COOS2_CARHZ
ID COOS2_CARHZ Reviewed; 636 AA.
AC Q9F8A8; Q3AFX7; Q9F8L4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Carbon monoxide dehydrogenase 2;
DE Short=CODH 2;
DE EC=1.2.7.4 {ECO:0000269|PubMed:11489867, ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691};
GN Name=cooS2; Synonyms=cooSII; OrderedLocusNames=CHY_0085;
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 [GENOMIC DNA].
RX PubMed=11024270; DOI=10.1111/j.1574-6968.2000.tb09346.x;
RA Gonzalez J.M., Robb F.T.;
RT "Genetic analysis of Carboxydothermus hydrogenoformans carbon monoxide
RT dehydrogenase genes cooF and cooS.";
RL FEMS Microbiol. Lett. 191:243-247(2000).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-16.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-429.
RA Gonzalez J.M., Robb F.T.;
RT "A genomic survey of the extreme thermophilic, CO-utilizing bacterium
RT Carboxydothermus hydrogenoformans.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
RP AND NICKEL-IRON-SULFUR CLUSTER (NI-4FE-5S), COFACTOR, AND SUBUNIT.
RX PubMed=11509720; DOI=10.1126/science.1061500;
RA Dobbek H., Svetlitchnyi V., Gremer L., Huber R., Meyer O.;
RT "Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S]
RT cluster.";
RL Science 293:1281-1285(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
RP AND NICKEL-IRON-SULFUR CLUSTER (NI-4FE-5S), COFACTOR, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15113209; DOI=10.1021/ja037776v;
RA Dobbek H., Svetlitchnyi V., Liss J., Meyer O.;
RT "Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S]
RT cluster of CO dehydrogenase.";
RL J. Am. Chem. Soc. 126:5382-5387(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 4-636 IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S); NICKEL-IRON-SULFUR CLUSTER (NI-4FE-5S) AND CARBON DIOXIDE,
RP COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=18048691; DOI=10.1126/science.1148481;
RA Jeoung J.H., Dobbek H.;
RT "Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon
RT monoxide dehydrogenase.";
RL Science 318:1461-1464(2007).
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}.
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:15113209,
CC ECO:0000269|PubMed:18048691};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:11509720};
CC Note=Binds 3 [4Fe-4S] clusters per homodimer.
CC {ECO:0000269|PubMed:11509720};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Evidence={ECO:0000269|PubMed:11509720, ECO:0000269|PubMed:15113209,
CC ECO:0000269|PubMed:18048691};
CC Note=Binds 2 [Ni-4Fe-5S] clusters per homodimer.
CC {ECO:0000269|PubMed:11509720, ECO:0000269|PubMed:15113209,
CC ECO:0000269|PubMed:18048691};
CC -!- ACTIVITY REGULATION: Inactivated by O(2).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11509720}.
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:0000269|PubMed:11509720,
CC ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691}.
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; AF249899; AAG29809.1; -; Genomic_DNA.
DR EMBL; CP000141; ABB15588.1; -; Genomic_DNA.
DR EMBL; AF244619; AAG23568.1; -; Genomic_DNA.
DR RefSeq; WP_011343033.1; NC_007503.1.
DR PDB; 1SU6; X-ray; 1.64 A; A=1-636.
DR PDB; 1SU7; X-ray; 1.12 A; A=1-636.
DR PDB; 1SU8; X-ray; 1.10 A; A=1-636.
DR PDB; 1SUF; X-ray; 1.15 A; A=1-636.
DR PDB; 2YIV; X-ray; 1.28 A; X=1-636.
DR PDB; 3B51; X-ray; 1.40 A; X=4-636.
DR PDB; 3B52; X-ray; 1.50 A; X=4-636.
DR PDB; 3B53; X-ray; 1.50 A; X=4-636.
DR PDB; 3I39; X-ray; 1.36 A; X=1-636.
DR PDB; 4UDX; X-ray; 1.03 A; X=1-636.
DR PDB; 4UDY; X-ray; 1.09 A; X=1-636.
DR PDB; 5FLE; X-ray; 1.23 A; X=4-636.
DR PDBsum; 1SU6; -.
DR PDBsum; 1SU7; -.
