COOS_RHORU
ID COOS_RHORU Reviewed; 639 AA.
AC P31896;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Carbon monoxide dehydrogenase;
DE Short=CODH;
DE EC=1.2.7.4 {ECO:0000250|UniProtKB:Q9F8A8};
GN Name=cooS;
OS Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RC STRAIN=UR1;
RX PubMed=1644755; DOI=10.1128/jb.174.16.5284-5294.1992;
RA Kerby R.L., Hong S.S., Ensign S.A., Coppoc L.J., Ludden P.W., Roberts G.P.;
RT "Genetic and physiological characterization of the Rhodospirillum rubrum
RT carbon monoxide dehydrogenase system.";
RL J. Bacteriol. 174:5284-5294(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UR1;
RX PubMed=8626276; DOI=10.1128/jb.178.6.1515-1524.1996;
RA Fox J.D., Kerby R.L., Roberts G.P., Ludden P.W.;
RT "Characterization of the CO-induced, CO-tolerant hydrogenase from
RT Rhodospirillum rubrum and the gene encoding the large subunit of the
RT enzyme.";
RL J. Bacteriol. 178:1515-1524(1996).
RN [3]
RP MUTAGENESIS OF HIS-265.
RX PubMed=9461598; DOI=10.1074/jbc.273.7.4059;
RA Spangler N.J., Meyers M.R., Gierke K.L., Kerby R.L., Roberts G.P.,
RA Ludden P.W.;
RT "Substitution of valine for histidine 265 in carbon monoxide dehydrogenase
RT from Rhodospirillum rubrum affects activity and spectroscopic states.";
RL J. Biol. Chem. 273:4059-4064(1998).
RN [4]
RP MUTAGENESIS OF CYS-531.
RX PubMed=12374822; DOI=10.1128/jb.184.21.5894-5897.2002;
RA Heo J., Wolfe M.T., Staples C.R., Ludden P.W.;
RT "Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a
RT hydroxylamine reductase.";
RL J. Bacteriol. 184:5894-5897(2002).
RN [5]
RP REVIEW.
RX PubMed=8561463; DOI=10.1146/annurev.mi.49.100195.001513;
RA Ferry J.G.;
RT "CO dehydrogenase.";
RL Annu. Rev. Microbiol. 49:305-333(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH NICKEL-IRON-SULFUR
RP CLUSTER (NI-4FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, AND SUBUNIT.
RX PubMed=11593006; DOI=10.1073/pnas.211429998;
RA Drennan C.L., Heo J., Sintchak M.D., Schreiter E., Ludden P.W.;
RT "Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S
RT carbon monoxide dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11973-11978(2001).
CC -!- FUNCTION: Allows growth in a CO-dependent manner in the dark. CODH
CC oxidizes carbon monoxide coupled, via CooF, to the reduction of a
CC 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:0000269|PubMed:11593006};
CC Note=Binds 3 [4Fe-4S] clusters per homodimer.
CC {ECO:0000269|PubMed:11593006};
CC -!- COFACTOR:
CC Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC Evidence={ECO:0000269|PubMed:11593006};
CC Note=Binds 2 [Ni-4Fe-4S] clusters per homodimer.
CC {ECO:0000269|PubMed:11593006};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11593006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC membrane protein; Cytoplasmic side. Note=Loosely attached to the inner
CC membrane, probably via CooF. {ECO:0000250}.
CC -!- INDUCTION: By carbon monoxide; under anaerobic conditions.
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 -!- MISCELLANEOUS: Methyl viologen can act as acceptor. Inactivated by
CC O(2).
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U65510; AAC45123.1; -; Genomic_DNA.
DR PIR; C42957; C42957.
DR RefSeq; WP_011389181.1; NZ_NHSM01000031.1.
DR PDB; 1JQK; X-ray; 2.80 A; A/B/C/D/E/F=1-639.
DR PDBsum; 1JQK; -.
DR AlphaFoldDB; P31896; -.
DR SMR; P31896; -.
DR OMA; MCCTGNE; -.
DR BioCyc; MetaCyc:MON-16431; -.
DR EvolutionaryTrace; P31896; -.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:CAFA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:CAFA.
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:0008198; F:ferrous iron binding; IDA:CAFA.
DR GO; GO:0016151; F:nickel cation binding; IDA:CAFA.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:CACAO.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR CDD; cd01915; CODH; 1.
DR DisProt; DP00239; -.
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 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Nickel; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1644755"
FT CHAIN 2..639
FT /note="Carbon monoxide dehydrogenase"
FT /id="PRO_0000157139"
FT BINDING 41
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:0000269|PubMed:11593006"
FT BINDING 49
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:0000269|PubMed:11593006"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 265
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 300
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 338
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 451
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 481
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT BINDING 531
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000269|PubMed:11593006"
FT MUTAGEN 265
FT /note="H->V: Great decrease in activity; diminishes
FT incorporation of nickel. Displays hydroxylamine reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:9461598"
FT MUTAGEN 531
FT /note="C->A: Displays hydrogenase activity."
FT /evidence="ECO:0000269|PubMed:12374822"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 76..109
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 209..238
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 376..391
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 460..471
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 503..515
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 534..547
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 567..579
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 582..587
FT /evidence="ECO:0007829|PDB:1JQK"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 604..608
FT /evidence="ECO:0007829|PDB:1JQK"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:1JQK"
FT HELIX 619..635
FT /evidence="ECO:0007829|PDB:1JQK"
SQ SEQUENCE 639 AA; 66854 MW; DCADD7C13D8D85B8 CRC64;
MTHHDCAHCS SDACATEMLN LAEANSIETA WHRYEKQQPQ CGFGSAGLCC RICLKGPCRI
DPFGEGPKYG VCGADRDTIV ARHLVRMIAA GTAAHSEHGR HIALAMQHIS QGELHDYSIR
DEAKLYAIAK TLGVATEGRG LLAIVGDLAA ITLGDFQNQD YDKPCAWLAA SLTPRRVKRL
GDLGLLPHNI DASVAQTMSR THVGCDADPT NLILGGLRVA MADLDGSMLA TELSDALFGT
PQPVVSAANL GVMKRGAVNI AVNGHNPMLS DIICDVAADL RDEAIAAGAA EGINIIGICC
TGHEVMMRHG VPLATNYLSQ ELPILTGALE AMVVDVQCIM PSLPRIAECF HTQIITTDKH
NKISGATHVP FDEHKAVETA KTIIRMAIAA FGRRDPNRVA IPAFKQKSIV GFSAEAVVAA
LAKVNADDPL KPLVDNVVNG NIQGIVLFVG CNTTKVQQDS AYVDLAKSLA KRNVLVLATG
CAAGAFAKAG LMTSEATTQY AGEGLKGVLS AIGTAAGLGG PLPLVMHMGS CVDNSRAVAL
ATALANKLGV DLSDLPLVAS APECMSEKAL AIGSWAVTIG LPTHVGSVPP VIGSQIVTKL
VTETAKDLVG GYFIVDTDPK SAGDKLYAAI QERRAGLGL
