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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//