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 04-NOV-2026, entry version 155. 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; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; 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 IN COMPLEX WITH CODH LARGE AND MEDIUM SUBUNITS; RP 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 IN COMPLEX WITH CODH LARGE AND MEDIUM SUBUNITS; RP IRON-SULFUR (2FE-2S), FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND REACTION RP 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=CO + a quinone + 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}. 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; 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 AlphaFoldDB; P19921; -. DR SMR; P19921; -. DR BindingDB; P19921; -. DR KEGG; ocg:OCA5_pHCG300300; -. DR PATRIC; fig|504832.7.peg.3605; -. DR HOGENOM; CLU_052511_3_1_5; -. DR OMA; AACWKGE; -. DR OrthoDB; 9806714at2; -. DR BioCyc; MetaCyc:MONOMER-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:0008805; F:aerobic carbon monoxide dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR FunFam; 1.10.150.120:FF:000003; Carbon monoxide dehydrogenase, small subunit; 1. DR FunFam; 3.10.20.30:FF:000020; Xanthine dehydrogenase iron-sulfur subunit; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 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 PANTHER; PTHR44379; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1. DR PANTHER; PTHR44379:SF5; OXIDOREDUCTASE WITH IRON-SULFUR SUBUNIT; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF01799; Fer2_2; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 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 28..32 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 //