ID   Q24Y26_DESHY            Unreviewed;       791 AA.
AC   Q24Y26;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Putative anaerobic dehydrogenase {ECO:0000313|EMBL:BAE83066.1};
GN   OrderedLocusNames=DSY1277 {ECO:0000313|EMBL:BAE83066.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83066.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE83066.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE83066.1,
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; BAE83066.1; -; Genomic_DNA.
DR   RefSeq; WP_005814601.1; NC_007907.1.
DR   AlphaFoldDB; Q24Y26; -.
DR   STRING; 138119.DSY1277; -.
DR   KEGG; dsy:DSY1277; -.
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          22..79
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   791 AA;  88777 MW;  A11C0F8C281A7C41 CRC64;
     MEFKNDLGKP WKYEEDGFTV IRTSVWSPPG CHPVGCGLKL YVNQAGILEK IEGDENDPIT
     KGRLCVRCLD LKEVIYNPSR ILYPMKRHPQ DRGKADKWER TTWEEAYAMI KQKRDFVIKN
     YGVEAIAAYS GTGRNGGIMV QEFAHEVLGT PNACYTQSGY ACYTPRAAAT AAITGCYYPE
     IDYGGGVEGT YDNPDYKIPE VIVLWGKEPL PSNGDGLFGH ALIDLMKRGT QIISVDPRVN
     WLATRSAVHL RLRPGTDAAM GMAWLNVIIN EELYDRDFVE NWCYGFDELK ERVADMTPEK
     AAEICQVDGE IIRKAARMYA GAAQAGIAWG LAIDQNQNGT QAAQCILSLI AITGNLDKPG
     GQLVGEAKSA VPEAEDGMTS TYAATGHQLD GWVALGEELR NKTIGMQEYP LYVNSIRNAH
     ADLMLDCLMT DKPYRIVMAM IQSTNIIAPT NSAESKKWHQ ALKRLDFVFA TDVFMTPTIQ
     ACADLFLPLK CAPEHDSINY THYSGSQIHF GITNKAIEVG QCKSDVEIAV ELGKYLGREQ
     YVTRHTDEKA WLNNRRAQRN LMGGGKEDFD TIREKVHIQQ GRKYYKYKTG HLRPDRQTGF
     LTTTGRVELY SYMFEGVGSD PLPYYQEPPF SPYSTPELAK EYPFILTTGA RTYAYFHSEH
     RQVPLLRELN PNPLLEVNPE DAAALGLLEG QWVEISNQFG EAKFKAKVTP TVRQGTVMAQ
     HGWWFPEQEA DEPNLSGVWH SNVNTLIPNH YNGSLGFGAP YKCMICKITP LKESYDVDMN
     RFQEKFRKVA G
//