EzCatDB: M00039
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DB codeM00039
CATH domainDomain 13.10.20.30 : Ubiquitin-like (UB roll)Catalytic domain
Domain 21.10.150.120 : DNA polymerase; domain 1Catalytic domain
Domain 33.90.1170.50 : Aldehyde Oxidoreductase; domain 3
Domain 43.30.365.10 : Aldehyde Oxidoreductase; domain 4
Domain 53.30.365.10 : Aldehyde Oxidoreductase; domain 4
Domain 63.30.365.10 : Aldehyde Oxidoreductase; domain 4Catalytic domain
Domain 73.30.365.10 : Aldehyde Oxidoreductase; domain 4Catalytic domain
Domain 83.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Domain 93.30.390.50 : Enolase-like; domain 1
Domain 103.30.465.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3Catalytic domain
E.C.1.2.99.2
CSA1qj2
MACiEM0107

CATH domainRelated DB codes (homologues)
3.10.20.30 : Ubiquitin-like (UB roll)M00042,M00049
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2M00001,M00004,M00179,T00003
3.30.465.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3T00003

Enzyme Name
UniProtKBKEGG

P19921P19919P19920
Protein nameCarbon monoxide dehydrogenase small chainCarbon monoxide dehydrogenase large chainCarbon monoxide dehydrogenase medium chaincarbon-monoxide dehydrogenase (acceptor)
anaerobic carbon monoxide dehydrogenase
carbon monoxide oxygenase
carbon-monoxide dehydrogenase
carbon-monoxide:(acceptor) oxidoreductase
SynonymsCO dehydrogenase subunit S
CO-DH S
EC 1.2.99.2
CO dehydrogenase subunit L
CO-DH L
EC 1.2.99.2
CO dehydrogenase subunit M
CO-DH M
EC 1.2.99.2
RefSeqYP_004638432.1 (Protein)
NC_015689.1 (DNA/RNA sequence)
YP_004638433.1 (Protein)
NC_015689.1 (DNA/RNA sequence)
YP_004638431.1 (Protein)
NC_015689.1 (DNA/RNA sequence)
PfamPF00111 (Fer2)
PF01799 (Fer2_2)
[Graphical view]
PF01315 (Ald_Xan_dh_C)
PF02738 (Ald_Xan_dh_C2)
[Graphical view]
PF03450 (CO_deh_flav_C)
PF00941 (FAD_binding_5)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00633Trinitrotoluene degradation
MAP00680Methane metabolism

UniProtKB:Accession NumberP19921P19919P19920
Entry nameDCMS_OLICADCML_OLICADCMM_OLICA
ActivityCO + H(2)O + A = CO(2) + AH(2).CO + H(2)O + A = CO(2) + AH(2).CO + H(2)O + A = CO(2) + AH(2).
SubunitDimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.
Subcellular location


CofactorBinds 2 2Fe-2S clusters.Binds 1 Cu(+) ion per subunit.,Binds 1 Mo(6+) ion per subunit.,Binds 1 molybdopterin cytosine dinucleotide (MCD) per subunit.Binds 1 FAD per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idL00023C99999L00006C00016C00237C00001C00028C00011C00030
Compound[2Fe-2S]Dinuclear [Cu-S-Mo(=O)OH] clusterMolybdopterin cytosine dinucleotideFADCOH2OAcceptorCO2Reduced acceptor
Typeheavy metal,sulfide groupheavy metal,sulfide groupamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,nucleotide,sulfhydryl groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideothersH2Oothersothersothers
ChEBI33739

