COOS_ARCFU
ID COOS_ARCFU Reviewed; 622 AA.
AC O28429;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Carbon monoxide dehydrogenase;
DE Short=CODH;
DE EC=1.2.7.4 {ECO:0000250|UniProtKB:Q9F8A8};
GN Name=cooS; OrderedLocusNames=AF_1849;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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 which is 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 positions 48 and 292;
CC they are replaced by a Ser and a Glu, respectively. It is therefore
CC possible that the C- and D-clusters are either altered or missing in
CC this protein, which may not form 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; AE000782; AAB89403.1; -; Genomic_DNA.
DR PIR; H69480; H69480.
DR RefSeq; WP_010879343.1; NC_000917.1.
DR AlphaFoldDB; O28429; -.
DR SMR; O28429; -.
DR STRING; 224325.AF_1849; -.
DR EnsemblBacteria; AAB89403; AAB89403; AF_1849.
DR GeneID; 24795591; -.
DR KEGG; afu:AF_1849; -.
DR eggNOG; arCOG02429; Archaea.
DR HOGENOM; CLU_030631_0_0_2; -.
DR OMA; PEYMEQK; -.
DR OrthoDB; 5135at2157; -.
DR PhylomeDB; O28429; -.
DR Proteomes; UP000002199; 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: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 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..622
FT /note="Carbon monoxide dehydrogenase"
FT /id="PRO_0000157140"
FT BINDING 40
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 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 68
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 334
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 442
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 473
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 514
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
SQ SEQUENCE 622 AA; 67496 MW; 018304F4C49177B4 CRC64;
MKIEGKVSEH ESINMMYERV SKEGVTNIVD RFNAQEKGRC PFCEKGLSCQ LCSMGPCRIS
KDKPTGACGI DAAGMVVRNF THKNMLGTEA YTYHAIEAAK TLKATAEGKT IYEIKDVEKL
KWFAKLLGIE GEDVNELAAK VADFVISDLS SLEKSRLVEI FAPEKRKELW EKLGIFPSGV
FQELLTMGSS AMTNVDSNYV SLAKKSMSMS IATCMAAQIA LETIQDILFG TPMPHESHSD
LGILDPEYVN IAVNGHEPFV GIALIKLAER EEIQEKARKA GAKGLRIIGF IETGQEILQR
VDSPVFAGIV GNWIVQEYAL ATGCVDVFAA DMNCTLPSLP EYQRYGVKIV PVSRLVRLKG
IDEGLDYEPE KAEEIAMKLI DMAIENFKQR DKSKAVKVEQ KKKIVVGFSP EAILKALNGD
LNVLLDAIKK GDIKGVVALV SCTTLKNGPH DSSTVTIAKE LIKRDILVLS MGCGNAALQV
AGLTSMEAVE LAGEKLKAVC KALNIPPVLS FGTCTDTGRA AYLVRLIADA LGVDVPQLPV
AVTAPEYMEQ KATIDAVFAV AYGLTTHVSP VPPITGSEDA VKLFTEDVEK LTGGKVVVEE
DPLKAAELLE KVIEEKRKAL GI
