UniProt: W0C910

Database: UniProt
Entry: W0C910_9ACTN

LinkDB:  W0C910_9ACTN 
Original site:  W0C910_9ACTN

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Ontology (4)   
   GO (4)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (40)   
   InterPro (21)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (48)   

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ID   W0C910_9ACTN            Unreviewed;      1881 AA.
AC   W0C910;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=PieA5 {ECO:0000313|EMBL:AHE80995.1};
GN   ORFNames=CAG99_26300 {ECO:0000313|EMBL:ARQ71873.1};
OS   Streptomyces marincola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2878388 {ECO:0000313|EMBL:AHE80995.1};
RN   [1] {ECO:0000313|EMBL:AHE80995.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SCSIO 03032 {ECO:0000313|EMBL:AHE80995.1};
RX   PubMed=24409990; DOI=10.1021/ol4034176;
RA   Chen Y., Zhang W., Zhu Y., Zhang Q., Tian X., Zhang S., Zhang C.;
RT   "Elucidating hydroxylation and methylation steps tailoring piericidin A1
RT   biosynthesis.";
RL   Org. Lett. 16:736-739(2014).
RN   [2] {ECO:0000313|EMBL:ARQ71873.1, ECO:0000313|Proteomes:UP000194218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ71873.1,
RC   ECO:0000313|Proteomes:UP000194218};
RA   Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT   "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT   diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; KF874660; AHE80995.1; -; Genomic_DNA.
DR   EMBL; CP021121; ARQ71873.1; -; Genomic_DNA.
DR   KEGG; smao:CAG99_26300; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000194218; Chromosome.
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; 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; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; 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; 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; 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; 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; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000194218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..459
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1722..1797
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1049..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1881 AA;  194587 MW;  0FB54ED79B960A00 CRC64;
     MAASNEQLLD ALRASLKETK RLKQANRELA DAWHEPVAVV AMACRFPGGV RSPEDLWRLL
     AADGDAVTPF PDDRGWDLDA LYDPDPDRPG TSYVRHGAFL DGADRFDADF FGISPREALA
     MDPQQRLLLE TTWETFERAG IDPESARGSR TGVFVGAAPL GYAGADQQSE GAEGYLLTGT
     TVSVASGRLA YTFGLEGPAV TVDTACSSSL VALHLAAQAL RRGECAMALA GGAAVMAAPH
     MFVEFSRQRG LAPDGRCKAF AAGADGTAWG EGVGMLLLER LSDARRNGHP VLAVVRGSAV
     NQDGASNGLT APSGPAQQRV ITDALADARL APADVDAVEA HGTGTSLGDP IEAQALLATY
     GRERPEGRPL WLGSIKSNIG HTQLAAGAAG VIKMVLAMRH GVLPRTLHVD EPSPHVDWSS
     GAVELLTSAT DWPGTERPRR GAVSSFGISG TNAHVILEHP GPEQDLTPAP DTDAGTGAAV
     PVPVLLSARS GDALPAQAAR LRDAVAAHPA WQPHTVAHAT ATARAALEHR AAVVAADRAA
     LLAGLDALAH GDDAPHVVRD RAPGPGRTAF LFTGQGAQRP GAGRELHARQ PAFARALDEV
     CEVLSARTGQ ALRDIMFAPE GDPLARLLDD TAVAQAALFA LEVALFRLTE SWGLRPDLLL
     GHSVGELAAA HVAGVFTLDD AATLVAARGR LMGAQPPGGA MVSLQADETE VRALLDGREH
     LAAIAAVNGP RTVVVSGDEA TVLGIAAHLN AEGRRTRRLR VSHAFHSPHM DGMLEPFREV
     VAGLAPREPG LTVVSNVTGL PLTAEQAGSP EYWAQHVRRP VRFLDGLRHL AAQKTTTCLE
     LGPAGVLSAL AHETFTADAA VADRDGAAGG RGDAAVAVPL LRRNRPEPET VAAAVARAHA
     RGTAVDWAAF HGGAAAPRVA LPTYAFQGRR YWLAPAPRGG DAAALGLDTA HHPLLGAAVR
     PADGDGLVLT GRLSTRSHRW LADHVVLGAV VVPGTAYLEL AAHAARLTGC DLIEELTQEA
     PLVLAAGRAA RVQVTVGPAD ATGRRAVALH SRPDEEPDAP WTRHADGVLA PGAPQPGPTG
     QDEEAGQDAR DGQWPPAGAV PADLSGFYAT VAAHGFAYGP AFRGLRAVWR RGDEVFAEAA
     LPEDHRGGAG AYGVHPALLD AVLHAGLVGH TGGPVLLPFA WRGVAVRAAG PSVLRARLSP
     AGPDARSLTV TDGTGTPVAT VAALRARPVT PAQLRAARAT HHDALFRVRW TPAPGAEGAP
     AGTYALVGGA PATPASPGAP ARYRDLADLA EAVAGGAPVP ATVFLTDDAP REDVTPAAVR
     AALDRTLTVL RTWLADRRFA GSSLVLVTRG AVAVADDEDV PDLTRAPLWG LLRAAQAEHP
     GRFRLLDTGG PAQGTEEDAG ESALMAALPA VAASDEPQLA LRAGHLLAPR LTRADRPGPD
     AGAAPATEGT VLITGGTGAL GAAVARHLAA TRRARHLLLL SRGGPGAEGA DGLRADLVAA
     GVQVTVEVCD VADRDALAKV IASVPAEHPL TAVVHAAGTV DDGVLDALTA ERVDAVLRPK
     ADAAWHLHEL TRDLELTAFV MFSSATATLG GAGQGNYAAA NAFLDALARH RGALGLPGVS
     LAWGPWAGGG MADGLDAPAH RRMRRAGVAP LAPADALALL DHTWSGPERN PVPLRLDPAA
     ARRAPEDSPP LLRDLVTAGP GTGEPPRLAE RLAGLPPGER EAAALDFVRA QVAQVLGHGA
     VDGITPDRAF DDLGFDSLTA VELRNRLNTA SGLRLPVTLI FDYPTTGALA RHVLAELPFD
     ETGGEHSTTG AVLAELDRLE AALTGVDPDD PGRAGVAARL RALAARWDDA RSSGDDARAD
     GLETAADDEV FDFIEKELGI S
//

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