ID Q250A3_DESHY Unreviewed; 691 AA.
AC Q250A3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Putative anaerobic dehydrogenase {ECO:0000313|EMBL:BAE82389.1};
GN OrderedLocusNames=DSY0600 {ECO:0000313|EMBL:BAE82389.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE82389.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE82389.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE82389.1,
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; BAE82389.1; -; Genomic_DNA.
DR AlphaFoldDB; Q250A3; -.
DR STRING; 138119.DSY0600; -.
DR KEGG; dsy:DSY0600; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR Proteomes; UP000001946; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR CDD; cd02775; MopB_CT; 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; 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 13..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 691 AA; 76618 MW; 5058DF8C0BBBBE02 CRC64;
MNSDDCRGDS GMDTLHHHIC PRNCYDTCSI ISTTRHGRLV SIEGNPAHPY TRGKLCPKVM
DEIHKVYSPQ RIRYPLRQRK RFSGQWERIT WDEALETISR KILDLKDKYG TTLPLAHNKY
SGNFGILHNA LEAFLTGLGP TTRAVGSPCW SAGVEAQVFD FGAFFCSDPL DMEKAKLIWI
WGANPAWNAA HQMPIIFRAM DQGAKVICLD THFSATAARV HQFVRVNPGT DGLLALGLAK
IIVDHQLTDP ELPDYSLGYN EFIDYLKAEI DLQKCSAVTG VSLETMKELA LEYGAVKPAC
IWAGFGLQRY TNGGQNLRAI DALGALTGNI GRPGGGVQYG HFETWRFAGP LAHSQCGHAQ
DRELDINQFP QLALAADPPV KMLWIASRNP FQQDGNHAGW QKLSEALELI VVSDLFHTRS
SAAADLFLPV TTHYEHWDLH ASYWHYYIGI NEPAVESVGE ARSDLQIAWD LSKRLNQSSP
GSSAFPTEGS EKEWVLGAIG PEMLAILGID SAEELLKGPR RVNYPGTAWQ GRQFQTPSGK
YEFYAEKAQE WGLPPLPVYR PPRQAPPETP LRLLTPHHLS GLNSQVYLYS EESDSLLKAR
LHPKTAEGYG LNRGDKAILW NRGGSFPVII EPDLGIGEGV IVIYQENPPN LKSPHLNLLN
LGELTDMGKY ATGAYGLALN ETFVGIRKTT S
//
