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).
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; 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
//