UniProt: C5HV18

Database: UniProt
Entry: C5HV18_STRAT

LinkDB:  C5HV18_STRAT 
Original site:  C5HV18_STRAT

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Ontology (4)   
   GO (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (38)   
   InterPro (20)   
   Pfam (9)   
   PROSITE (4)   
   SMART (5)   
All databases (43)   

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ID   C5HV18_STRAT            Unreviewed;      2547 AA.
AC   C5HV18;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ACN69992.1};
GN   Name=idmP {ECO:0000313|EMBL:ACN69992.1};
OS   Streptomyces antibioticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1890 {ECO:0000313|EMBL:ACN69992.1};
RN   [1] {ECO:0000313|EMBL:ACN69992.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL8167 {ECO:0000313|EMBL:ACN69992.1};
RA   Kelly W.L., Li C., Roege K.E.;
RT   "Analysis of the indanomycin biosynthetic gene cluster from Streptomyces
RT   antibioticus NRRL 8167.";
RL   ChemBioChem 0:0-0(2009).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; FJ545274; ACN69992.1; -; Genomic_DNA.
DR   SMR; C5HV18; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 3.30.70.3290; -; 3.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 6.10.140.1830; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR041618; PKS_DE.
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; IPR037401; SnoaL-like.
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; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF12680; SnoaL_2; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
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; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          35..468
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1504..1579
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1602..2026
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   2547 AA;  267768 MW;  A305618CD4993BB0 CRC64;
     MSSASSEKIV EALRASLTEN ERLRRLNQEL AAAAHEPVAI VSMACRFPGG VESPEDFWDL
     ISEGRDAVSG LPDNRGWDLD ALYDPDPEAQ GKTYVREGAF LYDAAEFDAE LFGISPREAL
     AMDPQQRLLM ETSWEVLERA GIRPDSLRGK PVGVFTGGIT SDYVTRHYAS GTAPQLPSGV
     ESHFMTGSAG SVFSGRIAYT YGFEGPAVTV DTACSSSLVA LHMAAQSLRQ GECSLAFAGG
     VAVLPNPGTF VGFSRQRALS PDGRCKAFSA DADGTGWGEG AGLVLLEKLS DARRNGHPVL
     AILRGSAVNQ DGASNGLTAP NGPSQQRVIR AALANARLSP DDVDVVEAHG TGTPLGDPIE
     AQALQATYGR SRSAERPLWL GSVKSNVAHA QAAAGVASVI KVVMALRHRL LPKTLHADER
     SPHIDWHSGA VELLTEAREW SRTEGRARRA GVSSFGISGT NAHVIIEEAP EPTVETTAAP
     AAEPAAERSP VEVVPWVTSA RSAAGLVAQA DRLARFVGVR PELDPVDVGW SLVGSRSVLE
     HRAVVLGRGR DELVAGLASL ASGVSAPGVV CGVGRGGVRP VLVFPGQGSQ WVGMAVGLLE
     SSPVFAERLG ECEAALAPFV EWSLRDVLGG GVGSVGLLER VDVVQPVLFA VMVSLAELWR
     SVGVVPAAVV GHSQGEIAAA CVAGGLSLGD AARVVALRSR ALRRLSGLGG MVSVAAGRER
     TEDLLAGWVG RVGVAAVNGP GSTVVSGDAD ALDELVVVCE GLGVRARRVA VDYASHSAHV
     DLIREELGEL LAPVVPVSSG VPFFSTVTGD WLDTARLDAG YWFENLRRPV RFGEATRALL
     DEGFSVFIES SAHPVLATGI SETVDAGDVP GAVVGSLRRG EGGMGRFLTS VAEAFVRGVE
     VDWASVLPGG RRVDLPTYAF QRKHYWLEST AAEQNDPNAL PADAADTRFW EAVESENLDE
     LARTLDTAEA RPALETLVPA LASWRRQRRE HSVVDSWRYR VGWRPAQISP RSDTTPTGTW
     LVIAPAAHQE HPWVTAATES LRDGGAEVRT VVLDPTALQR DSLAQELGTD GAQIDGVLSL
     LALDETPLPR HPGVPAGLGA TLTLLQALGD AGIEAPLWCA TQGAVSVSGV DHLTRPLQAQ
     VWGLGRVAGL EHPDRWGGLV DLPETVDARS AGRLRALLAE PGDEDQLALR PSGAFVRRLT
     RAPLEDTPPV REWRPDGTTL ITGGTGGLGG HVARWLAAQG AGHLVLTSRR GPDADGAAEL
     REELQGMGSR VSIVACDASD RNALGALLRR LRDEGTPVRA VVHTAGVAGR FTTLADADLA
     DLAETLGAKA GGAAALDELL AGEGEPDAFV LFSSNAGVWG GAGQGPYAAA NAYLDALAEQ
     RRARGAAATS VAWGMWSGQG LVAGQPGVEE ALRRLGLKAM DPDLAITALH QALDRDETTL
     SVTDMDWDRF VSVFTAARPR PLLDELPEAA RILRAAEAGH EANSESRSAL AEQLAGLAPA
     EQHRLLVEMV RAQAATVLGH DSGDAVDQDR QFQELGFNSV SAVELRNRLN EATGLRLPAS
     LVFDHPTPAA LARRIRAEVL GEAQEPAAAG LGGPAGGAAV GDDAVAIVGM SCRLPGGVES
     PDDLWRVVVE GRDVISELPT DRAWEAVERL RELGMDMPGG RWLRAGGFID SAAEFDPDFF
     GVSTAEALAM DPQQRLLLEM SWEAIERAGI DPHTLRGSST GVYVGTFFQP YWAGSNRIAE
     DVKPFLGTGV TPTFASGRIA YLLGLEGPTF TVDTGCSSSA VALHQACQAV RRGECSTALV
     GGVTVLSSPM GVPDLGGMAE DGRCKAFSAE ADGTGWGEGA AMVMIERLSE ARRLGHPVLA
     VVRGSAVNHN GESNGMSAPN GPSQQRLIRQ ALADARLSPD EVDAVEAHGT GTPLGDPIEA
     QALLATYGRD RAEDRPLWLG TVKTNIGHPQ AASGLVGVIK MVLAMRHGLL PRSLYADSPT
     PQVDWASGAV SLLAENTPWP EAGRPRRAGV SSFGASGTKA HIILEQDAWL PDAGTPEPAV
     GTDGRTAAVP LLVSARTPDG VRQQARRLRE FVESHPEAEP TDLAWSLATS RSAFEHRAAL
     FAVDREELLG GLADLEQGDL LGRTLRGEAG ATARTAFVFA GEALPDTPAP AARQLYEALP
     DFADALDEAC VHLDACARLG RPVQEFALGV HPAADAVAAA CVAFAHESAL SRALPRLGVT
     PEVAAGLRLG EISAAHAAGV LGIEDAAALL VAVARLRDGA ADREAALDGF GRTAKNIASH
     PARLRLVSAL TDEPLDAERL LDPGHWLDEE TPVDVPTADG GRAPRVHGVF VGLPDGVPAG
     SAGAVTGLMR VLARAHVDGV TVDWRETLTA VGAQGRSVEL PTYSFRRDHY WLEANPVAVL
     GDALAGKNVA NWSAVEGVEL LDETSRKEVV EEYFRRLNAG DLDKVLEMLA PDVRMEDPVG
     GPPKLGREAV GEYIAQVIEA NAEITVGPIV AAQDGLRVAL PLVGRLAQLG RSDGPRMEIN
     CVDVIQVNGE GLIQEVLVFW GMTDIAR
//

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