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Database: UniProt
Entry: A0A4Y6I7X2_9GAMM
LinkDB: A0A4Y6I7X2_9GAMM
Original site: A0A4Y6I7X2_9GAMM 
ID   A0A4Y6I7X2_9GAMM        Unreviewed;       838 AA.
AC   A0A4Y6I7X2;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Dimethyl sulfoxide reductase subunit A {ECO:0000313|EMBL:QDF65735.1};
GN   ORFNames=FJQ87_02760 {ECO:0000313|EMBL:QDF65735.1};
OS   Shewanella sp. SNU WT4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=2590015 {ECO:0000313|EMBL:QDF65735.1, ECO:0000313|Proteomes:UP000316850};
RN   [1] {ECO:0000313|EMBL:QDF65735.1, ECO:0000313|Proteomes:UP000316850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SNU WT4 {ECO:0000313|EMBL:QDF65735.1,
RC   ECO:0000313|Proteomes:UP000316850};
RA   Oh W.T., Park S.C.;
RT   "Complete genome sequence of Shewanella sp. SNU WT4 isolated from diseased
RT   rainbow trout.";
RL   Submitted (JUN-2019) 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP041151; QDF65735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y6I7X2; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000316850; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.12440; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR011888; Anaer_DMSO_reductase.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR   PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316850}.
FT   DOMAIN          41..102
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   838 AA;  91284 MW;  BE9088CC2C897957 CRC64;
     MERRSFLKMS AAMSCAATVT GCNSSSKDAN LVPPQPPVSE EAINWSSCLV NCGSNCPIKV
     FSRDGVITRV ETDHEVDDVY GLHQVRACAR GRSLRQRTYA PDRLKTPMKR VGKRGEGKFV
     PISWDEATSI VAENLQRVIN QYGNQAVFRS YGSGAYYGFA SNANFNRLFN LVGGCLNAYG
     NYSWAQQMEA AQHTFGTGST MGSSTSTIAD SDFFLGVAYN PSEIRQSGSG EGYDFLQALQ
     KNNDLKVVMI DPRYTDSMLG KESMWLPIRP GTDAAFAEAV AYQMISTDWV AKNSLDFINT
     HVVGYDAASI AVQQAKFEAS NDATKQEYAK IMDSQDNYHD YILGLNKFAG PARTPEWAES
     ITGISADKIR EVADDLMAAK APYIVIGAGV NRQANGEQSM RALYMLSVLT GKLGTRGASN
     GELPYMSGMG RAGIPTGSNP VEESISFFTW SEAIVNGKDF TARTHGLRGV KGLDTKLGTN
     IHFILSASDS SLLNQHAEIN NTAQILRDAE DLFVVSCDCW MTPGAKFADI ILPDTSWLES
     NDLVDNSYAA GALGYLTAMS AAVEPMWDCK SMHDAAAMIA DKMGVGPQFT EGKTEAQWLE
     ELYQKTRVMS QNQGVVPPFP ATYKEAQAQG LFRKDMQLNH VALADFVHEG KALSTPSGKI
     EIYSAELAWR AANWNTEDKT GVKGDTITAI PQYTVTWDGY EDAETSVAYP LQLASYHTKG
     RTHSSYHNVP WLREAVEDAL WINQFDANAY GLKSGDKVEV YNARGSIEVP VKITPRVAPN
     VVALGQGAWY LADAKGRVGA SGKVIDVGGA VNSLTRYQPS PVAKGNPQLT IRVQIKKA
//
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