ID A8FSU5_SHESH Unreviewed; 829 AA.
AC A8FSU5;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family protein {ECO:0000313|EMBL:ABV35918.1};
DE Flags: Precursor;
GN OrderedLocusNames=Ssed_1307 {ECO:0000313|EMBL:ABV35918.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35918.1, ECO:0000313|Proteomes:UP000002015};
RN [1] {ECO:0000313|EMBL:ABV35918.1, ECO:0000313|Proteomes:UP000002015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35918.1,
RC ECO:0000313|Proteomes:UP000002015};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV35918.1; -; Genomic_DNA.
DR RefSeq; WP_012141654.1; NC_009831.1.
DR AlphaFoldDB; A8FSU5; -.
DR STRING; 425104.Ssed_1307; -.
DR KEGG; sse:Ssed_1307; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000002015; 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.
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:UP000002015}.
FT DOMAIN 38..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 829 AA; 92171 MW; 9CDFEB9C23DF38D3 CRC64;
MQRREFLKLS AAASAVTCVT ACGSKKTETI IPEVPVSEKH FWSACLGNCG SNCPLKVITV
DGKITRIEPE TYGEDSFDSP HIRPCLRGHA NRARVYNPDR LMYPMKRIAN AKRGEGKFER
ISWEQATSEI GMKLKETYDQ YGPRAVYQNR GSGAFYDING KYAWGRLLNC MGGGLKHYGS
YSSSMVRTIM PYIFGSRKSS TPREMKYSDL LVFFGYNPLE TRMSGSGEGF EVQTVTEGKK
VIHIDCRYSD SAMGRESEYY PCRPGTDAAL CEAMAYVLIT EELLDEQFLS DKCYGFRAEP
SIQDARDSSK MLPEVVYEDS YEAHILGVKD GQPKTPQWAA EICGIPADSI RNIARQIGNA
KAPYLAPGLG MQRHINGEDN IRSVMTLGML VGAIGKRGTN TGDYPKSPRK IYSKGLPTVS
EQQEVSIDDA KISMFSWTQA VENGENLTVL RDGVKLPAEE LDENGDGKLG TNIKAIINFA
SGCLVNQHGD AFGTTRILQD ESKCEMIVVI DNHMTSSAKL ADYILPDNTW LESTDFANKT
YYAGAVSYMT ALKTGIKPLG ECRGSFDVCT DLAEKMGVKE IFTEGRTTDE WIEHYYQTKV
RTLDPELFPA TAKEMQDIGV VKTFSPCDDS EESAKVNCAM WDYVQNGGTL KTASGKLEIF
SHALQELSDL WEVPDYWLDK DNYLNAIPKY WVGLESYQDP SPELKDKPLQ LIGHHTKART
HSTFGSVKWL KEAVNGDAVW INPDDAIKYG IVDDQYAIIE SLRGKVKVKA RVTNRIMPGV
MSLSQGAWFD PKNDVDVGGC VNALTSQGRP SPLAKGNPQH TNRVRIYKA
//
