COOS1_CARHZ
ID COOS1_CARHZ Reviewed; 636 AA.
AC P59934; Q3AB40;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Carbon monoxide dehydrogenase 1;
DE Short=CODH 1;
DE EC=1.2.7.4 {ECO:0000269|PubMed:11489867, ECO:0000269|PubMed:12423371};
GN Name=cooS1; OrderedLocusNames=CHY_1824;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-21 AND 164-173, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11489867; DOI=10.1128/jb.183.17.5134-5144.2001;
RA Svetlitchnyi V., Peschel C., Acker G., Meyer O.;
RT "Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the
RT anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus
RT hydrogenoformans.";
RL J. Bacteriol. 183:5134-5144(2001).
RN [3]
RP PROTEIN SEQUENCE OF 3-25, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12423371; DOI=10.1046/j.1432-1033.2002.03282.x;
RA Soboh B., Linder D., Hedderich R.;
RT "Purification and catalytic properties of a CO-oxidizing:H2-evolving enzyme
RT complex from Carboxydothermus hydrogenoformans.";
RL Eur. J. Biochem. 269:5712-5721(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:0000269|PubMed:11489867, ECO:0000269|PubMed:12423371}.
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:0000269|PubMed:11489867, ECO:0000269|PubMed:12423371};
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 -!- ACTIVITY REGULATION: Inactivated by O(2).
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9F8A8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11489867}. Cell
CC membrane {ECO:0000269|PubMed:11489867}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11489867}; Cytoplasmic side
CC {ECO:0000269|PubMed:11489867}. Note=Loosely attached to the membrane,
CC probably via CooF.
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}.
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DR EMBL; CP000141; ABB14432.1; -; Genomic_DNA.
DR RefSeq; WP_011344718.1; NC_007503.1.
DR AlphaFoldDB; P59934; -.
DR SMR; P59934; -.
DR STRING; 246194.CHY_1824; -.
DR EnsemblBacteria; ABB14432; ABB14432; CHY_1824.
DR KEGG; chy:CHY_1824; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_030631_0_0_9; -.
DR OMA; MPHNIDA; -.
DR OrthoDB; 136177at2; -.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Cytoplasm; Direct protein sequencing; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Nickel; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11489867"
FT CHAIN 2..636
FT /note="Carbon monoxide dehydrogenase 1"
FT /id="PRO_0000157137"
FT BINDING 38
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="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 262
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 297
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT BINDING 335
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 528
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000250|UniProtKB:Q9F8A8"
FT CONFLICT 10
FT /note="P -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 67679 MW; 78CDD333C2A296C7 CRC64;
MSNWKNSVDP AVDYLLPIAK KAGIETAWDR YEAMQPQCGF GELGVCCRIC WKGPCRIDPF
GNGPQRGVCG ADAHTIVARN LIRMIAAGAA AHSEHGRHIA LTLLEVGEGH APAYRIKDEQ
KLRKIAEKLN LAPAGKDIRQ VAKEVALASL DDYSRQKRNV PCNWAKETLT AERVDKLAEL
GVMPHNIDAV ITEIMGRTHV GCDADAVNLL LGGIKGALAD YTGMCLSTEL SDVIFGTPKP
VITQANLGVL KEDAVNIAVH GHNPLLSEII CDVALKMNEE AKKAGAKEGI NVVGICCTGN
EVMMRRGIPL ATNYLSQEMA IITGALDAMV VDVQCIMPAL TSVAECFHTE IITTMAENKI
TGATHIEFRE DSAVESAKKI VEVAIEAFKK RDKRKVNIPD CKQTAITGFS AEAIMAVLSK
LNANDPLKPL IDNIINGNIQ GIALFAGCNN PKAIHDNSFI TIAKELAKNN VLMLATGCGA
GAFAKNGLMT QEATEAYAGE SLKAVLTALG KAAGLNGPLP LVLHMGSCVD NSRAVNVAVA
IANKLGVDLD KLPLVASAPE FMSEKAVAIG TWAVTLGIPT HIGIVPQIMG SSVVVEFLTE
KAKDLLGGYF IVETNPELAA AKLVAVIKER RRGLGI
