; -.
DR   eggNOG; COG3424; Bacteria.
DR   OMA; GQESPFM; -.
DR   PhylomeDB; P9WPF5; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0034081; C:polyketide synthase complex; IMP:UniProtKB.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR   GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IMP:MTBBASE.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..353
FT                   /note="Polyketide synthase-like Pks10"
FT                   /id="PRO_0000406360"
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