ID A0A3S9PE18_STRLT Unreviewed; 3681 AA.
AC A0A3S9PE18;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=SDR family NAD(P)-dependent oxidoreductase {ECO:0000313|EMBL:AZQ70589.1};
GN ORFNames=EKH77_04590 {ECO:0000313|EMBL:AZQ70589.1};
OS Streptomyces luteoverticillatus (Streptoverticillium luteoverticillatus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66425 {ECO:0000313|EMBL:AZQ70589.1, ECO:0000313|Proteomes:UP000267900};
RN [1] {ECO:0000313|EMBL:AZQ70589.1, ECO:0000313|Proteomes:UP000267900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 15060 {ECO:0000313|EMBL:AZQ70589.1,
RC ECO:0000313|Proteomes:UP000267900};
RA Feng Z., Chen G., Zhang J., Zhu H., Yu X., Zhang W., Zhang X.;
RT "The whole draft genome of Streptomyce luteoverticillatus CGMCC 15060.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP034587; AZQ70589.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000267900; 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: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; 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; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 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; 2.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000267900};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..468
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1407..1482
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1502..1928
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3514..3589
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2483..2508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3469..3496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..39
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2485..2508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3681 AA; 387227 MW; 0C974FA7D8656714 CRC64;
MHVSSTAPAS NEEKLREYLR RAMTDLHEAR ERIRQVESSR SEPIAIVGMG CRFPGGVTSP
EGLWDLVASG TDAISPFPVD RGWDVEALYD PVPGRPGRTY SREGGFLHDA GDFDAAFFGI
SPREALAMDP QQRLLLETSW EALERAGIDP HTLRGSRTGV YAGVMYHDYG TSVADTAEAE
VGGFLGTGTS GSVFTGRVSY TLGFEGPAVT VDTACSSSLV ALHLAVQALR NGECDLALAG
GVTVMAGPGT FVEFSRQRGL AADGRCKAFS NAADGTGWSE GAGVLAVERL SDALRNGRRV
LAVVRGSAVN QDGASNGLTA PNGPSQQRVI HEALRNAGLG TGDVDAVEAH GTGTRLGDPI
EAQALMATYG KGRATEQPLW LGSLKSNIGH TQAAAGVGGI IKMVLAMQHG ELPRTLHAEQ
PSTEIDWSAG TVTLLNEPVP WPRHDRPRRS AVSSFGVSGT NAHVILEQAP EPTKADEPEN
VRALSTVPVV VSARSREALR AQARRLVDHV AAASVLDLGY STAVARSAFE HRAVVLAEDS
AALRAGLEAI AADEPSVDVV SGALVGDGGQ TVFVFPGQGT QWVGMAVPLL DESPVFAEAM
ARCEAALAGL VDWKLTDILD DEDALRRVDV VQPACFAIMV SLAELWKSMG LQPDAVIGHS
QGEIAAAVVS GALSLEDGAR IVTLRAQIIG RELAGHGGMA AIAQTPTDVE QRMTPWAGRL
HIAAVNGPNA TVIAGDPDAL AEMVTACQAE GIRARTIAVD YASHSTHVET IRAELLDALA
NIRPQASAIP FYSTVEASSL DTTALDADYW YRNLRHTVRF HDTVELLQAD GYTLFIESSA
HPVLTPTLPD AVVATGTLRR NEGNLRRFLT STAEAFTHGA PIQWPATFGE TGAHHTDLPT
YPFQRRHYWL EASQAQQESL SYQVAWKHLP FTGSARLTGR WLLISPTGRE TDLGQALTTH
GATVTHLTID PTTTDRAALA TLLTAHHDQP VTGIVSLLGL AATVALTQAL GDSGLDAPLW
