ID S5UUC4_STRC3 Unreviewed; 3118 AA.
AC S5UUC4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Type-I PKS {ECO:0000313|EMBL:AGS70773.1};
GN ORFNames=B446_19805 {ECO:0000313|EMBL:AGS70773.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS70773.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS70773.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP006259; AGS70773.1; -; Genomic_DNA.
DR RefSeq; WP_020941231.1; NC_021985.1.
DR STRING; 1214242.B446_19805; -.
DR KEGG; sci:B446_19805; -.
DR PATRIC; fig|1214242.5.peg.4055; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_8_11; -.
DR Proteomes; UP000015423; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; 2.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..421
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 951..1026
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1044..1468
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2985..3059
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 425..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2033..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3058..3094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3118 AA; 320626 MW; E67367D270A91EE8 CRC64;
MGSAGHGRRE RRSRAIAVIG IGCRFPQADG PEAFWRLLRD GGDAVTGRRD GRGPERGGFL
DRVDTFDPGF FGISRREADV MDPRQRLALE LAWEALEHAR TLPGDLSGSR TGVFLGAIGD
DFATLLHGLG PDAVTGHTLT GTQRGVIANR ISYALGLNGP SLVVDTGQSS SLTAVHLACA
SLRSGESDLA LAGGVSLILA PESTLALERA GTLSADGRCW TFDARANGYV RGEGGGIVVL
KPLDAAVRDG DRVLAVIRGS ALNNDGATET LPTPGRASQE RVILAACADA GVEPGEVRYV
ELHGSGTRAG DPVEAAALGA ALGSARTGDE PLLVGSVKTN IGHLEGAAGI AGFVKTVLCV
GERELVPSLN HSAPGERIPL DALRLRVNTE TGPWPVPEGP LVAGVSSFGI GGTNCHVILA
DRQGAEPAGG DADRPALPPS RALPPAPAGG GGAGAPAWVL SARDEGALRE QAARLRAHVE
ARPELDTASV ARSLAVTRTT FEHRTVVVAD DRDGFLDGLR MRAAGQPAAA VVAGRHDGPP
VRPVFVFPGQ GSQWAGMAAE LIDTFPVFAG RIGACAEALG PYVDWSPLDV LRGVRGAPPL
ETDDVIQPVL WAVMVSLAAL WRSAGVEPAA VVAHSQGEIA AATAVGALSL ADGARLVALR
GRTLHRIAGR GGMLSVELPA AQVRRDVAAV AAPLSVAAVN GPAQTVVAGP GFALDALAAH
YGDRVRTRRL RVDYASHSAD VEDLREDLLA AFAGITPRSV DVPFHSTVTA APVDTAELDA
GYWFRNMREP VRFGPAVERL LDAGHSTFLE ISPHPVLTTG VRQAIDLRGG DGAALSTLRR
GHGDRQRFLT SAAEAFVRGV AVDWAALLPG SAPLTDLPTY PFQRVSCRPA RSPGVAGRVP
DPTGVPAPAP AAGADGPWVP EPAAGADGPS VLSAVGADAP SVLSAVGADG PSVLELVRSL
TAVVLGAATA ADVPPGRSFR DLGLDSVMTL ELRDRLSAAT GLKLDSTVLY DHPSPAALAA
