UniProt: A0A0K2B0Q6

Database: UniProt
Entry: A0A0K2B0Q6_STRA7

LinkDB:  A0A0K2B0Q6_STRA7 
Original site:  A0A0K2B0Q6_STRA7

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (49)   
   InterPro (26)   
   Pfam (11)   
   PROSITE (5)   
   SMART (7)   
Literature (1)   
   PubMed (1)   
All databases (60)   

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ID   A0A0K2B0Q6_STRA7        Unreviewed;      3724 AA.
AC   A0A0K2B0Q6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:AKZ58672.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:AKZ58672.1};
GN   Name=srm10 {ECO:0000313|EMBL:AKZ58672.1};
GN   ORFNames=SAM23877_5627 {ECO:0000313|EMBL:AKZ58672.1};
OS   Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS   NBRC 12836 / NRRL B-2516).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=278992 {ECO:0000313|EMBL:AKZ58672.1, ECO:0000313|Proteomes:UP000061018};
RN   [1] {ECO:0000313|Proteomes:UP000061018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL
RC   B-2516 {ECO:0000313|Proteomes:UP000061018};
RX   PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA   Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA   Leblond P.;
RT   "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT   spiramycin producer.";
RL   J. Biotechnol. 214:117-118(2015).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP012382; AKZ58672.1; -; Genomic_DNA.
DR   STRING; 1889.SAM40697_5121; -.
DR   KEGG; samb:SAM23877_5627; -.
DR   Proteomes; UP000061018; 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: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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08952; KR_1_SDR_x; 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; 2.
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; 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; 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; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 2.
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; 2.
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; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
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; 2.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:AKZ58672.1};
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:UP000061018};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AKZ58672.1}.
FT   DOMAIN          35..461
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1450..1525
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1544..1971
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          3558..3633
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          462..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3724 AA;  388274 MW;  1C2FA7763731DDCB CRC64;
     MSATNEEKLR EYLRRAMADL HSARERLREV ESASREPIAI VGMACRYPGG VASPEELWDL
     VAAGTDAISP FPVDRGWDAE GLYDPEPGVP GKSYVREGGF LHSAAEFDAE FFGISPREAA
     AMDPQQRLLL ETSWEALERA GIVPASLRGT RTGVFTGVMY HDYGSHQVGT AADPSGQLGL
     GTAGSVASGR VAYTLGLQGP AVTMDTACSS SLVALHLAVQ SLRRGECDLA LAGGATVLAT
     PTVFVEFSRQ RGLAADGRCK AFAEGADGTA WAEGAGVLLV ERLSDARRNG HRVLAVVRGS
     AVNQDGASNG LTAPSGPAQQ RVIRDALADA GLTPADVDAV EAHGTGTPLG DPIEAGALMA
     TYGSERVGDP LWLGSLKSNI GHTQAAAGAA GVIKMVQALR QSELPRTLHV DAPSAKVEWD
     AGAVQLLTGV RPWPRREHRP RRAAVSAFGV SGTNAHVIIE EPPAAGDTSP AGDTPEPGEA
     TASPSTAAGP SSPSAVAGPL SPSSPAVVWP LSAETAPALR AQAARLRAHL ERLPGTSPTD
     IGHALAAERA ALTRRVVLLG DDGAPVDALA ALAAGETTPD AVHGTAADIR RVAFVFPGQG
     SQWAGMGAEL LDTAPAFAAE LDRCQGALSP YVDWNLADVL RGAPAAPGLD RVDVVQPATF
     AVMVGLAALW RSLGVEPAAV IGHSQGEIAA ACVAGALSLE DAARIVALRS QVIARELAGR
