ID G0TK12_MYCCP Unreviewed; 2126 AA.
AC G0TK12;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Putative polyketide synthase PKS7 {ECO:0000313|EMBL:CCC44002.1};
GN Name=pks7 {ECO:0000313|EMBL:CCC44002.1};
GN OrderedLocusNames=MCAN_16701 {ECO:0000313|EMBL:CCC44002.1};
OS Mycobacterium canettii (strain CIPT 140010059).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC44002.1, ECO:0000313|Proteomes:UP000008896};
RN [1] {ECO:0000313|EMBL:CCC44002.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44002.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=22389744; DOI=10.1371/journal.pntd.0001552;
RA Bentley S.D., Comas I., Bryant J.M., Walker D., Smith N.H., Harris S.R.,
RA Thurston S., Gagneux S., Wood J., Antonio M., Quail M.A., Gehre F.,
RA Adegbola R.A., Parkhill J., de Jong B.C.;
RT "The Genome of Mycobacterium Africanum West African 2 Reveals a Lineage-
RT Specific Locus and Genome Erosion Common to the M. tuberculosis Complex.";
RL PLoS Negl. Trop. Dis. 6:e1552-e1552(2012).
RN [2] {ECO:0000313|EMBL:CCC44002.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44002.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=23291586; DOI=10.1038/ng.2517;
RA Supply P., Marceau M., Mangenot S., Roche D., Rouanet C., Khanna V.,
RA Majlessi L., Criscuolo A., Tap J., Pawlik A., Fiette L., Orgeur M.,
RA Fabre M., Parmentier C., Frigui W., Simeone R., Boritsch E.C., Debrie A.S.,
RA Willery E., Walker D., Quail M.A., Ma L., Bouchier C., Salvignol G.,
RA Sayes F., Cascioferro A., Seemann T., Barbe V., Locht C., Gutierrez M.C.,
RA Leclerc C., Bentley S.D., Stinear T.P., Brisse S., Medigue C., Parkhill J.,
RA Cruveiller S., Brosch R.;
RT "Genomic analysis of smooth tubercle bacilli provides insights into
RT ancestry and pathoadaptation of Mycobacterium tuberculosis.";
RL Nat. Genet. 45:172-179(2013).
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DR EMBL; HE572590; CCC44002.1; -; Genomic_DNA.
DR RefSeq; WP_014000873.1; NC_015848.1.
DR GeneID; 45425631; -.
DR KEGG; mce:MCAN_16701; -.
DR HOGENOM; CLU_000022_35_2_11; -.
DR OMA; GFACRLP; -.
DR Proteomes; UP000008896; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 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 Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
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; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1976..2051