DR PDBsum; 1SU8; -.
DR PDBsum; 1SUF; -.
DR PDBsum; 2YIV; -.
DR PDBsum; 3B51; -.
DR PDBsum; 3B52; -.
DR PDBsum; 3B53; -.
DR PDBsum; 3I39; -.
DR PDBsum; 4UDX; -.
DR PDBsum; 4UDY; -.
DR PDBsum; 5FLE; -.
DR AlphaFoldDB; Q9F8A8; -.
DR SMR; Q9F8A8; -.
DR STRING; 246194.CHY_0085; -.
DR EnsemblBacteria; ABB15588; ABB15588; CHY_0085.
DR KEGG; chy:CHY_0085; -.
DR eggNOG; COG1151; Bacteria.
DR HOGENOM; CLU_030631_0_0_9; -.
DR OMA; GIPACTH; -.
DR OrthoDB; 136177at2; -.
DR BRENDA; 1.2.7.4; 1178.
DR EvolutionaryTrace; Q9F8A8; -.
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 3D-structure; 4Fe-4S; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Iron; 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 2"
FT /id="PRO_0000157138"
FT BINDING 39
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:11509720"
FT BINDING 47
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:11509720"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11509720"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11509720"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11509720"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11509720"
FT BINDING 261
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT BINDING 295
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT BINDING 333
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT BINDING 446
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT BINDING 476
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT BINDING 526
FT /ligand="[Ni-4Fe-5S] cluster"
FT /ligand_id="ChEBI:CHEBI:177874"
FT /evidence="ECO:0000269|PubMed:11509720,
FT ECO:0000269|PubMed:15113209, ECO:0000269|PubMed:18048691"
FT CONFLICT 528
FT /note="D -> H (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="A -> S (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="G -> W (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="L -> M (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="E -> Q (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="L -> F (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 615..617
FT /note="ETA -> VQQR (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="W -> R (in Ref. 1; AAG29809)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 74..108
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 205..234
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 371..388
FT /evidence="ECO:0007829|PDB:4UDX"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:1SU7"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 455..466
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 475..483
FT /evidence="ECO:0007829|PDB:4UDX"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 498..510
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 529..543
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 550..556
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 562..574
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:4UDX"
FT TURN 585..588
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 590..597
FT /evidence="ECO:0007829|PDB:4UDX"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:4UDX"
FT STRAND 607..610
FT /evidence="ECO:0007829|PDB:4UDX"
FT HELIX 614..631
FT /evidence="ECO:0007829|PDB:4UDX"
SQ SEQUENCE 636 AA; 66914 MW; 61C1011E86022A63 CRC64;
MAKQNLKSTD RAVQQMLDKA KREGIQTVWD RYEAMKPQCG FGETGLCCRH CLQGPCRINP
FGDEPKVGIC GATAEVIVAR GLDRSIAAGA AGHSGHAKHL AHTLKKAVQG KAASYMIKDR
TKLHSIAKRL GIPTEGQKDE DIALEVAKAA LADFHEKDTP VLWVTTVLPP SRVKVLSAHG
LIPAGIDHEI AEIMHRTSMG CDADAQNLLL GGLRCSLADL AGCYMGTDLA DILFGTPAPV
VTESNLGVLK ADAVNVAVHG HNPVLSDIIV SVSKEMENEA RAAGATGINV VGICCTGNEV
LMRHGIPACT HSVSQEMAMI TGALDAMILD YQCIQPSVAT IAECTGTTVI TTMEMSKITG
ATHVNFAEEA AVENAKQILR LAIDTFKRRK GKPVEIPNIK TKVVAGFSTE AIINALSKLN
ANDPLKPLID NVVNGNIRGV CLFAGCNNVK VPQDQNFTTI ARKLLKQNVL VVATGCGAGA
LMRHGFMDPA NVDELCGDGL KAVLTAIGEA NGLGGPLPPV LHMGSCVDNS RAVALVAALA
NRLGVDLDRL PVVASAAEAM HEKAVAIGTW AVTIGLPTHI GVLPPITGSL PVTQILTSSV
KDITGGYFIV ELDPETAADK LLAAINERRA GLGLPW
