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}.
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; 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
//