COOS1_METAC
ID COOS1_METAC Reviewed; 628 AA.
AC Q8TKW2;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carbon monoxide dehydrogenase 1;
DE Short=CODH 1;
DE EC=1.2.7.4 {ECO:0000250|UniProtKB:Q9F8A8};
GN Name=cooS1; OrderedLocusNames=MA_3282;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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}.
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 ---------------------------------------------------------------------------
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; AE010299; AAM06652.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TKW2; -.
DR SMR; Q8TKW2; -.
DR STRING; 188937.MA_3282; -.
DR EnsemblBacteria; AAM06652; AAM06652; MA_3282.
DR KEGG; mac:MA_3282; -.
DR HOGENOM; CLU_030631_0_0_2; -.
DR InParanoid; Q8TKW2; -.
DR OMA; MCCTGNE; -.
DR PhylomeDB; Q8TKW2; -.
DR Proteomes; UP000002487; 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..628
FT /note="Carbon monoxide dehydrogenase 1"
FT /id="PRO_0000157141"
FT BINDING 44
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 52
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 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 266
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 302
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 340
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 448
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 478
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 519
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
SQ SEQUENCE 628 AA; 66367 MW; 721C1103A7CE4119 CRC64;
MGKEMKQTAF EKSIDSASQI MLQKAEDEGI ETAWDRYEQQ LPQCSFGQLG ICCRNCNMGP
CRIDPFGEGT EKGICGATAD IIVARNLLRM IAAGAAAHSD HARDAVLTFK KMSEGKAGSY
RIKDEAKLYS LASEYGISAE EKSREEVAVE LASALLSEFG KQEGPILCTK RAPESRLKLW
SELGIEPRGI DREIVECMHR THIGVDNDAT HILLHGLRTS LSDGWGGSMI ATEIQDVLFG
TPEPKKSTVN LGVLSHDKVN VIVHGHEPIL SEMIVEAAED PELLELAEEK GATGINVAGI
CCTGNETLMR HGTPIAGTFL QQELAVITGA VEAMVVDVQC IMPSLGNLTG CYHTKFISTS
PKADFPGTAR MEFHEEEAYA TAKEIVKAAV ENFPNRNLKK VSIPEEKQEC MVGFSAEAIL
KALGGSPAPL IEAIAGGAIK GIGAVVGCNN VKIQHNYGHV NLVKELIKNN VLVVTTGCNA
IACAEAGLLV PEAAALAGDG LKGVCEALGI PPVLHMGSCV DISRILVLAS AVANSLGVDI
SDLPAAGAAP EWMSEKAVSI GAYVVSSGVF TVLGTIPPVL GSQAVTALLT KGLDGVIGAS
FAVEPDPFKA ADLMLEHIEG KRKALGLK
