DCMS_HYDPS
ID DCMS_HYDPS Reviewed; 163 AA.
AC P19915; Q9ZAR6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carbon monoxide dehydrogenase small chain;
DE Short=CO dehydrogenase subunit S;
DE Short=CO-DH S;
DE EC=1.2.5.3 {ECO:0000250|UniProtKB:P19921};
GN Name=cutS;
OS Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=47421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, AND SUBUNIT.
RX PubMed=10482497; DOI=10.1128/jb.181.18.5581-5590.1999;
RA Kang B.S., Kim Y.M.;
RT "Cloning and molecular characterization of the genes for carbon monoxide
RT dehydrogenase and localization of molybdopterin, flavin adenine
RT dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga
RT pseudoflava.";
RL J. Bacteriol. 181:5581-5590(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-21.
RX PubMed=2818128; DOI=10.1007/bf00425170;
RA Kraut M., Hugendieck I., Herwig S., Meyer O.;
RT "Homology and distribution of CO dehydrogenase structural genes in
RT carboxydotrophic bacteria.";
RL Arch. Microbiol. 152:335-341(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=10966817; DOI=10.1006/jmbi.2000.4023;
RA Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.;
RT "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on
RT the crystallographic structure of the seleno-molybdo-iron-sulfur
RT flavoenzyme carbon monoxide dehydrogenase.";
RL J. Mol. Biol. 301:1221-1235(2000).
RN [4]
RP REVIEW.
RX PubMed=11076018; DOI=10.1515/bc.2000.108;
RA Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M.,
RA Meyer-Klaucke W., Huber R.;
RT "The role of Se, Mo and Fe in the structure and function of carbon monoxide
RT dehydrogenase.";
RL Biol. Chem. 381:865-876(2000).
CC -!- FUNCTION: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
CC {ECO:0000250|UniProtKB:P19921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + CO + H2O = a quinol + CO2; Xref=Rhea:RHEA:48880,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.2.5.3;
CC Evidence={ECO:0000250|UniProtKB:P19921};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10482497};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000269|PubMed:10482497};
CC -!- SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large,
CC a medium and a small subunit. {ECO:0000269|PubMed:10482497}.
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DR EMBL; U80806; AAD00362.1; -; Genomic_DNA.
DR PDB; 1FFU; X-ray; 2.35 A; A/D=1-163.
DR PDB; 1FFV; X-ray; 2.25 A; A/D=1-163.
DR PDBsum; 1FFU; -.
DR PDBsum; 1FFV; -.
DR AlphaFoldDB; P19915; -.
DR SMR; P19915; -.
DR BRENDA; 1.2.5.3; 2729.
DR EvolutionaryTrace; P19915; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008805; F:carbon-monoxide oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..163
FT /note="Carbon monoxide dehydrogenase small chain"
FT /id="PRO_0000079816"
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 136
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT BINDING 138
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT CONFLICT 11
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:1FFV"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:1FFV"
SQ SEQUENCE 163 AA; 17752 MW; 9307050CC033410C CRC64;
MAKKIITVNV NGKAQEKAVE PRTLLIHFLR EELNLTGAHI GCETSHCGAC TVDIDGRSVK
SCTHLAVQCD GSEVLTVEGL ANKGVLHAVR EGFYKEHGLQ CGFCTPGMLM RAYRFLQENP
NPTEAEIRMG MTGNLCRCTG YQNIVKAVQY AARKLQEPST AAA