     GGMASVALPA AEVEARLAGG VEIAAVNGPG STVVCGEPGA LEALLVTLES EGTRVRRIDV
     DYASHSHYVE SIRAELATVL GPVRPRRGDV PFYSTVEAAL LDTATLDADY WYRNLRLPVR
     FEPTVRAMLD DGVDAFVECS AHPVLTVGVR QTVESAGGAV PALASLRRDE GGLRRFLTSA
     AEAQVVGVPV DWATLRPGAG RVDLPTYAFQ RERHWVGPAR PDSAATAATT GDDAPEPGDR
     LGYHVAWKGL RSTTGGWRPG LRLLIVPTGD QYTALADTLE QAVASFGGTV RRVAFDPART
     GRAELFGLLE TEINGDTAVT GVVSLLGLCT DGRPDHPAVP VAVTATLALV QALADLGSTA
     PLWTVTCGAV ATAPDELPCT AGAQLWGLGR VAALELPEVW GGLIDLPARP DARVLDRLAG
     VLAEPGGEDQ IAVRMAGVFG RRVLRNPADS RPPAWRARGT VLIAGDLTTV PGRLVRSLLE
     DGADRVVLAG PDAPAQAAAA GLTGVSLVPV RCDVTDRAAL AALLDEHAPT VAVHAPPLVP
     LAPLRETAPG DIAAALAAKT TAAGHLVDLA PAAGLDALVL FSSVSGVWGG AAQGGYAAAS
     AHLDALAERA RAAGVPAFSV AWSPWAGGTP ADGAEAEFLS RRGLAPLDPD QAVRTLRRML
     ERGSACGAVA DVEWSRFAAS YTWVRPAVLF DDIPDVQRLR AAELAPSTGD STTSELVREL
     TAQSGHKRHA TLLRLVRAHA AAVLGQSSGD AVSSARAFRD LGFDSLTALE LRDRLSTSTG
     LKLPTSLVFD HSSPAALARH LGEELLGRND TADRAGPDTP VRTDEPIAII GMACRLPGGV
     QSPEDLWDLL TGGTDAITPF PTNRGWDNET LYDPDPDSPG HHTYVREGGF LHDAAEFDPG
     FFGISPREAL AMDPQQRLIL ETSWESFERA GIDPVELRGS RTGVFVGTNG QHYVPLLQDG
     DENFDGYIAT GNSASVMSGR LSYVFGLEGP AVTVDTACSA SLAALHLAVQ SLRRGECDYA
     LAGGATVMST PEMLVEFARQ RAVSPDGRSK AFAEAADGVG LAEGAGMLLV ERLSEAQKKG
     HPVLAVVRGS AVNQDGASNG LTAPSGPAQQ RVIREALADA GLTPADVDAV EAHGTGTPLG
     DPIEAGALLA TYGRDRRDGP LWLGSLKSNI GHTQAAAGVA GVIKMVLALR HGELPRTLHA
     STASSRIDWD AGAVELLDEA RPWLQRAEGP RRAGISSFGI SGTNAHLVIE EPPEPTAPEL
     LAPEPAADGD VWSEEWWHEV TVPLMMSAHN EAALRDQARR LRADLLAHPE LHPADVGYTL
     ITTRTRFEQR AAVVGENFTE LIAALDDLVE GRPHPLVLRG TAGTSDQVVF VFPGQGSQWP
     EMADGLLARS SGSGSFLETA RACDLALRPH LGWSVLDVLR REPGAPSLDR VDVVQPVLFT
     MMVSLAETWR SLGVEPAAVV GHSQGEIAAA YVAGALTLDD AARIVALRSQ AWLRLAGKGG
     MVAVTLSERD LRPRLEPWSD RLAVAAVNGP ETCAVSGDPD ALAELVAELG AEGVHARPIP
     GVDTAGHSPQ VDTLEAHLRK VLAPVAPRTS DIPFYSTVTG GLIDTAELDA DYWYRNMREP
     VEFEQATRAL IADGHDVFLE SSPHPMLAVS LQETISDAGS PAAVLGTLRR GQGGPRWLGV
     ALCRAYTHGL EIDAEAIFGP DSRQVELPTY PFQRERYWYS PGHRGDDPAS LGLDAVDHPL
     LGSGVELPES GDRMYTARLG ADTTPWLADH ALLGSPLLPG AAFADLALWA GRQAGTGRVE
     ELTLAAPLVL PGSGGVRLRL NVGAPGTDDA RRFAVHARAE GATDWTLHAE GLLTAQDTAD
     APDASAATPP PGAEQLDIGD FYQRFSELGY GYGPFFRGLV SAHRCGPDIH AEVALPVQAQ
     GDAARFGIHP ALLDAALQTM SLGGFFPEDG RVRMPFALRG VRLYRAGADR LHVRVSPVSE
     DAVRIRCADG EGRPVAEIES FIMRPVDPGQ LLGGRPVGAD ALFRIAWREL AAGPGTRTGD
     GTPPPVRWVL AGPDALGLAE AADAHLPAVP GPDGALPSPT GRPAPDAVVF AVRAGTGDVA
     ADAHTVACRV LDLVQRRLAA PEGPDGARLV VATRGAVAVR DDAEVDDPAA AAAWGLLRSA
     QAEEPGRFLL VDLDDDPASA RALTDALASG EPQTAVRAGT VYVPRLERAA DRTDGPLTPP
     DDGAWRLGRG TDLTLDGLAL VPAPDAEAPL EPGQVRVAVR AAGVNFRDAL IALGMYPGEA
     EMGTEGAGTV VEVGPGVTGV AVGDRVLGLW DGGLGPLCVA DHRLLAPVPD GWSYAQAASV
     PAVFLSAYYG LVTLAGLRPG ERVLVHAAAG GVGMAAVQIA RHLGAEVLAT ASPGKWDALR
     AMGITDDHLA SSRTLDFATA FTGADGTSRA DVVLNSLTKE FVDASLGLLR PGGRFLELGK
     TDVRDPERIA AEHPGVRYRA FDLNEAGPDA LGRLLRELMD LFAAGVLHPL PVVTHDVRRA
     ADALRTISQA RHTGKLVLTM PPAWHPYGTV LVTGGTGALG SRIARHLASR HGVRRLLIAA
     RRGPDGEGAA ELVADLAALG ASATVVACDV SDADAVRGLL AGIPADHPLT AVVHSTGVLD
     DGVLPGLTPE RMRRVLRPKV EAAVHLDELT RDLDLSAFVL FSSSAGLLGS PAQGNYAAAN
     ATLDALAARR RSLGLPSVSL AWGLWSDTSR MAHALDQESL QRRFARSGFP PLSATLGAAL
     FDAALRVDEA VQVPMRFDPA ALRATGSVPA LLSDLVGSAP ATGSAAPASG PLPAPDAGTV
     GEPLAERLAG LSAEERHDRL LGLVGEHVAA VLGHGSAAEV RPDRPFREVG FDSLTAVELR
     NRMAAVTGVR LPATLVFDHP TPAALSSHLD GLLAPAQPVT TTPLLSELDR IEEALAALTP
     EHLAELAPAP DDRAEVALRL DALADRWRAL HDGAPGADDD ITDVLSSADD DEIFAFIDER
     YGTS
//

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