ID Q185W8_CLOD6 Unreviewed; 725 AA.
AC Q185W8;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Anaerobic dehydrogenase {ECO:0000313|EMBL:CAJ69063.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CAJ69063.1};
GN OrderedLocusNames=CD630_21790 {ECO:0000313|EMBL:CAJ69063.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ69063.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ69063.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ69063.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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}.
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DR EMBL; AM180355; CAJ69063.1; -; Genomic_DNA.
DR RefSeq; WP_011861481.1; NZ_JAUPES010000011.1.
DR RefSeq; YP_001088692.1; NC_009089.1.
DR AlphaFoldDB; Q185W8; -.
DR STRING; 272563.CD630_21790; -.
DR EnsemblBacteria; CAJ69063; CAJ69063; CD630_21790.
DR KEGG; cdf:CD630_21790; -.
DR PATRIC; fig|272563.8.peg.2294; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9803192at2; -.
DR PhylomeDB; Q185W8; -.
DR BioCyc; PDIF272563:G12WB-2336-MONOMER; -.
DR Proteomes; UP000001978; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
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 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; IPR006655; Mopterin_OxRdtase_prok_CS.
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 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; PS00490; MOLYBDOPTERIN_PROK_2; 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:0000313|EMBL:CAJ69063.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT DOMAIN 36..94
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 725 AA; 82636 MW; 737E92B90B5DDB9B CRC64;
MYNKYNNLYL LLGKENVNMD SYKQLKAKIP CKETGIEIKR TLCDICSPGV HCGIDAYVKD
GKVIKIEGTK EHPMNKGLLC TKGLCNREYI YREDRIKTPL KRIGKRGEGK FKPISWDEAY
REIAEKLNRV KSEYGAKHVA FFTGYGKWYR PFLQRFASSF GSPNYGTESS SCSTSAQMAG
NVATGRNFTM QDMENAKTYL GWGFNPYYSK FLNSVNLIKL KEKGLKFIIV DPRITPTTQK
LADLHLRIKP GTDGALALGM ANLFIQKDLI DREYIEKHVH GFNEYKEYVK LFDLDTVSRI
TGVSKDNIVK AVEMLSQGPF CINESAAPIV HHQNGFQNYR AMMSLSAITG NYDRIGGNIP
KQDYFAGKIG GFQTLEKEFV KEVLPKNINE RIGGERFPLW NEMVTQFQAM DLPRQIEEKT
PYEIRALFCH GINARMFPNS GRLFKALNSV DFFVNIDLFM TDTSKYADIL LPACTSFERE
ECKSYPGGYI TYTKKVIDKL YDSKSDVEIL SDLANAMNID DDLLKAGYEA SVRHMFKNTC
VDVDKLKESD LPLKCKDFKP YIVGSYTREG YDTSTSRFEL KSTIIEKYKD FGLDALPTYR
GFNDNIDDEY THLLTSGARI SNALHSRLHD IKLSRILKNE ASCDISSLDA KELGVISGDY
IKITTKIGSL DVKVNVTDRV LYKNIHMYHG YREADINSII CDNFDPYSGF PAYRSCKCKI
EKMNR
//
