DCMM_AFIC5
ID DCMM_AFIC5 Reviewed; 288 AA.
AC P19920; F8C0Z4; Q51323;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Carbon monoxide dehydrogenase medium chain;
DE Short=CO dehydrogenase subunit M;
DE Short=CO-DH M;
DE EC=1.2.5.3 {ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368};
GN Name=coxM; OrderedLocusNames=OCA5_pHCG300290;
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 1-29.
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=1510563; DOI=10.1007/bf00245166;
RA Hugendieck I., Meyer O.;
RT "The structural genes encoding CO dehydrogenase subunits (cox L, M and S)
RT in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with
RT the exception of Streptomyces thermoautotrophicus, conserved in
RT carboxydotrophic bacteria.";
RL Arch. Microbiol. 157:301-304(1992).
RN [5]
RP PROTEIN SEQUENCE OF 1-14.
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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND SMALL
RP SUBUNITS AND FAD, 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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) IN COMPLEX WITH CODH LARGE AND SMALL
RP SUBUNITS AND FAD, 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=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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995};
CC Note=Binds 1 FAD per subunit. {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; AEI08104.1; -; Genomic_DNA.
DR PIR; A56279; A56279.
DR RefSeq; WP_013913728.1; NC_015689.1.
DR PDB; 1N5W; X-ray; 1.50 A; C/F=1-288.
DR PDB; 1N60; X-ray; 1.19 A; C/F=1-288.
DR PDB; 1N61; X-ray; 1.30 A; C/F=1-288.
DR PDB; 1N62; X-ray; 1.09 A; C/F=1-288.
DR PDB; 1N63; X-ray; 1.21 A; C/F=1-288.
DR PDB; 1ZXI; X-ray; 1.70 A; C/F=1-288.
DR PDBsum; 1N5W; -.
DR PDBsum; 1N60; -.
DR PDBsum; 1N61; -.
DR PDBsum; 1N62; -.
DR PDBsum; 1N63; -.
DR PDBsum; 1ZXI; -.
DR AlphaFoldDB; P19920; -.
DR SMR; P19920; -.
DR EnsemblBacteria; AEI08104; AEI08104; OCA5_pHCG300290.
DR KEGG; ocg:OCA5_pHCG300290; -.
DR PATRIC; fig|504832.7.peg.3604; -.
DR HOGENOM; CLU_058050_3_0_5; -.
DR OMA; MVEINFD; -.
DR OrthoDB; 1017413at2; -.
DR BioCyc; MetaCyc:MON-19675; -.
DR BRENDA; 1.2.5.3; 4399.
DR BRENDA; 1.2.7.4; 4399.
DR SABIO-RK; P19920; -.
DR EvolutionaryTrace; P19920; -.
DR Proteomes; UP000007730; Plasmid pHCG3.
DR GO; GO:0008805; F:carbon-monoxide oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Plasmid; Reference proteome.
FT CHAIN 1..288
FT /note="Carbon monoxide dehydrogenase medium chain"
FT /id="PRO_0000079813"
FT DOMAIN 1..177
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 32..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT BINDING 111..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT CONFLICT 1
FT /note="M -> MM (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 208..222
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 264..285
FT /evidence="ECO:0007829|PDB:1N62"
SQ SEQUENCE 288 AA; 30241 MW; E3EA980056731FC5 CRC64;
MIPGSFDYHR PKSIADAVAL LTKLGEDARP LAGGHSLIPI MKTRLATPEH LVDLRDIGDL
VGIREEGTDV VIGAMTTQHA LIGSDFLAAK LPIIRETSLL IADPQIRYMG TIGGNAANGD
PGNDMPALMQ CLGAAYELTG PEGARIVAAR DYYQGAYFTA IEPGELLTAI RIPVPPTGHG
YAYEKLKRKI GDYATAAAAV VLTMSGGKCV TASIGLTNVA NTPLWAEEAG KVLVGTALDK
PALDKAVALA EAITAPASDG RGPAEYRTKM AGVMLRRAVE RAKARAKN