43955
16238
17245
15377

16526


PubChem

4369128
643975
281
962
22247451

280


                  
1n5wA01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wD01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60A01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60D01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61A01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61D01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62A01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62D01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63A01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63D01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2A01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2G01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiA01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiD01Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wA02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wD02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60A02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60D02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61A02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61D02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62A02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62D02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63A02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63D02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2A02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2G02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiA02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiD02Bound:FESUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wB01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wE01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60B01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60E01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61B01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61E01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62B01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62E01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63B01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63E01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2B01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2H01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiB01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiE01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wB02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wE02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60B02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60E02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61B02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61E02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62B02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62E02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63B02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63E02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2B02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2H02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiB02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiE02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wB03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n5wE03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n60B03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n60E03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n61B03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n61E03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n62B03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n62E03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n63B03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n63E03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1qj2B03UnboundUnboundAnalogue:PCDUnboundUnbound UnboundUnboundUnboundUnbound
1qj2H03UnboundUnboundAnalogue:PCDUnboundUnbound UnboundUnboundUnboundUnbound
1zxiB03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1zxiE03UnboundUnboundBound:MCNUnboundUnbound UnboundUnboundUnboundUnbound
1n5wB04UnboundBound:CUM(oxidized)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wE04UnboundBound:CUM(oxidized)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60B04UnboundAnalogue:OMOUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60E04UnboundAnalogue:OMOUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61B04UnboundBound:CUN(reduced)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61E04UnboundBound:CUN(reduced)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62B04UnboundAnalogue:CUBUnboundUnboundUnbound UnboundUnboundUnboundIntermediate-analogue:CUB
1n62E04UnboundAnalogue:CUBUnboundUnboundUnbound UnboundUnboundUnboundIntermediate-analogue:CUB
1n63B04UnboundBound:CUN(reduced)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63E04UnboundBound:CUN(reduced)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2B04UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2H04UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiB04UnboundBound:CUM(oxidized)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiE04UnboundBound:CUM(oxidized)UnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wB05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wE05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60B05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60E05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61B05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61E05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62B05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62E05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63B05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63E05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2B05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2H05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiB05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiE05UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wC01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wF01UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60C01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n60F01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n61C01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n61F01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n62C01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n62F01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n63C01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n63F01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1qj2C01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1qj2I01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1zxiC01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1zxiF01UnboundUnboundUnboundBound:FADUnbound UnboundUnboundUnboundUnbound
1n5wC02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wF02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60C02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60F02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61C02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61F02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62C02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62F02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63C02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63F02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2C02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2I02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiC02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiF02UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n5wC03UnboundUnboundUnboundAnalogue:FADUnbound UnboundUnboundUnboundUnbound
1n5wF03UnboundUnboundUnboundAnalogue:FADUnbound UnboundUnboundUnboundUnbound
1n60C03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n60F03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61C03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n61F03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62C03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n62F03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63C03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1n63F03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2C03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1qj2I03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiC03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound
1zxiF03UnboundUnboundUnboundUnboundUnbound UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P19921, P19919, P19920 & literature [3], [4], [5]
pdbCatalytic residuesCofactor-binding residuesModified residuesMain-chain involved in catalysis
            
1n5wA01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n5wD01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n60A01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n60D01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n61A01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n61D01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n62A01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n62D01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n63A01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n63D01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1qj2A01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1qj2G01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1zxiA01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1zxiD01 
CYS  42;CYS  47;CYS  50;CYS  62(2Fe-2S cluster-1 binding)
 
 
1n5wA02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n5wD02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n60A02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n60D02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n61A02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n61D02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n62A02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n62D02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n63A02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n63D02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1qj2A02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1qj2G02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1zxiA02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1zxiD02 
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
 
 
1n5wB01                               
 
 
 
1n5wE01                               
 
 
 
1n60B01                               
 
 
 
1n60E01                               
 
 
 
1n61B01                               
 
 
 
1n61E01                               
 
 
 
1n62B01                               
 
 
 
1n62E01                               
 
 
 
1n63B01                               
 
 
 
1n63E01                               
 
 
 
1qj2B01                               
 
 
 
1qj2H01                               
 
 
 
1zxiB01                               
 
 
 
1zxiE01                               
 
 
 
1n5wB02                               
 
 
 
1n5wE02                               
 
 
 
1n60B02                               
 
 
 
1n60E02                               
 
 
 
1n61B02                               
 
 
 
1n61E02                               
 
 
 
1n62B02                               
 
 
 
1n62E02                               
 
 
 
1n63B02                               
 
 
 
1n63E02                               
 
 
 
1qj2B02                               
 
 
 
1qj2H02                               
 
 
 
1zxiB02                               
 
 
 
1zxiE02                               
 
 
 
1n5wB03                               
 
 
 
1n5wE03                               
 
 
 
1n60B03                               
 
 
 
1n60E03                               
 
 
 
1n61B03                               
 
 
 
1n61E03                               
 
 
 
1n62B03                               
 
 
 
1n62E03                               
 
 
 
1n63B03                               
 
 
 
1n63E03                               
 
 
 
1qj2B03                               
 
 
 
1qj2H03                               
 
 
 
1zxiB03                               
 
 
 
1zxiE03                               
 
 
 
1n5wB04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n5wE04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n60B04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n60E04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n61B04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n61E04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n62B04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n62E04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n63B04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n63E04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1qj2B04       ;GLU 763
EYS 388(Copper binding);GLU 763(Molybdenum binding)
EYS 388(Selanylated)
ARG 387
1qj2H04       ;GLU 763
EYS 388(Copper binding);GLU 763(Molybdenum binding)
EYS 388(Selanylated)
ARG 387
1zxiB04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1zxiE04CYS 388;GLU 763
CYS 388(Copper binding);GLU 763(Molybdenum binding)
                    
ARG 387
1n5wB05GLN 240
 
 
 
1n5wE05GLN 240
 
 
 
1n60B05GLN 240
 
 
 
1n60E05GLN 240
 
 
 
1n61B05GLN 240
 
 
 
1n61E05GLN 240
 
 
 
1n62B05GLN 240
 
 
 
1n62E05GLN 240
 
 
 
1n63B05GLN 240
 
 
 
1n63E05GLN 240
 
 
 
1qj2B05GLN 240
 
 
 
