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Database: UniProt
Entry: O06586_MYCTU
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Original site: O06586_MYCTU 
ID   O06586_MYCTU            Unreviewed;      1017 AA.
AC   O06586; F2GKM5; I6XC29; Q7D872;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   08-NOV-2023, entry version 169.
DE   SubName: Full=Probable polyketide synthase Pks9 {ECO:0000313|EMBL:CCP44429.1};
GN   Name=pks9 {ECO:0000313|EMBL:CCP44429.1};
GN   OrderedLocusNames=Rv1664 {ECO:0000313|EMBL:CCP44429.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP44429.1, ECO:0000313|Proteomes:UP000001584};
RN   [1] {ECO:0000313|EMBL:CCP44429.1, ECO:0000313|Proteomes:UP000001584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584};
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D.,
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., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J.,
RA   Squares R., Squares S., 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] {ECO:0007829|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011445;
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).
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DR   EMBL; AL123456; CCP44429.1; -; Genomic_DNA.
DR   RefSeq; NP_216180.1; NC_000962.3.
DR   RefSeq; WP_003900389.1; NZ_NVQJ01000010.1.
DR   AlphaFoldDB; O06586; -.
DR   SMR; O06586; -.
DR   STRING; 83332.Rv1664; -.
DR   PaxDb; 83332-Rv1664; -.
DR   DNASU; 885519; -.
DR   GeneID; 885519; -.
DR   KEGG; mtu:Rv1664; -.
DR   PATRIC; fig|83332.111.peg.1850; -.
DR   TubercuList; Rv1664; -.
DR   eggNOG; COG3321; Bacteria.
DR   InParanoid; O06586; -.
DR   OMA; TYAFDAR; -.
DR   OrthoDB; 9778690at2; -.
DR   PhylomeDB; O06586; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001584};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..394
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          864..942
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1017 AA;  106403 MW;  B93A22D8818AE0EC CRC64;
     MQPTGIAIIG LACRFPTVVS PGDLWDLLRD GREAAGSIDN VADFDADFFN LSPREASAMD
     PRQRLALELT WELLEDAFVV PETLRGQPIA VYLGAMNDDY AVLTLAADRV DHHAFAGTSR
     AIIANRVSFA FGLRGPSVTI DSGQSSSLVA VHLACESVRT GEAPLAIAGG VHLNLARETA
     MLEQEFGAVS PSGHTYAFDE RADGYVPGDG GGLVLLKPVQ AALDDGDRIH AIIRGSAVGN
     AGHSATGLTV PSVAGQVDVI RRAMSGAGVD CHQVHYVEAH GTGTKIGDPI EARALGEIFA
     ARQRRPVSVG SVKTNIGHTG GAAGIAGLLK AVLAIENAVI PPSLNYVGAA IDLDSLGLRV
     DTALTPWPVA DEPRRAGVSS FGMGGTNAHV ILEQGPTQSP EIVESVAAAG SNAPVAVPWV
     LAARSPQALT NQAGRLLAHL TADDGLTALD VGWSLVSTRS VFDHRAVVVG ADRGRLMAGL
     AGLAAGEPGA GVVVGRARSV GKTVFVFPGQ GSQWLGMGRQ LYGRYSVFAR AFDEVVAVLD
     GQLRLSVRQV MWGADAGLLE STEFAQPALF VVQVALAALL QDWGVLPDLV MGHSVGEIAA
     AYVAGALSLV DAARVVAARG RLMQALPAGG VMVAVAASED EVAPLLTEGV CIAAVNAPES
     VVISGEQAAV GVVVDRLVGL GRRVRRLAVS HAFHSVLMDP MVEEFSKVLA DVCVRAPRIG
     LVSNVTGQLA GAGYGSPAYW VEHVRKPVRF FDGVGLAESL GARVFVEVGP GAGLEASVAL
     LARDRPEVES VLAGVGRLFA EGVAVDWSSV FAGLGGRRVE LPTYGFARQR FWLGDNGELS
     VDQTGKDAGA IARLQSLAPP ELQRQLVELV CFHAAIVLGR KSSHDIDPEC AFQDLGFDSM
     SGVELRNRLQ MAIGLPGLSL PRTLIFDYPT ASALAECLGQ LLGGQHESSD DESIWQLLKN
     IPIHQLRRTG LLDKLLLLAG QPEESLAGRT VSDEVIDSLS PEALIGLALD EDENDIR
//
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