ID B8DS21_DESVM Unreviewed; 820 AA.
AC B8DS21;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family {ECO:0000313|EMBL:ACL08560.1};
GN OrderedLocusNames=DvMF_1612 {ECO:0000313|EMBL:ACL08560.1};
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL08560.1};
RN [1] {ECO:0000313|EMBL:ACL08560.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL08560.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001197; ACL08560.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DS21; -.
DR STRING; 883.DvMF_1612; -.
DR KEGG; dvm:DvMF_1612; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR OrthoDB; 9810782at2; -.
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 CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
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; IPR006311; TAT_signal.
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; PS51318; TAT; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 54..115
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 820 AA; 89043 MW; 1FEEFD01EB37B4CD CRC64;
MPAGTGPQDC AARGLDRRTF LKWCALLGGA AMLPGGLAGL CPAVAEAAGG GEPQDFVWSS
CNVNCGSRCV LRAMVRDGAI VRMDTDNLGS DDYGTHQIRA CLRGRAMRQR VYAPERLKYP
MLRTGKRGEA AFRRATWDEA LDVIAAKMKD IKERYGNEAF YLNYGTGNLG SVMSKSWPTD
QTPITRLMNC YGGYLNHYNT YSTAQIATSM PYLYGGGLGN ALSDIVNSKL VVLFGNNPAE
TRMSGGGVVY DIQRAKRESN VRVIVIDPRY TDTAVAVADE WIPIRPATDA ALAAGIAYVL
FTEGMADRSF MDTYCVGHDE AHLPEGVPAG SSYEAYITGK GPDGVAKTPG WASAICGVPV
DTIVRLAREI GTAKPCCISQ GWGPQRHHNG ETNCRAIAVL AALTGNVGIS GGNTGAREGG
YSIPFPGFPT LKNPVAASIS FFLWTDAIVR GPEMTAERDG VRGVPRLNVP VKFIWNYAGN
ALINQHSDIN RTAQILSDDT KCEMIVVVEN FMTPSARFAD VLLPAVTNLE ENDFAHQGST
AEMGYVVFAQ KAIEPLFESR SVYDMCADIA ERLGVREQYT EGRTRDQWLQ KILTDARQKL
PDLPATLEEA WKLGVYKVRN PGKPFVAYKA FRDDPVANPL ATPSGRIEIF SKRLWDIGHK
WELPAGERIT ALPEYDEAAE GQGDPLRKKY PLQLVTHHYK QRTHSTYGNV PWLKEAAPQT
VWVNPLDAAD RGLAHGDMVR VFNDRGATVL PVKVTPRIMP GIISIPQGAW YTPGAGGTDF
GGSANILTSL RPSPLAKGNP QHTTLVEMAR HSGGSHANAS
//
