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Database: UniProt
Entry: Q24Y27_DESHY
LinkDB: Q24Y27_DESHY
Original site: Q24Y27_DESHY 
ID   Q24Y27_DESHY            Unreviewed;       750 AA.
AC   Q24Y27;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Putative anaerobic dehydrogenase {ECO:0000313|EMBL:BAE83065.1};
GN   OrderedLocusNames=DSY1276 {ECO:0000313|EMBL:BAE83065.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83065.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE83065.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE83065.1,
RC   ECO:0000313|Proteomes:UP000001946};
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(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; AP008230; BAE83065.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24Y27; -.
DR   STRING; 138119.DSY1276; -.
DR   KEGG; dsy:DSY1276; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02759; MopB_Acetylene-hydratase; 1.
DR   CDD; cd02781; MopB_CT_Acetylene-hydratase; 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   InterPro; IPR041930; Acetylene_hydratase.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
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   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.
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:UP000001946}.
FT   DOMAIN          19..75
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   750 AA;  85103 MW;  A2C2B646FEC8EAF2 CRC64;
     MKQMAVKYKK GTEKDYTVRT CAWSAPGCHP TGCGLLMHVK DGKLVEVEGD PEHPVSQGRV
     CVRCLSLPEA VYHPDRILYP MKRAGKKGED KWERITWDEA YDLIEEKVRY YQKQYGPESI
     AMMGGTGREA TFYFPALSYA VLQTPNNVGV LSGLSCYGPR CAVTEYVLGA GYPEIDYAAY
     FADRYDNPEF QLPEYIIIWG KSPLESNSDG FFGHAIVDMM KRGTKIIAVD PRVTWLTSRA
     EYHLQLRPGT DAALALGMLN VIINEDLYDH EFVEKWTFGL DALRERVQEY SPRRVADICW
     IKEETIVQAA RAFAQAGNSS IQWGVALDMN WNGIQAIQGV LYLMTLTGNL DVPGGNTLAE
     PASFMGKWRY DTHKQIPEEI YENRIGNKEF PFFNYGLMAC SPDNTLEYFE QQQPYPIKMV
     WSNSQNPLAN AAPVPKRWYE AFKKIEFWVC QELFMTPTVA AYADIVLPIA TFAEHDGVVI
     PHFGRNSAFL GAVNQCIERV GECKSDLEIC FELGKRLNPQ AWPWQTVSDF FTEQIEEKTG
     LDYPGLKDKV VQQQHYVYRK YEQGLLRSDG EPGFETLTGL IELKATIFES WGEDPLPYFQ
     EPPFSPYRTP ELFAQYPLVL TTGGRKFTSF HSEHRQIPSL RQITPWPTVE IHPDTAAGLG
     IQDGDWVAIE NHLGQCRMKA LVQPTVHPKV VHALHGWWYP EQAGTEPNLF GTFKSNINML
     MPHKKIGKLG LGANYKSNLC KVYKVSGLDD
//
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