COOS_METJA
ID COOS_METJA Reviewed; 624 AA.
AC Q58138;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Carbon monoxide dehydrogenase;
DE Short=CODH;
DE EC=1.2.7.4 {ECO:0000250|UniProtKB:Q9F8A8};
GN Name=cooS; OrderedLocusNames=MJ0728;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP REVIEW.
RX PubMed=11841199; DOI=10.1021/bi015932+;
RA Lindahl P.A.;
RT "The Ni-containing carbon monoxide dehydrogenase family: light at the end
RT of the tunnel?";
RL Biochemistry 41:2097-2105(2002).
CC -!- FUNCTION: CODH oxidizes carbon monoxide coupled, via CooF, to the
CC reduction of a hydrogen cation by a hydrogenase (possibly CooH).
CC {ECO:0000250|UniProtKB:Q9F8A8}.
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:0000250|UniProtKB:Q9F8A8};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9F8A8};
CC Note=Binds 3 [4Fe-4S] clusters per homodimer.
CC {ECO:0000250|UniProtKB:Q9F8A8};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Evidence={ECO:0000250|UniProtKB:Q9F8A8};
CC Note=Binds 2 [Ni-4Fe-5S] clusters per homodimer.
CC {ECO:0000250|UniProtKB:Q9F8A8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9F8A8}.
CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster
CC C is a mixed Ni-Fe-S cluster is to be the active site of CO oxidation.
CC Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges
CC the two subunits of the CODH dimer. {ECO:0000250|UniProtKB:Q9F8A8}.
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: This protein lacks the conserved Cys in position 45; it is
CC replaced by a Tyr. It is therefore possible that the D-cluster is
CC either altered or missing in this protein, which may not form
CC homodimers. {ECO:0000305}.
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; L77117; AAB98724.1; -; Genomic_DNA.
DR PIR; H64390; H64390.
DR RefSeq; WP_010870233.1; NC_000909.1.
DR AlphaFoldDB; Q58138; -.
DR SMR; Q58138; -.
DR STRING; 243232.MJ_0728; -.
DR PRIDE; Q58138; -.
DR EnsemblBacteria; AAB98724; AAB98724; MJ_0728.
DR GeneID; 1451605; -.
DR KEGG; mja:MJ_0728; -.
DR eggNOG; arCOG02429; Archaea.
DR HOGENOM; CLU_030631_0_0_2; -.
DR InParanoid; Q58138; -.
DR OMA; PEYMEQK; -.
DR OrthoDB; 5135at2157; -.
DR PhylomeDB; Q58138; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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-EC.
DR GO; GO:0050418; F:hydroxylamine reductase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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 PANTHER; PTHR30109; PTHR30109; 1.
DR Pfam; PF03063; Prismane; 1.
DR PIRSF; PIRSF005023; CODH; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR01702; CO_DH_cata; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..624
FT /note="Carbon monoxide dehydrogenase"
FT /id="PRO_0000157143"
FT BINDING 37
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:0000250|UniProtKB:Q9F8A8"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 256
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 292
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 336
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 444
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 475
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 516
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
SQ SEQUENCE 624 AA; 67408 MW; FFB6AA3376D1050E CRC64;
MKNCIAAIPE VKEMVEKAKL KGIETPHTRF PNQFPKCPYG LKGVYCILCA NGPCRITEKT
PYGVCGATAD VIVARNLCRA VAAGTSCYVH CAENAARALL SAGKGEGSYE IRNEKKLKFL
AKKLGFDANK DAKQLAVEVA EFILDDMYKP RWEKSELVPK LCPEKRLEVF EKLDILPGGA
KGEIVDALTK TSTNLNSNPM DLLVHCLRLG LHAGFTGLLM TCWLNDILFG SPKITVVENG
FSSVKPNNVN IMITGHQHAL IQPLCEAAME EDLIKMAKEA GADEIKIIGA TCNGQDMETR
IAHLPESFVG YIANNFTTEP LVATGLIDAV VSEFNCTFHG LKFVAEKTKT KLICIDDMAY
VEGAEYIPWE PENAKEKARE IIKKAIEAFK ERKGMQKDYY DEKVKSVVGV GEESLVEFLG
GSVKPLIELI ASGKIKGVVG VVGCSNLASG GHDNIIVTLT KELIKRDILV LAGGCVNSPL
KHAGLFDPAS AELAGENLKE VCKSLGIPPV LNFGACLSIA RIEQVAVAIA EELGVDIPDL
PVAASAPQWL EEQALADATY AVDMGFTVHV SPVPFVTGSE LVTKVLTEAV EGLTGGKLIP
EPNPYKAADL LEQTIMEKRK KLGI
