COOS1_METMA
ID COOS1_METMA Reviewed; 628 AA.
AC Q8Q0L5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=MM_0121;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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 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; AE008384; AAM29817.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8Q0L5; -.
DR SMR; Q8Q0L5; -.
DR STRING; 192952.MM_0121; -.
DR PRIDE; Q8Q0L5; -.
DR EnsemblBacteria; AAM29817; AAM29817; MM_0121.
DR KEGG; mma:MM_0121; -.
DR PATRIC; fig|192952.21.peg.139; -.
DR eggNOG; arCOG02429; Archaea.
DR HOGENOM; CLU_030631_0_0_2; -.
DR OMA; MCCTGNE; -.
DR Proteomes; UP000000595; 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..628
FT /note="Carbon monoxide dehydrogenase 1"
FT /id="PRO_0000157145"
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; 66452 MW; 477E826EC46CCA6E CRC64;
MGCKMKQTAF EKSIDPASQK MLEKAENEGI ETAWDRYEKQ LPQCSFGQLG ICCRNCNMGP
CRIDPFGEGA EKGICGATAD IIVARNLLRM IAAGAAAHSD HARDAVLTFK KMTEGEAGSY
GIKDKTKLFS LASEYGISLE GKSHEEVAGE LASALLAEFG KQEGPIQYTR RAPEARLRLW
TSLGIEPRGV DREIVECMHR THIGVDNDAT HILLHGLRTS LSDGWGGSMI ATEIQDVLFG
TPEPKKSTVN LGVLSHDKVN VIIHGHEPIL SEMIVQAAED PELLELAKEK GAAGINVAGI
CCTGNETLMR HGTPIAGNFL QQELAVVTGA VEAMIVDVQC IMPALGNLTG CYHTKFISTS
PKADFPGTVR MEFHEERAYD TAREIVRTAV ENFPNRNIEK VNIPEEKQEC MVGFSAEAIL
KALGGSPAPL IDAIAGGAVK GIGAVVGCNN VKVQHNYGHV NLVKELIKNN VLVVTTGCNA
IACAEAGLLV PEAAAQAGDG LKGVCEALGI PPVLHMGSCV DISRILVLAS AIAKSLGVDI
SDLPAAGAAP EWMSEKAVSI GAYVVSSGVF TVLGTVPPVL GSQAVTALLT KGLDNVIGAS
FAVEPDPFKA ANLMLEHIEG KRKALGLN
