ID A0A438M1U4_9ACTN Unreviewed; 1867 AA.
AC A0A438M1U4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Enediyne polyketide synthase {ECO:0000313|EMBL:RVX39779.1};
GN ORFNames=EDD27_2152 {ECO:0000313|EMBL:RVX39779.1};
OS Nonomuraea polychroma.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX39779.1, ECO:0000313|Proteomes:UP000284824};
RN [1] {ECO:0000313|EMBL:RVX39779.1, ECO:0000313|Proteomes:UP000284824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX39779.1,
RC ECO:0000313|Proteomes:UP000284824};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVX39779.1}.
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DR EMBL; SAUN01000001; RVX39779.1; -; Genomic_DNA.
DR OrthoDB; 4537517at2; -.
DR Proteomes; UP000284824; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 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; 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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; 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 SUPFAM; SSF47336; ACP-like; 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; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000284824};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 927..1003
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 901..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1867 AA; 197362 MW; 2A2313248665E82C CRC64;
MTDAIAIVGM GCRYPDASDP GQLWENVLAC RRSFRPIPRE RLNLEDYAPD GGDADSTYVR
FAGVLEGWQF DRARFRIPGS AHRVTDTTHW LALDVAADAL AAAGYPDARG LDRDRVAVVL
GNSMNGEFSR AVGLRVRWPY VRRVLQGALA EEGWTDEQRA GFLAAAEQAF KAPFPEPNDE
SLAGALANTM AGRVCNHFDL HGGGYTVDGA CASSLLAVTT ACSTLLAGEA DFVLAGGVDI
SLDPFELVGF ARTGALATSD MRIYDASPTG FWPGEGCGMV ALMRWEDAMA AGRTPLALIR
GWGVSSDGRG GISRPEKNGQ LLALWRAYTR AGWGPETISL FEGHGTGTAI GDEVELSALI
EAHRCLRRDQ AAALGSIKAN IGHTKAAAGV AGLLKATLAL QRQVIPPTTG CREPHQLLRR
DGAPLRIVSD AEPWPEAPLR AAVSAMGFGG INTHVVLESE ARRRRNGLSA AERKTATRPL
SHEAFVVGGD TVRELAGAVA RVAETAGGMA FAQHVDLAAE LAATAAERSG RFRMGIVARD
PDQLARRAVQ ALSMLDDLEG NAEGIPLMAP GIVAAHGRAA TIGLLFTGQG APPTTSAGAL
GKVLPEVESV FTSDWTLTAD TAVAQPSIVR ASLAGLKWLA KLGVRAEAAV GHSLGEITAL
HWAGALSETD LLDLVTRRGR LMSELGTPGS GMVSIAASAA SVAEFIDDTS LTIAADNGVA
QVVAGPLPDI EKVLERAARA GVTAQRLRVS HAFHTQEMKA VEHPLSEHLS RMAIRPVERR
VYSTISGRLL TPAHDLRRLL TLQVTSPVHF GRAVTALAAE CDLLVEVGPG QGLASMAAAQ
TSVPAVALGV GSASAEGLCL AGAALYAAGA ISDLRPFFAE RFHRPFDLDR APEFLSNPCE
RAAEPAPRSE RPSPGEADHV GEADRVDDVP AMVRALVADA LELPSDAIAD DDRLLSDLHL
NSLRVAQLSL QAVTAAGRAM PIEPLIMSDV SVADLARAIE ALPAGGDGDE AAASLPGLAD
WHRILLPTAE PVTLPEQAET YAWQVVGAGP LLHGLASLLP VPSAERSAML IFLPEDPTDS
DVDVMVSSVR AAVAEGMPLT VVDHGDTASG LLATIRQEYP GQVARWIGVA DCHSPGALLR
VLRSSGEETP EILLDSAGRP CVPAYRPIAH AGDHSTLPLT AADVVLVTGG GKGIGFETAL
ALGRASAARI ALLGRSRPDS DEELRANLAK LTEAGITFVY ERADVTDAAS THRAIDVISR
TLGTITAVVH SSGVNRPQRF ADLDAAAFAD HSAPKHHGLR NVIAALDRDA LRVVISYGSV
IGRFGLGGEA HYALANGRLR EYMRILRREL PQCQVCDVDW TVWSGAGMGE RFDVLDSLMR
AGVVPLPSAK GTDLLLELLT VRPDTSSVVV TGRLPQLTCA YTAAEHRYVQ TAPFFVPGIE
LVAEAELSAE ADPYLADHRI DGLRVLPAVC MLEAMAQSAH VLTGSRPMGI ADARFDRAIL
VPDEGTRTIR LCALVREDGD IDVAVRSDES GYAVDHASAR ILMSEPPETV KVPEQRLSLP
SHDGRGLYGG LFFHGPLFQR LRGYQHLEAT GCTAVLASGP DFPFGPGLPT KLMLGDPARN
DASIHVLQAC VPQRRLLPVG CAAFIVQTTR STDGELVLSA VEREHSGADY LYDVTLRERS
GRPVLSWTGL RLRDVGPLDP AGGRPDLLLA PYLERGAAAL IPDSPVRVEV TPSGADRASA
RQNGRGRSHL DGLAMAVHGR GVVACDWEWA DGDPEALRGL IAWTAQAREI ARLTGEPEAH
VLTRLWTVRE CLSKTGRTGQ ASLTVAGAYE QGWVLMRAGK SHVASAIVDI GGESRPAAVA
VLVEGES
//