TITRGAVAVT PGEAPDPEAA QLWAFGRVAA LEHPDRWGGL IDLPHTPTPR TTDHLTQALT
NTNTEDQIAL RPSGAYGRRL VRVPVARTAD EGRQPRGTVL LVGDTTPVAE QLVRRLLAQG
AERVLIADPS LTDLPGTLTD LAPRAAVAAG AEVTDRASLA ALLDEHSPTT VVIAPPQAAP
TPLATTTPAE FAAAVAAKTT TAALLDALLT PGEGTEAGSD AAHDVPEFVV FSSVSGVWGG
ARQGAYAAGT GYLDALAERR RARGLPAVSV AWTPWSGGVT AEGTSAEAMR RYGIAPLEPQ
AALAELERAL ARGAGSVAVV DVDWERFLTS FTSVRPTALF DELPEARRMQ AAGTTTADGP
GVADTSPGSG TELARVLRAL PVTERDKTLM DLVASHAAVV LGEGSATAVD PDRAFKDVGF
TSMTAVELRN RLKEATGLTL PASLVFDHPN PRALAGHLRT ELLGEDADVT EPTPAPAAFH
SDEPIAIIGM ACRFPGGVTT PEDLWDLLST GRDAITDLPD NRGWDLAELY DPDPDAAGRS
YVRGGGFLHD AGDFDAAFFG ISPREALAMD PQQRLVLELA WESFERAGLR PTEQRGTRTG
VFMGTNGQHY MPLLQSGTES FDGYLGTGNS ASVMSGRISY VLGLEGPAVT VDTACSSSLV
ALHLAAQALR RGECDLAFAG GATVMSSPDP LVEFSGQRAA SPDGRCKAFA DSADGFGPAE
GAGMLLVERL SDALRNGRRV LAVVRGSAVN QDGASNGLTA PNGPSQQRVI HEALRNAGLG
TGDVDAVEAH GTGTRLGDPI EAQALMATYG KGRATEQPLW LGSLKSNIGH TQAAAGVGGI
IKMVLAMQHG ELPRTLHAEQ PSTEIDWSAG TVTLLNEPVP WPQLDRPRRS AVSSFGMGGT
NAHVVLEQAP TSADERDDSA RELSSVPVVL SGRDSGALRE QARRLIDRVD AASVLDLGYS
TAVTRSVFEH RAVVLAKDST TLRAGLEAIA SGTPSSDVVT GVVTGGGTPR SVFVFPGQGT
QWAGMAADLL DESPVFAAAM ARCEALLAEH LDWNLTDLIR QTDNAPSLER EDVVQPACFA
VMVSLAELWK SMGVEPHAVI GHSQGEIAAA VVCGALSLED GVRVVALRAR LIERELAGHS
GMLSLTLPLA ETEQRITGWG DQLSVAVIAG PTSTVIAGPL DQIETALTAC ETEGIRARRV
PISYASHTPH TEPIRNELIH TLHNIRPQAS TIPFYSTVEA APIDTTTLNA TYWYRNLRET
VRFHDTVELL QADGYTLFIE ASAHPVLTPT LPDNITATGT LRRNEGDLRR FLTSTAEAFT
HGAPIQWPAT FNATNAHHTD LPTYPFQRQR YWYEPRSRRG DVTSFGMSAV DHPLLDGGVE
LPDGGGYLYT ARLGAETQPW LREHTLLDTP LMPGAAFVDL TLWAGGRVGC ELVEELMLAA
PLLLPESGAV RLRLVVGAAD GDGRRSVTVH SRPETGREQW EKPEESESWT RHVQATVAPA
DEARHASLPW EESSSAASTA FRPADFYASF AERGYTYGPL FQGVKAGHDD GTAAYSEVAL
PEGAATAGPD RFGIHPALLD AAFQTMNLGS FFPHDGQVRM PFALRGIRLY ATGAERLRVR
VTAAGDDAVR IEGVDEGGRP VCVIDSLAVR AVPAEQFQLP GRPARGLGDG MLHRVEWPAL
SLPSAGSPSA PHWTLIGGDV FGLAEGLSTA GVPFTAVTTL TEAVEGVENL EDADDSPTGV
IAVSVPRSPS TDPGAVRGAV HNALELLQEL QAADTGQRLV FVTSGAVAAG RGDRLGDPVA
AAVWGLVRSA QSEQPDRFVL VDVEEAGSVD GAALAAGLAS GEPQMAIRAG KVRVPRLATI
PEEDAEALLP PAGARSWQLV GGSGTISELA LVPTAADTVP LGPGQVRIAV RAAGINFRDT
LIALGMYPGE AVMGAEGAGV VTEVGPEVSG LAVGDRVLGM WTDAFAPYAV ADHRMVAHMP
RGWSYAEAAS VPAVFLSAYY ALKHLAGLRP GQSLLVHAAA GGVGMAAVQL ARHFGAEVYG
TASPGKWDVL RAQGLDDRHI ANSRTLDFAE QFLEATGGRG VDVVLNSLAG PFVDASLRLL
PRGGQFVELG KADVREAERI AAEQPGTGYR VLELMEHGPG LIGEMLAELL ELFERGVLRL
LPVAPYDLRN AREAFRTLSQ AGHIGKLVLT MPAAFDAHGT VLITGGTGNL GGTLARHLVT
EHGVRHLLLM SRRGAQAEGA GELAAELRGL GASVTVAACD AADRAALREL LAAVPPEHPV
TAVLHAAGVL DDGVVTSLTP ERIDGVLRPK ADAALNLHEA SLDPDLGLDL SVFVLFSSVA
ALLGGPGQGS YAAANGFLDA LARYRRDRAL PGLSLGWGLA GSGQLTAHLD TEELHRRMAR
GGLLPLSGEQ SMALFDTAQR VDEAFQAPVR LNIAALAAGG NVPPVLRDLL PDAAGDPGRG
SDGASRPASG AAPADGAEAL VERLSSLGAA EQRELLLETV RTHAAVVLGH TEPEGILGER
AFKDLGFDSL TAVEMRNRLA AATGLHLAAT LVFDNPTPAA LAEHLRERLA PETAPAAPLL
AELESLEAVF KGLAADDVAS LAPDGITRRE IAARLAALGS RWSALQGDGA PQEEDRSIVE
EIDTADDDDL FAFLDEKLGG S
//