ID A0A1V2RU11_9ACTN Unreviewed; 755 AA.
AC A0A1V2RU11;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase {ECO:0000313|EMBL:ONK15940.1};
DE EC=1.7.2.3 {ECO:0000313|EMBL:ONK15940.1};
GN ORFNames=STBA_67830 {ECO:0000313|EMBL:ONK15940.1};
OS Streptomyces sp. MP131-18.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK15940.1, ECO:0000313|Proteomes:UP000189065};
RN [1] {ECO:0000313|EMBL:ONK15940.1, ECO:0000313|Proteomes:UP000189065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP131-18 {ECO:0000313|EMBL:ONK15940.1,
RC ECO:0000313|Proteomes:UP000189065};
RA Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT "New natural products identified by combined genomics-metabolomics
RT profiling of marine Streptomyces sp. MP131-18.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:ONK15940.1}.
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DR EMBL; LZNS01000001; ONK15940.1; -; Genomic_DNA.
DR RefSeq; WP_077062738.1; NZ_LZNS01000001.1.
DR AlphaFoldDB; A0A1V2RU11; -.
DR STRING; 1857892.STBA_67830; -.
DR Proteomes; UP000189065; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ONK15940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189065}.
FT DOMAIN 10..48
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 51..505
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 617..729
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 81030 MW; 50147DDFF36A6A7E CRC64;
MNGPPGGRPH SSHWGAFHAV HDADGLRVRP DPADPEPSPL LDNLPGFTRA RVTRPHVRRG
WLTGGPGPDT ARGTDDFVPV DWAEVVPLLA GELDRVRTVH GNRAIFGGSY GWGSAGRFHH
AQSQVHRFLN ALGGYTRSVN TYSLGASRPL LRHVVGSDAP IAEPTTYPVL AEHTRLFVCF
GGMPAKNAQV NAGGVSRHGA AGHLRAARAR GARFVLVSPL RDDLTDDLDA EWLAPEPGTD
TALMLALAHV LLTEDRHDEG FLARHVTGFD AFRGYVLGHT DHVPKTPDWA AAICGIPAAR
IASLAREMAA TRTMISLSWS LQRAHRGEQP LWAGVALAAL LGQIGLPGGG FGHGYGATAG
IGAGVLPYRL PTLPQGINPV PDFIPVARIA DLLLNPGGRC DYDGQRLTYP DIRLVYWSGG
NPFHHHQDLA RLRRAFTRPD TVVVHEPYWT ATARHADIVL PATTTLERED IGGAKEDPVL
IAMHRIAEPQ GQARDDYAIF AALAAELGVA EEFTQGRTAR QWLAHLYESW RAGLAPEHAP
AEDFAAFWHA GRVPLRGRRE RHTLYAAFRA DPDAHPLPTP SGRIELFSRT IDSFGYDDCP
GHPAWLPPAP PDPSFPLHLI ANNPATRLHS QLDHGPHSAA SKIDGREPLR MHPGDVAAFG
LRPGEVIRVR SAVGSCLAAV VPSDALRRGV VQLATGAWFD PSAPGTATCV HGNPNALTAD
VGTSRLAQGC TGQLARVTVE RLAAPPPPVR AHGPA
//
