ID B8J3R0_DESDA Unreviewed; 631 AA. AC B8J3R0; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=Carbon monoxide dehydrogenase {ECO:0000256|PIRNR:PIRNR005023}; DE EC=1.2.7.4 {ECO:0000256|PIRNR:PIRNR005023}; GN OrderedLocusNames=Ddes_0382 {ECO:0000313|EMBL:ACL48295.1}; OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48295.1}; RN [1] {ECO:0000313|EMBL:ACL48295.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL48295.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Hazen T.C.; RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. RT ATCC 27774."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4; CC Evidence={ECO:0000256|ARBA:ARBA00000152, CC ECO:0000256|PIRNR:PIRNR005023}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; 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; CP001358; ACL48295.1; -; Genomic_DNA. DR AlphaFoldDB; B8J3R0; -. DR STRING; 525146.Ddes_0382; -. DR KEGG; dds:Ddes_0382; -. DR eggNOG; COG1151; Bacteria. DR HOGENOM; CLU_030631_0_0_7; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-EC. DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-UniRule. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro. DR CDD; cd01915; CODH; 1. DR Gene3D; 1.20.1270.30; -; 1. DR Gene3D; 3.40.50.2030; -; 2. DR InterPro; IPR016101; CO_DH_a-bundle. DR InterPro; IPR010047; CODH. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR InterPro; IPR011254; Prismane-like_sf. DR NCBIfam; TIGR01702; CO_DH_cata; 1. DR PANTHER; PTHR30109:SF4; CARBON MONOXIDE DEHYDROGENASE; 1. DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR SUPFAM; SSF56821; Prismane protein-like; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR005023, ECO:0000256|PIRSR:PIRSR005023-1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR005023}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR005023}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR005023}; Nickel {ECO:0000256|PIRSR:PIRSR005023-1}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR005023, KW ECO:0000313|EMBL:ACL48295.1}. FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 52 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 55 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 60 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 77 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 268 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 304 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 342 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 450 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 480 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" FT BINDING 521 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT /evidence="ECO:0000256|PIRSR:PIRSR005023-1" SQ SEQUENCE 631 AA; 66614 MW; B2E9C4CEEA0ADAE2 CRC64; MDDRQTDINN MSIWEDAQKM LHKARAEGIE TAWDRLAQQT PHCRFCELGT TCRNCVMGPC RISAKAAPGG KLSRGVCGAD AHVIVARNFG RFIAGGSAGH SDHGRDVIET LEAVVEGKAE GYEIRDPAKL LRIAGELGIA VDGLAVNEVA ALVVDACYSD FGSRRGAVNF ISRVPAKRRQ VWEKLGITPR GVDREIAEMM HRTHMGCDND APNTMLHAAR CALSDGWAGS MIATELCDIL FGTPSPRMST VNLGVIKKET VNILVHGHNP VVSEMILAVS REPEVLEQAR QAGAAGITVA GLCCTGNELL MRQGIPMAGN HLMTELAIVT GAVEAVVVDY QCIMPSLVQV AACYHTRFID TAPKARFTGA VHMNFTPENA RQEASAILHM AIEAFAARDP GRVDIPVSPV NIMTGFSNEA ILEALGGSLD PLLDAVKAGT VRGFAAVVGC NNPKVRQDSA NVGIIKELIK KDIMVLVTGC ITTAAGKAGL LLPEGAAMAG PGLQKLCASL GIPPVLHMGS CVDNARIMHL CGLIANSLGV DISDLPVVAS APEWYSEKAA AIGLYAVASG VYTHLGLPPN ILGSDVVTDI ALNGLEGLVG ASFVVEADPV KAADLLDRRI RTKRSALGLD A //