AVDGLRTGAA AGDAPAAAPE RADDDPVVVV GMACRFPGGV HSPEDLWHLV DTGTDAIGDF
PDDRGWDLAT LHHPDPERTG TSYVRQGGFV RDAADFDAEF FGISPREALA MDPQQRLLLE
VAWEALERAG IDPTALKGSR TGVFAGAMHS GYGPAMEAAG HGVAGHLLTG TGTSVISGRI
AYVLGLNGPA LTVDTACSAS LVALHQAVRA VRSGECSLAL AGGVTVMATP GMFVELSRQR
VLAADGRCKA FSARADGTGW GEGAGMLVVE RLSDARRRGH PVLAVVAGSA VNSDGASNGL
SAPSGVAQQR VIADALADAG LAPRQVDAVE AHGTGTALGD PIEANALLAA YGRDRDRPLW
LGSLKSNIGH AQAAAGVGGV IKMVQALRHA TLPATLHAEE PSPHVDWASG PLSLLDRARP
WPDTGGPRRC GVSSFGISGT NAHVILAEPP APAGPAEEPV RPPVVPLVLS ARTPDALREQ
ARRLAAAPLD PVAAAPALTA RAALGERAVV IAGDRREAGH GLAALARGEE TPHVVVGRAG
EPGRTVLVFP GQGGQWRGMA AELAAESPVF AARLAECERA LAPYVDWSLA DVLAGAPLLD
RVDVVQPALW AVMVSLAELW RSAGVVPDAV VGHSQGEIAA AVVAGALCLD DGARAIALRS
ALAVDLMGTG AMAVVPLPVE RVRERLGALS VAAVSGPATT TVAGAADAIA DLVDAYRAEG
VNARVVPAAF ASHSPAVEPI RERILDGLAP LAPRTGEIPL MSSVTADWQD GGALDASYWY
RNLRHTVRFQ EAVEALIASG HTTFVEAGPH PVLTGSIGQI LEKAGTGGIV TGSLRRDDGG
LRRFLTSAAE AHVRGLPLAW ERLTGTAAGH VELPTYPFQR RRHWLTGASG PSATAALGQA
PAGHPLLGAA VELGDGETVF TGRLTTRSHP WLADHTLSGT IVLPPTLFLE TALHAGAHAG
TPRIEELTVS PLVELPEDGA VDLRVRVSGE DGDGRRACRV SGRATGGEWA EYATGTLGPA
PATAPARATV DRPPADATPV PPARLYEDLA LRGHEHGPVF QGLRTAARRD GERFAEAVLP
EPEAAQAGAY HLHPALLDAS LHGLVADAAA REGRCVQPLR WRGVSLSGTG GRTSLRMHAT
PAAAGGLRLT LADGSGEPAG LVESLELCPV AAARPADPAA VARGSLFALD WEPLSEPTAV
PPTGPVPVPW DAFAPDALAA EPAEHAVVAC PAGERGTDPA TAARGAVRRT RELLGRWLAE
DRLAGSRLVL VTRGAVAVRP GETVRDLAQA AVWGLVRTAQ VEHPGRFFLV DLAPDAAEVP
AAALVPDENQ VAVRDGAVLV PRFAPAAGDP ALPLPGDAPD WRLDIPERGT LTSLELRPCP
EAAAAPGPGQ VRLAVRAAGL NFHDVLGALD MHPGDPGPLG LEGAGVVTAT GPGVTGLAPG
DRVMGLFSGA FGTVAHADHR TLVKIPEGWS YTRAAAVPVA HMTAVHALAE LGGVRPGDPV
LIHAGAGGVG MAAVQLARHL GAEVHATASA AKWPALRALG VADDHLASSR EPGFGERFGA
GGRRMAVVLN SLTGELVDES LRLLRPGGLL VELGRTDPRD PAEVAAAHPG ARYRASNLLR
LPPEHLGRLL NRVVELFAEG AFTWPAVTDL DVRRAPEAFG LLRRGAHVGK VVLTVPPVLD
PDGTVLITGG TGAVGRAVAR HLVTAHGARR LLLAGRRGGD APGAAELASA LEALGAEVRF
AAVDVADRDA VAGMIEAVPG RHPLTAVVHA AGVVDDAPVT SLTPAQIDRV MRVKADGAWH
LHELTAGHPL TAFVLVSSIM GTLGGAGQGG YTAANAFLDA LARHRRARGL PALALTWGLW
DDPDGMIGSL TAADRARFAR AGLVAMAPEY GLALLEAALP SPHAVLAPAR LDHEALRALG
QDLPPVLRAV VAAAGAGRPG GLPGHRRQRP LREELTALAA AERAALLAEV IRGHMAAVLG
SRPEAIPDDR SFGELGFDSL TSVEFRNRLN TATGLTLPLT LLYEAPTLPG LVALLDGELV
PDGETPDGET PDGGTPADGT PAAPEDTSGD PGADVAALVD AATAEELLDF IDRELSGS
//