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2126 AA; 221072 MW; C25376F78BF76CE9 CRC64;
MNSTPEDLVK ALRRSLKQNE RLKRENRDLL ARTTEPVAVV GMGCRYPGGV DSPETLWELV
AHGRDAVSEF PADRGWDVAG LFDPDPDAVG KSYTRCGGFL TDVAGFDAEF FGIAPSEALA
MDPQQRLLLE VSWEALERAG IDPITLRGSQ TGVFAGVFHG SYGGQGRVPG DLERYGLRGS
TLSVASGRVA YVLGLQGPAV SVDTACSSSL VALHLAVQSL RLGECDLALV GGVTVMATPA
MFIEFSRQRA LSADGRCKAY AGAADGTAFA EGAGVLVLAR LADARRLGHP VLALVRGSAV
NQDGASNGLA TPNGPAQQRV ITAALASARL GVADVDVVEG HGTGTTLGDP IEAQAILATY
GQRPADRPLW LGSIKSNIGH TSAAAGVAGV IKMVQAMRHG VLPKTLHVDV PTPHVDWSAG
AVSLLTEPRP WHVPGRPRRA GVSSFGISGT NAHVILEQAP AVEPVGAAHG NDPVAVPWVL
SARSAQALTN QARRLLAWVG ADENVRPLDV GWSLVNTRSL FDHRAVVVGA DRTQLMEGLT
GLAAGVPGAD VVAGRAQTVG KTAFVFPGQG AQWLGMGAQL CATAPVFAEH IHRCERALRE
HVEWSLLDVL RGAPGAPGLD RVDVVQPALW AVMVSLAELW RSVGVVPDAV IGHSQGEIAA
AYVAGALSLR DAAAVVALRS RLLVRLGGAG GMVSLACGQP QAEKLASQWG DRLNIAAVNG
VSSVVLAGET DAVTELMQRC EAEGIRARRI DVDYASHSAQ VDAIREELIA ALRGIEPRTS
TVAFFSTVTG ELMDTAGVNA EYWYRSIRQP VQFERAVRNA FDGGYRVFVE SSPHPVLIAG
IEETLVDCDR GATGEPIVIP TLGRDDGGVG RFWLSAGQAH VAGVGVDWRA AFADLGGRRV
ELPTYGFARQ RFWLDGLGAV GGDLGGVGLV GAEHGLLAAV VQRPDSGGVV LTGRISVVAA
PWLADHAVGP VVLFPGTGFV ELALRAGDEV GCSVLQELTL QAPLVLPAGG VRVQVVVGGV
EQSGTRNVWV YSAAGQADSS PGWTLHAQGV LGVGSVQPAA ELSVWPPVGA RAMDVADGYQ
VLAARGYGYG PAFRGLQALW RRGAEVFADV TLPEGVPIRG FGIHPAVLDA ALHAWGIVEG
EQQTMLPFSW EGVCLHASGA ARVRVRLAPV GRGAVSVELA DPQGLPVLSV RQLMVRPVSA
AALSRSTAGD RGLLEMIWTP VPLEGGDIGD DAVVWELPPH AGAQAGGDVL AAVYRGVHEV
LEVLQSWLAS DVTGLGVVVT RGAVGPVDDD VTDLAGAAVW GLVRSAQAEH PGRVVLVDTD
GSVAVEDAVG FGARSGEPQL VVRRGRVYAA RLAPVAAGLT LPSASAGGWR LVAGGGGTLA
DVVVAPVAPV ELATGQVRVA VGAVGVNFRD VLVALGMYPG GGELGVDGAG VVVEVGPGVT
GLAVGDRVMG LLGLVGSEAV VDARLVTMVP AGWSLVEAAA VPVAFLTAFY GLSVLAEVAA
GQKVLVHAGT GGVGMAAVSL ARYWGAEVFV TASRAKWDTL RAMGFDDIHI SDSRSLEFEE
AFLRATEGSG VDVVLNSLAG EFTDASLRLL PRGGRFIELG KTDIRDGQTV AERHRGVRYR
AFDLVEAGPD RIAAMLSEVV GLLAAGVLAR LPVKTFDARC APAAYRFVSQ ARHIGKVVLT
IPDGPGGQSG LAGGTVVVTG GTGMAGSAVA THLVRRHGVA NLVLVSRSGE QADRAAEVAA
LLREGGAQVA VVSCDVADRD ALAALLAGLD PRYPLKGVFH AAGVLDDAVI TGLTPDRVDT
VLRAKVDGAW NLHELTEDMD LSAFVVFSSM AGIVGTPAQG NYAAANAFLD GLVAYRRSRG
LAGLSVAWGL WEQASAMTRH LGERDRARMT QAGLAPLTTE QALGFLDTAL QADRAVVVAA
RLDRAALAGA GAALPALFSQ LAAGPTRRRI DAADTAVSMS GLVSRLHALT PERRQRELTD
LVISNAAAVL GRSSSVDINA HKAFQDLGFD SLTAVELRNR LKTATGLTLS PTLIFDYPTP
ATLAEHLDSR LVTASGSDQQ SLSDRVDDIT RELVVLLDQP DLSANVKAHL RTRLQTMLTS
LTTEDDDIAA ATESQLFAIL DEELGS
//