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Database: UniProt
Entry: R4KLX7_9FIRM
LinkDB: R4KLX7_9FIRM
Original site: R4KLX7_9FIRM 
ID   R4KLX7_9FIRM            Unreviewed;       834 AA.
AC   R4KLX7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AGL00646.1};
GN   ORFNames=Desgi_1121 {ECO:0000313|EMBL:AGL00646.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL00646.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL00646.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL00646.1,
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; AGL00646.1; -; Genomic_DNA.
DR   RefSeq; WP_006523661.1; NC_021184.1.
DR   AlphaFoldDB; R4KLX7; -.
DR   STRING; 767817.Desgi_1121; -.
DR   KEGG; dgi:Desgi_1121; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   OrthoDB; 9803192at2; -.
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; -; 2.
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:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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          12..68
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   834 AA;  94675 MW;  D725F2DF92CF7774 CRC64;
     MAKVATHTKS GDKWVRSACK MCLHGCGIKV RVKDGVILKI EGDPDNANNM GKLCPKGQSG
     IMRHYDPNRI KTPVRRTNPQ KGPGVDPKWE PISWNEALDI VGKRLKKIRS EDPRKLLVAI
     NDFQRIHLWG WGAAFGTGHY FNTVGQFCGA AYHPFCGFFD GSFACANDYK YCNYWIQIGG
     GDGFGAHLHL SGSIKRMADA RVNRGLKLIG VDPRMASYCA KADEWVPIIP GTDRAFILGM
     VYVILYELDR YDAEFIKKYT NGPYLIKPDG RYFRDKETQK PMVWDSVDNR AKVYDDPTIK
     DFTLEGYFKI DGIKVRPGFQ VIKDTLKDHT PERMSKICDV SPGTMRRIAR EFVEEARIGS
     TIMIEGKEYP YRPAAINFYR GAIGHYDGTL DHAAIKLMNS LVGNIDVPGG HLGVGLDHRL
     LIVEPGEDGM LKPQPHILHP GVPFAYPPQT LQMIEYFPMG LDPGHLVCHN ILHPEEWGFD
     FKPEAALIFH SNPLKNINGY PKVLEVFKQL EFIVAIDILA NESTEWADII LPDHDYLEST
     MLTLCEPPEV TGHTLRKPVV EPLYDSRDGH DILTDISERC GCLNELNGLL NFTMFIKPEY
     ALKPGRKYSH LECIDRMAKS IYGEHMGLKW FQENNNAVRP QKPEECYLPW KGNRISFYHE
     YFLQVAEELQ EQFRAVGREW DTSSYLAVPV WREEHPLHKI PGEYDLYAIN FKAEAMLNHC
     ENTTIPWIKE LVSNIPIHKG VLINTKTAQA KGIKTGDRIS IESPFGKVEG LARVIEEIHP
     RVIGISNAIT RWTIHPVERK MNVNFNHLLP GNLEFTDLAS GHQETATKVR ISKI
//
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