ID A0A1V4DBL9_9ACTN Unreviewed; 2484 AA.
AC A0A1V4DBL9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Hybrid non-ribosomal peptide synthetase/type I polyketide synthase {ECO:0000313|EMBL:OPF83730.1};
GN ORFNames=VT50_0202710 {ECO:0000313|EMBL:OPF83730.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF83730.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF83730.1, ECO:0000313|Proteomes:UP000033615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:OPF83730.1}.
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DR EMBL; LAKD02000004; OPF83730.1; -; Genomic_DNA.
DR RefSeq; WP_046087921.1; NZ_LAKD02000004.1.
DR OrthoDB; 3488622at2; -.
DR Proteomes; UP000033615; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR024011; Biosynth_lucif-like_mOase_dom.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 985..1059
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1083..1513
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2009..2084
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 961..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2103..2119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2484 AA; 263556 MW; 122184EE9DEC6B34 CRC64;
MTFAQERLYF TGEAEGHDTY LVAVAMLIDG DLDVEALHRA VQEVTARHDA LRATFVFEGG
ALLQRIGDRL GEPSWTVTEA DPAAERSAAV RELVTQLNAP PFDLAAGPLV RWGLTRIGPA
AFGLALVAHH IVCDGWSLGV IFRDLETIYA ARVADRDQQL FDGQAPSPLV WAARERALWT
QGDASSADLD FWRGHLAGMS PLALPTDLPR PAVPSGAGGS LLVPLDEELV TRLRATAQRA
GATVFMAFAA IYATVLGRYA RQDDVVISSP VAGRNSEEEQ DLVGCHVNMV PLRLDVSGRP
GFTDLLRRTR SAVLPAMARQ NVPVDVLVRE LGLRGAAGRS PLMQCSLAVQ NFDAGLPELA
GVTVTDVEVH SDRAKWDLAL TVDLSGESPS LRLEYDADIL VASSAGTLVR HLESALRHAV
EFPERPLRMV DAEEAEYLTL GANPPPAAAE TQTVLARFRR ARTAHPDHPA LTDGRTTLTY
AELDAHADRV CRDLRSAGVV PGTRVGVCGQ RSPWTVVAML AAWKAGATYV PLDPAGPSER
LRSITSRAQV GLVMADRASR PVVREWLPAL DCLVPDAQEH RTAPTAAAPT AADAVGGLPL
EESDPAQAAY VIFTSGSTGE PKGVEVPHSN LSQLFADRPA GLETDATDVW LCTHSFAFDF
SVWEIWGPLT TGGTCVIAGQ DQVRDPTALA AVVLQRGVTV LSQTPGSLYR LAPALTAAAR
PNDSKLRYIV LGGEALDWDR LALLLGDSDL AATVVNMYGI TEGTVHVTVR RVPAAELGSV
RANSIGVPLP QARCYVLDEY GEPAGLDVPG ELCIAGGHVA RGYLNDSEQT AERFTPDPFH
ASGTIYRTGD LARWRTGGEL EYLGRNDDQV KVRGYRVEPA EIERAVLRLP GPRPSACAVL
AHDDTLVAFV VVDGPLPETE LREHLRSVLP PYLRPSRFVQ LESIPLTPNG KADRALMRGL
LSTGPREEPP GQASTAAAPP KPGRRDLADL TRTVLATWQA VLVQSDIGLD DNFFDVGGHS
FALLEVHEAL GRAGLEISVN DLFRHTTVRA CARFLHGTYG TSPSAGTQPL PADRPSGRRR
PVDGRIAVVG MAARLPGTGE DLDAFWRMVL SGEHAAARFG EEELRAAGVP RSSLEAAGYV
PVRAVLDDVR AFDRTLFGYS PLEASLLDPQ QRILLECAWR ALEDAGYAPA GPEENRTAVF
TGIGGNAYLQ EVLADPKTAQ NAGPLQVAIA GDKDFASTRI SYKLNLQGPS VTVQTACSTS
LVATHMAVQS LLSHESDLAL AGGCSLAPPS QHGYVHEPGG IFSPDGLCRP FDEHAQGTIP
GDGAGIVVLK RLEDALADGD TVHGVILGSA VNNDGARKVG YTAPGPAAQT QVIRAALDAA
GVPAESIGLV EAHGTATRLG DPVEVSALRE VFLGQARDAQ SPPLYVSAVK SNTGHLDAAA
GVVGLIKAVL AVHHGTVPPI ANFTRPAERL ASEGTALRFP ATPQPWPQGP APRRAGVSSF
GIGGTNAHVI VEEPPAQPAV APQPAAPQLL TLSAADEAAL GRAVNRLADH LEANPDLSLA
DVAHTLRVGR AVLPWRAALV TADTARAPAL LRRTALGRAR ATAGSGTVLM FPGQGTQRPG
MGRTRYDADP VYRACADEGL EAVDPALRQQ VADALLARPD SAQPDAPDGS VSTLLAQPCL
FLDQVATALS LTARGLEPRA LLGHSLGELS AACAGGVLTL ADGMTAVTAR ARLMQAAPPG
AMTTVIASAD QVTHLLAEGA AGGADPPHEE AAGLVVAAHN GPHSTVVSGP PESVAAFTDR
CRAAGLTTVA LRTTRAFHSP GMAAAAADFA EVMAGIGLNT PSTPLFSAAT GRRLDDSQAI
DPQFWASQIR LPVRFSDAVR AASDELSPAV WWETGAGSTL QGLVSDILRD RTPLLGGFDR
PRHGGSLASG LEAIGELWRR GLGELRRGEA ESARRVSLPT YSFTRERCWI EPEATVPAPR
ASGTAQHMEI DEPSDVKEDV KEEETAMSKV TGDTDSVLSA LWCEVLGVEA VSPEDDFFDQ
GGHSLAALRL SARIRDALGL EISLDSFFDE STFGGLAQVV RDRLGSAAPT APPAAQTPAA
PVTAAPAPAP APAPAPKEHR PATPADNLTT SVYFFSSAQG DLGSDYDLIL AAAREADALG
YEAIWTPERH FHEFGAQYPN PAVLSAALAA STERIHIRAG SVIPALHNPL RLIEDWRIVD
RISGGRIGVS FAPGFHPSDY VLAPDRFAGR RDTFEADVRR LGTLWSDGVA TDAVDGTGGR
IQVSLYPKPV QPELPTWLTA TSNDESFRRA GTLGANLLTA LLELKVDELA DKIRIYRKAR
EEAGHDPGTG RVTLMVHCYV GESEDMVEEV CHDPFLRYLR SHTQLLGTLT AALPQEQIDL
DRASPKDVDA ILRRAYRKFR GERALLGDPV TVRQRCELLR EAGVNEIGAL VDFGLTQRQV
LGSLRRLAQL RDEMAGADAG TATR
//
