DCMM_HYDPS
ID DCMM_HYDPS Reviewed; 287 AA.
AC P19914; Q9ZAR7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 106.
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:0000250|UniProtKB:P19920};
GN Name=cutM;
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 1-14.
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 [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:P19920}.
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:P19920};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10482497};
CC Note=Binds 1 FAD per subunit. {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; AAD00361.1; -; Genomic_DNA.
DR PDB; 1FFU; X-ray; 2.35 A; C/F=1-287.
DR PDB; 1FFV; X-ray; 2.25 A; C/F=1-287.
DR PDBsum; 1FFU; -.
DR PDBsum; 1FFV; -.
DR AlphaFoldDB; P19914; -.
DR SMR; P19914; -.
DR BRENDA; 1.2.5.3; 2729.
DR EvolutionaryTrace; P19914; -.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IDA:CACAO.
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.
FT CHAIN 1..287
FT /note="Carbon monoxide dehydrogenase medium chain"
FT /id="PRO_0000079812"
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 BINDING 111..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT CONFLICT 2..3
FT /note="IP -> MI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="S -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:1FFV"
FT STRAND 208..222
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:1FFV"
FT HELIX 264..285
FT /evidence="ECO:0007829|PDB:1FFV"
SQ SEQUENCE 287 AA; 30722 MW; F3E9848BDCF4138E CRC64;
MIPPRFEYHA PKSVGEAVAL LGQLGSDAKL LAGGHSLLPM MKLRFAQPEH LIDINRIPEL
RGIREEGSTV VIGAMTVEND LISSPIVQAR LPLLAEAAKL IADPQVRNRG TIGGDIAHGH
PGNDHPALSI AVEAHFVLEG PNGRRTVPAD GFFLGTYMTL LEENEVMVEI RVPAFAQGTG
WAYEKLKRKT GDWATAGCAV VMRKSGNTVS HIRIALTNVA PTALRREGGR SRLLGKAFTK
EAVQAAADAA IAICEPAEDL RGDADYKTAM AGQMVKRALN AAWARCA
