DCMS_AFIC5
ID DCMS_AFIC5 Reviewed; 166 AA.
AC P19921; F8C0Z5; Q51324;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
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:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368};
GN Name=coxS; OrderedLocusNames=OCA5_pHCG300300;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OG Plasmid megaplasmid pHCG3.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=7721710; DOI=10.1128/jb.177.8.2197-2203.1995;
RA Schuebel U., Kraut M., Moersdorf G., Meyer O.;
RT "Molecular characterization of the gene cluster coxMSL encoding the
RT molybdenum-containing carbon monoxide dehydrogenase of Oligotropha
RT carboxidovorans.";
RL J. Bacteriol. 177:2197-2203(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT utilization of CO, H(2) and CO(2).";
RL Gene 322:67-75(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21275368; DOI=10.1021/bi1017182;
RA Wilcoxen J., Zhang B., Hille R.;
RT "Reaction of the molybdenum- and copper-containing carbon monoxide
RT dehydrogenase from Oligotropha carboxydovorans with quinones.";
RL Biochemistry 50:1910-1916(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND MEDIUM
RP SUBUNITS; IRON-SULFUR (2FE-2S), COFACTOR, AND SUBUNIT.
RX PubMed=10430865; DOI=10.1073/pnas.96.16.8884;
RA Dobbek H., Gremer L., Meyer O., Huber R.;
RT "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur
RT flavoprotein containing S-selanylcysteine.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND
RP MEDIUM SUBUNITS; IRON-SULFUR (2FE-2S), FUNCTION, COFACTOR, CATALYTIC
RP ACTIVITY, AND REACTION MECHANISM.
RX PubMed=12475995; DOI=10.1073/pnas.212640899;
RA Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.;
RT "Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase
RT resolved at 1.1-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002).
CC -!- FUNCTION: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
CC {ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368}.
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:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000269|PubMed:10430865,
CC ECO:0000269|PubMed:12475995};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.4 uM for 1,4-benzoquinone {ECO:0000269|PubMed:21275368};
CC -!- SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large,
CC a medium and a small subunit. {ECO:0000269|PubMed:10430865}.
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DR EMBL; CP002827; AEI08105.1; -; Genomic_DNA.
DR PIR; B56279; B56279.
DR RefSeq; WP_013913729.1; NC_015689.1.
DR PDB; 1N5W; X-ray; 1.50 A; A/D=1-166.
DR PDB; 1N60; X-ray; 1.19 A; A/D=1-166.
DR PDB; 1N61; X-ray; 1.30 A; A/D=1-166.
DR PDB; 1N62; X-ray; 1.09 A; A/D=1-166.
DR PDB; 1N63; X-ray; 1.21 A; A/D=1-166.
DR PDB; 1ZXI; X-ray; 1.70 A; A/D=1-166.
DR PDBsum; 1N5W; -.
DR PDBsum; 1N60; -.
DR PDBsum; 1N61; -.
DR PDBsum; 1N62; -.
DR PDBsum; 1N63; -.
DR PDBsum; 1ZXI; -.
DR AlphaFoldDB; P19921; -.
DR SMR; P19921; -.
DR BindingDB; P19921; -.
DR EnsemblBacteria; AEI08105; AEI08105; OCA5_pHCG300300.
DR KEGG; ocg:OCA5_pHCG300300; -.
DR PATRIC; fig|504832.7.peg.3605; -.
DR HOGENOM; CLU_052511_3_1_5; -.
DR OMA; IIHYLTG; -.
DR OrthoDB; 1843415at2; -.
DR BioCyc; MetaCyc:MON-19676; -.
DR BRENDA; 1.2.5.3; 4399.
DR BRENDA; 1.2.7.4; 4399.
DR SABIO-RK; P19921; -.
DR EvolutionaryTrace; P19921; -.
DR Proteomes; UP000007730; Plasmid pHCG3.
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; Plasmid; Reference proteome.
FT CHAIN 1..166
FT /note="Carbon monoxide dehydrogenase small chain"
FT /id="PRO_0000079817"
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 /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 137
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 139
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:1N62"
SQ SEQUENCE 166 AA; 17792 MW; E63AD31D726D22C1 CRC64;
MAKAHIELTI NGHPVEALVE PRTLLIHFIR EQQNLTGAHI GCDTSHCGAC TVDLDGMSVK
SCTMFAVQAN GASITTIEGM AAPDGTLSAL QEGFRMMHGL QCGYCTPGMI MRSHRLLQEN
PSPTEAEIRF GIGGNLCRCT GYQNIVKAIQ YAAAKINGVP FEEAAE
