ID R4KIV2_9FIRM Unreviewed; 692 AA.
AC R4KIV2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AGL03148.1};
GN ORFNames=Desgi_3836 {ECO:0000313|EMBL:AGL03148.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL03148.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL03148.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL03148.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003273; AGL03148.1; -; Genomic_DNA.
DR RefSeq; WP_006520545.1; NC_021184.1.
DR AlphaFoldDB; R4KIV2; -.
DR STRING; 767817.Desgi_3836; -.
DR KEGG; dgi:Desgi_3836; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 219031at2; -.
DR Proteomes; UP000013520; 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 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 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:UP000013520}.
FT DOMAIN 6..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 692 AA; 77676 MW; 8A2C9539819CCD20 CRC64;
MTAANRKTFY TGCVLCYHSC GAEVTVEDGR VVKVSGLKSH PLNKGELCPK GEAMIEQLYH
PDRLKYPLKK VDGKWERITW EQALSEIAFK LNDLKEKYGP SVNAFFCGSI GVESLEMVSL
THRFRAALDS PQFFSVESIC YRMRIRSRQI TFGKYPVEEM DSSLYVLWGH NPDASDFPLS
LSIKENLKKG SKVVVIDPRK IPLADQAEMY MAIRPGTDGA LALALINVII NEKLYDADFV
EKWTYGFDQL VPHIQQYTPE WAEGITGVRA DDIRALARLF SKTKGASIYQ GTCTQDQSAN
GSQTDRAIAI LQSITGNINV PGGWVISPRL RLANISLPCE GKPLGADKYP LFYELWGRTS
PYAVQNMVPE SIPDKLKSFI VVGGNPLVTM PDSNALKEAY RKLDLLVVYE MFMSETAQEA
HYVLPAAHQL EYCSLAYNYN VCHSMPYVML REKAIEPYYE SKSILSFYTE LAQACGIGDK
FHWKSDEELV AEEIAPSGVD FETLSQNRGG VYYKERSYGI DEKTFATPTG KIEIYSQAYK
DVGFDPLPTY LEPSKSPQGP LWKELGDKYP LVLSTGTRSL IYNNSQLHNI KALQLEEPYP
KAEIGPQTAA KYGVSHEDDV IIETDRGWVK MKAHVDERIM EGVVLVPHGW HGEANCNRLT
DCQCREPIMG YPQFKGLLCN IRKAGEPQLA GN
//
