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Database: UniProt
Entry: A0A1V2RU60_9ACTN
LinkDB: A0A1V2RU60_9ACTN
Original site: A0A1V2RU60_9ACTN 
ID   A0A1V2RU60_9ACTN        Unreviewed;       789 AA.
AC   A0A1V2RU60;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Erythronolide synthase, modules 3 and 4 {ECO:0000313|EMBL:ONK15963.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:ONK15963.1};
GN   ORFNames=STBA_68070 {ECO:0000313|EMBL:ONK15963.1};
OS   Streptomyces sp. MP131-18.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK15963.1, ECO:0000313|Proteomes:UP000189065};
RN   [1] {ECO:0000313|EMBL:ONK15963.1, ECO:0000313|Proteomes:UP000189065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP131-18 {ECO:0000313|EMBL:ONK15963.1,
RC   ECO:0000313|Proteomes:UP000189065};
RA   Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA   Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT   "New natural products identified by combined genomics-metabolomics
RT   profiling of marine Streptomyces sp. MP131-18.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ONK15963.1}.
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DR   EMBL; LZNS01000001; ONK15963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2RU60; -.
DR   STRING; 1857892.STBA_68070; -.
DR   Proteomes; UP000189065; Unassembled WGS sequence.
DR   GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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; IPR036736; ACP-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:ONK15963.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189065};
KW   Transferase {ECO:0000313|EMBL:ONK15963.1}.
FT   DOMAIN          620..695
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          739..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  81126 MW;  2FF0D78775B5FE6A CRC64;
     MTAEVAAVVD EDLSGTWPPA GAEAVPLPGF YERLAEDGYE YGPAFRGLRA AWRRGEEIFA
     EVRLPEERHG DDFDLHPALL DAALHTSLVG GVDEVRLPFS WAGVTLHATG ATALRVRLTP
     TGPDTMSLAL ADETGAPVAT VESLAVRPVR AEQLRDVVGD ALFGVDWAEV PPVSADAPHQ
     APVESAELLP GEPAPPAVAL RWLPEPGGDP AEAVVRALAS LQEWLTDGRF VASRLVWVTR
     GAVSVSEGED VTDLAGAAVW GAVRSAQAEH PGRIVLVDLD AASADGGGEP AVLPSALPLD
     AEPQLAVRGG RVLAPRLARL RRPAAAPAWP GLGGTVLITG GTGTLGGLVA RHLVEAHGVR
     HLLLVSRRGP RAAGADRLVT ELTGLGAEVT MVACDAADRD ALAAVLDTVP ADRPLAGVVH
     AAGVLDDGVL GSLTPERVRA VVRPKADAAR HLHDLTRDAD LSMFVLFSAA GGVLGAAGQA
     NYAAANAFLD ALAQRRRARG LPAVSMGWGL WEAASGMTGG LDGTDRARMR RSGVLPLASA
     DGLALFDAAL AEGRPVVLPV RLDLAAVREA QEPPPLLRRL VDTAARRVVR ARAAVGAGAE
     RDAAGFPGGL AGLPAAERAE ALVDLVRSHV ATVLGLAGPG QVDVGRGFLE SGFDSLRAVE
     LRNRLGAATG LRLPATLIFD FPTAAALAAH LDAQLVPESA VPPVLARLDG VEAGLAGLSP
     DDPVRGLLAA RLQSLLTRLG GNGQNGGNGE NGENGAGRPG GTNAGGSGEI EAAGLEEIFD
     IVENELRNS
//
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