ID B2HJA4_MYCMM Unreviewed; 2197 AA.
AC B2HJA4;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Polyketide synthase PKS {ECO:0000313|EMBL:ACC38573.1};
GN OrderedLocusNames=MMAR_0102 {ECO:0000313|EMBL:ACC38573.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC38573.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC38573.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; CP000854; ACC38573.1; -; Genomic_DNA.
DR SMR; B2HJA4; -.
DR STRING; 216594.MMAR_0102; -.
DR KEGG; mmi:MMAR_0102; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_5_11; -.
DR Proteomes; UP000001190; 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 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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
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; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 45..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2020..2095
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2197 AA; 229646 MW; 4FB0273E266099E3 CRC64;
MKGAKTMNPE CMDPEHNNLF EALKRVAVEL NQTRAQLREH EERADVPVAI VGVGCRYPGG
VESAGGLWDV VVGGRDVISG FPVDRGWDVE GVFDPDPDAL GKTYCRLGGF LDGADRFDAG
FFGIGPSEAL VMDPQQRLLL ECSWEALEDA GIDPVSLRGS VTGVFTGLMS SDYGAGRVSG
DLEGYGLTSA AASVASGRVA YLLGLEGPAV SVDTACSSSL VALHLAASSL RSGECDVALA
GGVTVMATPA TFVGFSRQRG LAADGRCKAF AGAADGTGFS EGAGVVVLMR LSEARRRGLA
VLGVIAGSAV NQDGASNGLT APNGPAQQRV IEAALANAGL TAADVDVVEG HGTGTTLGDP
IEAQALLATY GQARPADRPL WLGSIKSNMG HTQAAAGIAG VIKMVQAMRH ELMPATLHVD
VPSPHVDWSS GAVSLLTQPR PWPAVDGRPR RAGVSSFGIS GTNAHVIVEQ VCPEVVAEAV
DVSPDSLPWV VSGKSEAAVA AQAKRLLAAV QADEGLDRLD VGFSLARRTA FEYRAVVLGE
DRQQLISGLT ELAAGQPGPT VLNGRAATVS KTVMVFPGQG SQWPGMGREL LAASPVFAEH
MRLCAEALGE FVDWSLLDVV NGVAGAPTLD RVDVVQPVLW AMMVSLAQLW RSVGVVPDAV
IGHSQGEIAA ACVAGALSLR DGAAVVALRS RALVDLAGTG GMVAIACGVE RVRELLADYG
DRLSLAAVNG VAAVVVSGEA KALRGLTGRC EAEGMRARRI EVDYASHSAQ VESIGSSLVE
ALAGVRPRSS DIEFVSTVTG ASVDGASLGA DYWYRNIRQT VRFDRAVRYC HEQGCRTFVE
ASPHPVLLAG IEESLAEGIG RPDSAGVIVI PTLGRNEGGV ERFWMSLSQA WLAGVGVDWS
AVFAGSGGRQ VGLPTYAFAR RRFWLDGSAS AADVGEAGLV AAGHALLGAV VEQPDTGAVV
LTGRLSLARQ PWLADHLVGG AVLFPGTGFV ELAIRAGDEV GCGVVEELTL ATPLVLNAGT
AVQVQVVVGS AGQSGQRLVS MYSRADQPDQ HWVLHAQGSV APAAVQPAAA ASAELSTWPP
AGAEAVDIGG LYERLARRGY GYGPAFQGLR AVWRRGRDVF AEVGLPNDDG LDLTDVGIHP
ALLDAALHAW LCVGGFGGDG EATVLPFSWQ HLSLHGSGAS RLRVRIAPAG PSAVSVELAD
GAGLPVLSVG SLTTRPVGAA QLQAAMSAGG DGTGRELLNV VWTPITFERD SVQRDGERRV
VSWDDFLAGR CAAARDLDRD VAVVWQWESG GAESVVNTVY TATHRVLEVL QRWLADDLPA
VLVVCTRGAM GLAGEAITDL AGAAVWGLVR SAQTEHPGRI VLIDTDTSMA LPTVIGVGEP
QLVVRAGDVY AARLARGRAA LRTPDAGQGW QLAATGGGTF DDVVLEPCPR SDEPLAVGQV
RVALAALGVN FRDVLVVLGL YPGNKPTLGG EGAGVVVEVG PGVSGLEPGD RVLGLMSGRS
ECVVDQRLLV PIPAGWSFAE AASAPIVFLT AFYGLSDLAG LRRGESVLVH AATGGVGMAA
IQLARLWGAR VFVTASRGKW DTLRAMGFDD DQIADSRTLE FEEKFSAATG GRGIDVVLNA
LAGEFTDASL RLLAERGRFI EMGKTDIRDA QEVAQEHPGV SYRAFDLANE VAPQRLGQML
AELMTLFAAG KLHRLPVKTW DVRCAPQAYQ FVSQARHIGK VVLSAPTELR DALAAGTVLI
TGGTGLVGSV LARHLVSAYG VRNLVLVSRM GEQGAGVAEL VDELSDAGAR VLVAACDVAD
QSAVEKLIAG WGREYPALTG VIHAAGVLDD AVITSMTPDQ VDSVLRAKVD GAWNLHHATR
GLGLSMFVLC SSIAGVVGAP GQGNYAAANA FLDALVTDRR AHGLAGVSLG WGLWEQASGM
TKHLRGSDVS RLSRGGFAAI SAQQALDLFD AALIVDQPTV LAARLDRRAL ENPALNADLP
TLFSDLITRP MRRNVDNDGT PTELALVNRL NMMNPDEQHD LLTEVVCTQA VMVLGRLNAA
DIDPNATFSD LGFDSLTAIE LRNRLKTVTG LTLPPTLIFD HRAPSALAQH LGQQLCVTHQ
HESHNAMAPA DSEDEKLRSI LSAISVADLR DAGLLDKLLR LRKDPDRNLR VDRVDRVDNV
GTKQQELEGM INSLSPEELV AMALAEPSGG NRMDSGG
//
