ID G2NJK5_STREK Unreviewed; 1803 AA.
AC G2NJK5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:AEN13370.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:AEN13370.1};
GN ORFNames=SACTE_5579 {ECO:0000313|EMBL:AEN13370.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN13370.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN13370.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN13370.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP002993; AEN13370.1; -; Genomic_DNA.
DR RefSeq; WP_014049320.1; NC_015953.1.
DR STRING; 862751.SACTE_5579; -.
DR KEGG; ssx:SACTE_5579; -.
DR PATRIC; fig|862751.12.peg.5789; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_5_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
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; 1.20.5.1140; Docking domain of the erythromycin polyketide synthase (DEBS); 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; IPR036347; DEBS_docking_sf.
DR InterPro; IPR015357; Erythronolide_synth_docking.
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; IPR036299; Polyketide_synth_docking_sf.
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; PF09277; Erythro-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; SSF101166; Docking domain A of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 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 ECO:0000313|EMBL:AEN13370.1};
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:UP000001397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEN13370.1}.
FT DOMAIN 33..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1649..1724
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1803 AA; 188957 MW; 972F3A3EBEB390E7 CRC64;
MNNEEQLLDY LRRTTADLRE ARRRLRENEQ RAHGPVAVVG IGCRYPGGVT SPEDLWNLVA
TGTDAVAEFP GDRGWDVEAL YDPDPDRPGT TYARTGGFLY DAPDFDYDFF GISPREALAM
DPQQRLLLET SFEAFERAGI VPASLRGSRT GVFAGVMYND YATRLDTVPD DLDGYLANGS
AASIASGRVA YTFGLEGPVV TVDTACSSSL VALHWAVRAL QAGECSLALA GGVTVMSTPE
TFVDFSRQRG LAPDGRCKAF STAADGTGWG EGAGMLLVER LADARRNGHP VLAVVRGSAV
NSDGASSRLT APNGPSQQRV IRQALAGAGL TAADVDVVEA HGTGTSLGDP IEAQALLATY
GREHPADRPL LLGSVKSNLG HTQAAAGVAG VVKMVMAMRH GEVPPTLHVD TPTDQVDWDA
GAVELALEKR PWPETGGPRR AAVSSFGISG TNAHVVLEQA PLEEEPGTGT APAPAGAEPR
ASAIAATPVP WIVTGRSPEA LAGQIARLRE HLTGRDDAPA DIALSLATTR THFEHRAVAV
GQDTGALLDA LATASPLTPV GGRTAFLFTG QGAQRPGMGR ALHRAHPVYA EAFDAVCALA
DPHLERPLGE VIDGDPALLT RTDYAQIAIF ATEVALYRLL ESWGVVPDYL AGHSVGELAA
AHVAGVFSLP DAVSLVLARG GLMAALPAGG AMAALRATEE EVAPYLDERV GLAAVNGPRS
VVVSGTEEAV DALAARFERA KRLTVSHAFH SPLMDPMLDA FAEAASRCDY REPRIPVVST
LTGVLTTPGE LTTPGYWVDH VRRPVRFAPA LATLHDLGVR AFLEVGPDAA LTSAAAECLP
PDSVCVPGLR RDGDETHDVV TSVARLHAAG GRVDWKAFHA PHHARRTDLP TYAFRRTRLW
LEAAPGGTGD AEGLGQEATG HPLLTAATEL PDTQGTVLTG RLSLSSQPWL GDHAVHGTVL
LPGTAFVEMA LRAAAQTGCD TVGELTLHAP VTLPEHGSVA VQVAVGAERD GRRELTVWSR
RTDTPWTRNA GGFLATTADE APPADPGTWP PAGAEPVDLD GLYTQLARTG YGYGEVFQGL
RAMWRRGEEL YAEAALPDGA RATAGAFGLH PALLDAALHV NLLDLPGGQA VLPFAWSGVT
LHRTGTDRLR LRLSPAGNDA VRLDLADQHG TPVATVRGLV ARPVTADQLT ADADDPLYRV
DLVPVTGAAH PAPSGLAVCG ADAGLDAPRY RDLAALADAG EVPDTVVLAV PADAVAGADL
PRRARELVGT TLERLRHWLD DARFTGRRLA VLLRDDHLAH APLFGLVRAA AAENPGRFLL
IGTDGSAAPD AALATALASG EPETVVRDGE VRVPRLARAK PGGPRGWDPD GTVLITGGTG
GLGALIARHL VTEHGVRRLL LAGRRGPDTP GAAELRDQLA TLGAEVTLAR CDVADRADLA
DLLDRHPVRA VVHAAGVVDN GVLTSLDADR VERVLRPKVD AAWHLHELTR ESDLSAFVLL
SSAAGLLVGG GQANYAAANT FLDGLAAHRR SLGLPAVSLA YGLWEADGGM SAGIDAADLE
RLRRLGLPPL APAQGLRLFD AALGAEDALV VPVRLDGAAV RARPDGVPAL LRGLVRPAAR
TPGAGATDGP PSAPWRERLA GLPDTERDRA LLDLVRTHVA RVLGHPSPQS VDPGRAFQEM
GFDSLAAVEL RNLLAGATGL TLPATLVFDQ PSPRTLAAHL KTELVPGPAD LTRSALADVD
RVEAALLALP DEDGSHARVT ARLEALLRGW QDARDAAPES PQDFGEASDA ELFARIDNEL
GAL
//
