ID   V6JKJ1_9ACTN            Unreviewed;      1055 AA.
AC   V6JKJ1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
DE   Flags: Fragment;
GN   ORFNames=N566_28205 {ECO:0000313|EMBL:EST20437.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST20437.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST20437.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST20437.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) 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:EST20437.1}.
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DR   EMBL; AWQV01000918; EST20437.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6JKJ1; -.
DR   STRING; 1380770.N566_28205; -.
DR   HOGENOM; CLU_290288_0_0_11; -.
DR   Proteomes; UP000017915; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
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; 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; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017915}.
FT   DOMAIN          1..202
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EST20437.1"
FT   NON_TER         1055
FT                   /evidence="ECO:0000313|EMBL:EST20437.1"
SQ   SEQUENCE   1055 AA;  109475 MW;  BEE099EE244F1E54 CRC64;
     EGVGVLVLER LSDARRNGHT VLALVTGSAT NQDGASNGLT APNGPSQQRV IRQALATAGL
     TTADVDAVEA HGTGTSRGAR HRHHGTGTSL GDPIEAQAVL ATYGQNRDAD RPLWLGSVKS
     NLGHTQAAAG VAGVMKMVLA MRHETLPKSL HISEPSSHID WSAGAVELLA EPRPWQRTDR
     PRRAGVSSFG ISGTNAHVII EEAPEPDEET PGRTGGSLPA VPWLVSSRTA AGLADQAGRL
     LAGPADPGSG AEPLDVALSS ATTRAALEHR AVVIGADPAG LRAGLEALAA GEAASGLIRD
     AVAGEGLTAF VFSGQGGQRT GMGRELAEAF PAFDDALREV CAHFDAVLEL PLREVMYDDP
     EGVLKQTGWA QPALFAVEVA LFRLAESWGL RPDYLAGHSV GELAAAHVAG VLSLEDACRL
     VTARASLMQA LPAGGAMWAV RATREDVEPH LVDGASIAAV NAPGQVVVSG AREAVEQVAS
     ALPERQSRWL EVSHAFHSVL MDPMLEDFRK AASAVTYGRP RIPVVSTLTG EPVREFTADY
     WVDQLRGTVR FADASARLAA EGVTRFVELG PDATLVAAIE ETNGDVLAVA LLRRDRPEPA
     TTVTALARLW ANGGTVDWTA FFAPTGARVT DLPTYAFQHR SYWPQPPVAV PGDVTAAGLA
     DAGHPLLGAA VTLAGDGGHL FTSRLSLRDH AWIADHDVLG TVLFPGTGFL ELALRAAAEV
     ACEQVEELTL AAPLVMPQDG AVQLQLALAA PDPDGLRTLQ IHSRAEGAAA DVPWTLHATG
     TVGGTPASAD TVDLAAWPPP GSEPLDVSGF YDMYLQGGFT YGPSFQGLRQ AWRAGDDVFA
     EISLPAGYET ETARYGIHPP MLDAAVQALT FIALDGSGES RLPFSWSGVS LYAPGASTLR
     VRLAQSGPDS LSMALADGAG RPVAHVESLA MRQVSAAQLR PAGDAYPDAM FRLDWAALPA
     GADVTAATTA DTSSWAVLGA DGPGLADALG AHSAADLAAL AGLPAPGGAD APDVVLAPCT
     GTADGDDPAT MAAEARRLSH GVLELLQQWL ADSRY
//