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Database: UniProt
Entry: A0A101QYY7_9ACTN
LinkDB: A0A101QYY7_9ACTN
Original site: A0A101QYY7_9ACTN 
ID   A0A101QYY7_9ACTN        Unreviewed;      1887 AA.
AC   A0A101QYY7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KUN38633.1};
GN   ORFNames=AQJ30_13915 {ECO:0000313|EMBL:KUN38633.1};
OS   Streptomyces longwoodensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN38633.1, ECO:0000313|Proteomes:UP000053271};
RN   [1] {ECO:0000313|EMBL:KUN38633.1, ECO:0000313|Proteomes:UP000053271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN38633.1,
RC   ECO:0000313|Proteomes:UP000053271};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT   for the species Streptomyces longwoodensis.";
RL   Submitted (OCT-2015) 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:KUN38633.1}.
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DR   EMBL; LMWS01000015; KUN38633.1; -; Genomic_DNA.
DR   RefSeq; WP_067233225.1; NZ_KQ948552.1.
DR   STRING; 68231.AQJ30_13915; -.
DR   Proteomes; UP000053271; Unassembled WGS sequence.
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:UP000053271};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          34..461
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1729..1804
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          462..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1887 AA;  195904 MW;  0F8D868334316062 CRC64;
     MAENEEKLLA YLKRVTGDLR QTQRRLREAE AAHSEPVAIV GMACRYPGGV DSPEGLWDLV
     ARGGDAVTGF PTDRGWDVEG LYDPDPARSG GNYVRGGGFL DGVTDFDAGF FGISPREALA
     MDPQQRLLLE GAWELFERSG IDPASLKGSP TGTFIGFSSM DYGWELPRIP ESVEGYFATG
     NFASVMSGRI AYTFGLEGPA VTVDAACSSS LVALHLAAQA LRSGECSLAV AGGVTVMSTA
     VGYAEFSRQR ALSPDGRCRA FSASADGFGP AEGLGLLLVE RLGDARRNGH RVLAVVRGSA
     VNQDGASNGL TAPNGPSQER VIRAALRNAR VSPDEVDAVE AHGTGTPLGD PIEAHALLAT
     YGERRPQERP LWLGSVKSNI GHTSAAAGVA GVIKMVQALR HGVLPRTLHA DEPTPHVDWS
     PGTVRLLTEP RPWPDTGDRP RRAGVSAFGI SGTNTHVILE QAPATPPDDT ESAPAPGTPS
     GLTATAVPLP LSARSAPALR AQAERLTAYL TAHAEAPLDG IGRTLATARA ALDHRAVLLA
     TDRDQTLTAL AAVSAGNPDA HVVQGVALTD GTEQELAGRV VFVFPGQGSQ WVGMGAGLWE
     SSPVFRERLA ECDAALSALV DWSVTDVVRG LPSAASLDDV VVVQASLWAV MVSLAAVWRS
     VGVEPGAVIG HSQGEIAAAV VAGGLSVEDG ARVVVLRAQA IAESLSGNGG MVSVAVSADR
     VRELIARWGE RISIASINGP TSTVVSGEPG ALDELTAACE AEGIRARRIA VDYASHSAQV
     ESIRDQVVEA LKNIEPGPAQ VPFYSTVTGA VIDTSGLDAT YWVTNLRQEV RFDATVRELL
     TDGFGYFVEC SPHPVLTVGM QETFEDHADA QAAVALGTLR RDEGGPERFL TSLAEGYVRG
     LTVDWIALFA GTTDAEPLLD LPTYAFQRRR YWLDGGAAAV TDPSGLGLAD AGHPLLGATV
     HVADDERKLL TGLLSRRAQP WLADHVVHGT ALVGGATVAE LALAAAAQAG AELVEALVVE
     APLPLPEKDG VQIQLSLGAP DTDERRELAL YARPGDALPD TPWTRHARGT VATSTSPTEP
     PAEEPFGTWP PEGAVPVGTG GAYERLEPVG YGYGPAFQGL RAVWRRGEDL FAEVALPDEQ
     ARDAGAFGLH PALLDAALHP ALLDHLDGAD DTGLRLPAEW HGLALHAVGA TVLRVRIRPT
     GPGAVSLLLA DAAGNPVASV DEVRLSEHAP EDVAGAARSL RDALFRLEWT PFDRPLPAVA
     PAGWTVVGPD ELGIGAGAEQ DAEPSLALAS FVSSAEGAPG AALAPRVHEA ATAALGLVQK
     WLADERSEAV PLVLVTGGAV AAAPGDRVTD VVNAPLWGLV RSVQAEYPAG RFLLVDVDGH
     EASRTALAAA AAAALEAGEP QLAVRNGTAL VPRLVRAEAP TQDTATPFSA SGTFPASGTF
     PASGAFPTSG TVLVTGGTGT SGARVARHLV AAHGVRHLLL IGRRGPDTPG ATELLDELHA
     LGADTVDLVA CDAADRDALA DVLASVPASR PLTAVVHAAG VLDDALTTSL TAPQLERVLR
     PKADAALHLH DLTRDRELSA FVLFSSAAGT LGNAGQANLA AASTVLDALA EHRRALGLPA
     VSLAWGPWTT EGNEEEDGGA AGGGVLPFSP SEGLALLDAA LADGAALAVP VRLDLPALGA
     AAAAGTLPAA LRRLVRVPAR RAAASGPGTA ADTGLARELA AAPEAERRRI LLDLVRTEVA
     AVLRHATVDD VEADRAFKEL GFDSLTAVEL RNRLGAATGL RLPPTLVFTY PNPTALVRFL
     LDEIAPGAGE GATTPVLAEL DRLDADLSGL TPDDATRDRI TRRLEALLWK WSGEPDGEEA
     VLGRETLEDA SDDEMFALID QELGEAG
//
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