ID Q72BM4_DESVH Unreviewed; 642 AA.
AC Q72BM4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Molybdopterin oxidoreductase domain protein {ECO:0000313|EMBL:AAS96089.1};
GN OrderedLocusNames=DVU_1611 {ECO:0000313|EMBL:AAS96089.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96089.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS96089.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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DR EMBL; AE017285; AAS96089.1; -; Genomic_DNA.
DR RefSeq; WP_010938902.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010830.1; NC_002937.3.
DR AlphaFoldDB; Q72BM4; -.
DR SMR; Q72BM4; -.
DR STRING; 882.DVU_1611; -.
DR PaxDb; 882-DVU_1611; -.
DR EnsemblBacteria; AAS96089; AAS96089; DVU_1611.
DR KEGG; dvu:DVU_1611; -.
DR PATRIC; fig|882.5.peg.1486; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR OrthoDB; 9810782at2; -.
DR PhylomeDB; Q72BM4; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 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.
PE 4: Predicted;
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:UP000002194}.
FT DOMAIN 5..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 642 AA; 69887 MW; 70B5B6D9BB0D6E1F CRC64;
MAAHPLRAIG ACTLDCPGCC SLVVTTDAEG KPHVSGNPDH PFTQGSICRK GRRMFERLHA
PDRVTTPLVR QGDALRPASW DEALGLCATR IDALRDMPER ILHIRGFGFR GALAEASRYL
FRSLGASATR GSLCDEAGLA ASELDFGDND QHAPADLANA SAIVNWGKDL TRSSHHLSLI
VRERRKAGIP VLTISPGGDA NDAFTDARIR IRPGTDRFLA AAALRRMVIA GDIPPPVIAA
CTGFEHLRAL LLAHEESDLL HTCDARPTDL ELLLRWFRSN GGRTATLLGW GMQRHVAGGE
NVRWVDALAM LSGNVGHAGG GVYYGISSSR NIDARWGKEA GTPARTLCLP LLAHELEQAD
PPVDFVWVDG SNVVNQIPEA TRAAKAFERC GFKVVVDAFL TDTARRADVV LPCALLLERE
DILGSYQHDN VQYAAAIFPP PGAAREDFDI IRDLGARLSS PVALPPREDI LRRAIDTPNL
EVSLEELRER GFSTADRPQV AYEGMRFAHD DGKFHLVDRL SPEPALTQEY PLYLLTVVRA
THLHSQMPED AQQGQPTVHV APDCTTLAHL DITRPARLVS PYGEMPVRVE TLPGLHPDAV
MMGRGGWLAT GWCPNVLIGA RLTDVGEGAA YYSQTVRLEK MD
//
