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Conserved domains on  [gi|2274274074|gb|UTS84175|]
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NO-forming nitrite reductase, partial [Thermus brockianus]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10135995)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions| multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 17-148 6.51e-53

Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center in the protein. The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


:

Pssm-ID: 259871 [Multi-domain]  Cd Length: 143  Bit Score: 168.89  E-value: 6.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274274074  17 PDLKLYIVQSEWYASGRD----------FFDGKATYVVFNGYNFRYV-NEPIPVRPGDYVRIYFLNAGPSLTSTFHVVGG 85
Cdd:cd04208     1 VDREYYLVQSELYTGGDDggvglfdyakMLDEKPDYVVFNGRVFAYTgTNPLQAKVGERVRIYVVNAGPNLTSSFHVIGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274274074  86 VWEYIYYQG-NPDNVMKGSQTVLAGPSDSWVIEWRVpPVEGDYTLVTHVFNTAIKGAVGILRAK 148
Cdd:cd04208    81 IFDRVYPEGsNPNNPLRGVQTVLVPPGGGAIVEFTF-PVPGNYALVDHALSRAEKGALGVLKVE 143
PetE COG3794
Plastocyanin [Energy production and conversion];
221-261 1.50e-03

Plastocyanin [Energy production and conversion];


:

Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 36.51  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2274274074 221 NSFYPKILEIPVGTTVEFVNEDvfdllegerTGRHDAVVIN 261
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD---------SVPHNVTSDD 32
 
Name Accession Description Interval E-value
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 17-148 6.51e-53

Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center in the protein. The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259871 [Multi-domain]  Cd Length: 143  Bit Score: 168.89  E-value: 6.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274274074  17 PDLKLYIVQSEWYASGRD----------FFDGKATYVVFNGYNFRYV-NEPIPVRPGDYVRIYFLNAGPSLTSTFHVVGG 85
Cdd:cd04208     1 VDREYYLVQSELYTGGDDggvglfdyakMLDEKPDYVVFNGRVFAYTgTNPLQAKVGERVRIYVVNAGPNLTSSFHVIGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274274074  86 VWEYIYYQG-NPDNVMKGSQTVLAGPSDSWVIEWRVpPVEGDYTLVTHVFNTAIKGAVGILRAK 148
Cdd:cd04208    81 IFDRVYPEGsNPNNPLRGVQTVLVPPGGGAIVEFTF-PVPGNYALVDHALSRAEKGALGVLKVE 143
PetE COG3794
Plastocyanin [Energy production and conversion];
221-261 1.50e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 36.51  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2274274074 221 NSFYPKILEIPVGTTVEFVNEDvfdllegerTGRHDAVVIN 261
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD---------SVPHNVTSDD 32
 
Name Accession Description Interval E-value
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 17-148 6.51e-53

Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center in the protein. The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259871 [Multi-domain]  Cd Length: 143  Bit Score: 168.89  E-value: 6.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274274074  17 PDLKLYIVQSEWYASGRD----------FFDGKATYVVFNGYNFRYV-NEPIPVRPGDYVRIYFLNAGPSLTSTFHVVGG 85
Cdd:cd04208     1 VDREYYLVQSELYTGGDDggvglfdyakMLDEKPDYVVFNGRVFAYTgTNPLQAKVGERVRIYVVNAGPNLTSSFHVIGG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274274074  86 VWEYIYYQG-NPDNVMKGSQTVLAGPSDSWVIEWRVpPVEGDYTLVTHVFNTAIKGAVGILRAK 148
Cdd:cd04208    81 IFDRVYPEGsNPNNPLRGVQTVLVPPGGGAIVEFTF-PVPGNYALVDHALSRAEKGALGVLKVE 143
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 45-119 1.16e-03

The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 38.39  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274274074  45 FNGYNFRYVnEPIPVRPGDYVRIYFLNAGPSLTStFHVVGGVWEYIYYQGNPdnvMKGSQ-----TVLAGPSDSWVIEWR 119
Cdd:cd04202    32 INGKSFPAT-PPLVVKEGDRVRIRLINLSMDHHP-MHLHGHFFLVTATDGGP---IPGSApwpkdTLNVAPGERYDIEFV 106
PetE COG3794
Plastocyanin [Energy production and conversion];
221-261 1.50e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 36.51  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2274274074 221 NSFYPKILEIPVGTTVEFVNEDvfdllegerTGRHDAVVIN 261
Cdd:COG3794     1 MAFEPATLTVKPGDTVTWVNTD---------SVPHNVTSDD 32
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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