1qj2H05GLN 240
 
 
 
1zxiB05GLN 240
 
 
 
1zxiE05GLN 240
 
 
 
1n5wC01                               
 
 
 
1n5wF01                               
 
 
 
1n60C01                               
 
 
 
1n60F01                               
 
 
 
1n61C01                               
 
 
 
1n61F01                               
 
 
 
1n62C01                               
 
 
 
1n62F01                               
 
 
 
1n63C01                               
 
 
 
1n63F01                               
 
 
 
1qj2C01                               
 
 
 
1qj2I01                               
 
 
 
1zxiC01                               
 
 
 
1zxiF01                               
 
 
 
1n5wC02                               
 
 
 
1n5wF02                               
 
 
 
1n60C02                               
 
 
 
1n60F02                               
 
 
 
1n61C02                               
 
 
 
1n61F02                               
 
 
 
1n62C02                               
 
 
 
1n62F02                               
 
 
 
1n63C02                               
 
 
 
1n63F02                               
 
 
 
1qj2C02                               
 
 
 
1qj2I02                               
 
 
 
1zxiC02                               
 
 
 
1zxiF02                               
 
 
 
1n5wC03                               
 
 
 
1n5wF03                               
 
 
 
1n60C03                               
 
 
 
1n60F03                               
 
 
 
1n61C03                               
 
 
 
1n61F03                               
 
 
 
1n62C03                               
 
 
 
1n62F03                               
 
 
 
1n63C03                               
 
 
 
1n63F03                               
 
 
 
1qj2C03                               
 
 
 
1qj2I03                               
 
 
 
1zxiC03                               
 
 
 
1zxiF03                               
 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Fig.4, p.8887-8889
[2]Fig.5, p.871-875
[3]Fig.1
[4]p.1224-1228
[5]Fig.2, p.15974-15976
[7]Fig. 2, Fig. 6, Fig. 12, p.891-897

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID99362680
PubMed ID10430865
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages8884-9
AuthorsDobbek H, Gremer L, Meyer O, Huber R
TitleCrystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
Related PDB1qj2
Related UniProtKBP19919,P19920,P19921
[2]
PubMed ID11076018
JournalBiol Chem
Year2000
Volume381
Pages865-76
AuthorsMeyer O, Gremer L, Ferner R, Ferner M, Dobbek H, Gnida M, Meyer-Klaucke W, Huber R
TitleThe role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.
[3]
PubMed ID10636886
JournalJ Biol Chem
Year2000
Volume275
Pages1864-72
AuthorsGremer L, Kellner S, Dobbek H, Huber R, Meyer O
TitleBinding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli.
[4]
PubMed ID10966817
JournalJ Mol Biol
Year2000
Volume301
Pages1221-35
AuthorsHanzelmann P, Dobbek H, Gremer L, Huber R, Meyer O
TitleThe effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).
Medline ID22364130
PubMed ID12475995
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages15971-6
AuthorsDobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O
TitleCatalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
Related PDB1n5w,1n60,1n61,1n62,1n63
Related UniProtKBP19919,P19920,P19921
[6]
PubMed ID12515558
JournalBiochemistry
Year2003
Volume42
Pages222-30
AuthorsGnida M, Ferner R, Gremer L, Meyer O, Meyer-Klaucke W
TitleA novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
[7]
PubMed ID15834924
JournalJ Comput Chem
Year2005
Volume26
Pages888-98
AuthorsSiegbahn PE, Shestakov AF
TitleQuantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase.
[8]
PubMed ID16091936
JournalJ Biol Inorg Chem
Year2005
Volume10
Pages518-28
AuthorsResch M, Dobbek H, Meyer O
TitleStructural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.
Related PDB1zxi

comments
This enzyme is composed of large subunits with dinuclear cluster of Mo and Cu along with Molybdopterin cytosine dinucleotide(MCD) as cofactors, small subunits with two iron-sulfur clusters, and medium subunits with FAD as cofactor.
Ni-containing carbon monoxide dehydrogenases and bifunctional enzymes (with acetyl-CoA synthetase) are not homologous, which classified into the identical E.C.
According to the literature [3], this enzyme catalyzes the following reactions:
(A) Oxidation of CO with H2O, yielding CO2, two electrons and two protons (H+) ions:
(B) Electron transfer from CO to S-selanylcysteine 388 (EYS 388 of 1qj2):
(C) Electron transfer from S-selanylcysteine 388 (EYS 388 of 1qj2) to Molybdenum cofactor:
(D) Electron transfer from Molybdenum cofactor to MCD cofactor:
(E) Electron transfer from MCD cofactor to 2Fe-2S cluster-2:
(F) Electron transfer from 2Fe-2S cluster-2 to 2Fe-2S cluster-1:
(G) Electron transfer from 2Fe-2S cluster-1 to flavin group of FAD:
(H) Electron transfer from flavin group of FAD to electron acceptor protein:

createdupdated
2005-06-032009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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