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Conserved domains on  [gi|1864317853|gb|QLC45183|]
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nitrite reductase, partial [uncultured Ochrobactrum sp.]

Protein Classification

copper-containing nitrite reductase( domain architecture ID 1903389)

copper-containing nitrite reductase catalyzes the reduction of nitrite to nitric oxide (NO)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cu_nitrite_red super family cl42876
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 1-172 1.83e-92

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


The actual alignment was detected with superfamily member TIGR02376:

Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 271.27  E-value: 1.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853   1 GMVPWHVVSGMNGAIMVLPREGLHDgkgkaltYDKIYYVGEQDFYVPRDEngkykkyeAPGDAYEDTVKVMRTLTPTHVV 80
Cdd:TIGR02376 128 GMVPWHVVSGMNGAIMVLPREGLPE-------YDKEYYIGESDLYTPKDE--------GEGGAYEDDVAAMRTLTPTHVV 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  81 FNGAVGALTGDKAMTAVVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPG 160
Cdd:TIGR02376 193 FNGAVGALTGDNALTAGVGERVLFVHSQPNRDSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPG 272

                         170
                  ....*....|..
gi 1864317853 161 IYAYVNHNLIEA 172
Cdd:TIGR02376 273 VYAYVDHNLIEA 284
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 1-172 1.83e-92

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 271.27  E-value: 1.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853   1 GMVPWHVVSGMNGAIMVLPREGLHDgkgkaltYDKIYYVGEQDFYVPRDEngkykkyeAPGDAYEDTVKVMRTLTPTHVV 80
Cdd:TIGR02376 128 GMVPWHVVSGMNGAIMVLPREGLPE-------YDKEYYIGESDLYTPKDE--------GEGGAYEDDVAAMRTLTPTHVV 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  81 FNGAVGALTGDKAMTAVVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPG 160
Cdd:TIGR02376 193 FNGAVGALTGDNALTAGVGERVLFVHSQPNRDSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPG 272

                         170
                  ....*....|..
gi 1864317853 161 IYAYVNHNLIEA 172
Cdd:TIGR02376 273 VYAYVDHNLIEA 284
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 33-172 1.34e-39

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: 131.14  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  33 YDKIYYVGEQDFYVPrdengkykkyEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAVVGEKVLIVHSQA--N 110
Cdd:cd04208     1 VDREYYLVQSELYTG----------GDDGGVGLFDYAKMLDEKPDYVVFNGRVFAYTGTNPLQAKVGERVRIYVVNAgpN 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864317853 111 RDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEA 172
Cdd:cd04208    71 LTSSFHVIGGIFDRVYPEGSNPNNPLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRA 132
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 35-172 3.06e-26

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 97.00  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  35 KIYYVGEQDFYvPRDENGKYKKYEAPGDAYEDTvkvmrTLTPTHVVFNGAVGALTGDKAMTAVVGEKVLIVhSQANRDTR 114
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF-----PPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853 115 PHLIGGHGDY-VWATGKFNTPPDVDqeTWFIPGGAAGAAFYTFQQ-PGIYAYVNHNLIEA 172
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNPFTVD--SLDIFPGQRYSVLVTANQdPGNYWIVASPNIPA 131
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 1-172 1.83e-92

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 271.27  E-value: 1.83e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853   1 GMVPWHVVSGMNGAIMVLPREGLHDgkgkaltYDKIYYVGEQDFYVPRDEngkykkyeAPGDAYEDTVKVMRTLTPTHVV 80
Cdd:TIGR02376 128 GMVPWHVVSGMNGAIMVLPREGLPE-------YDKEYYIGESDLYTPKDE--------GEGGAYEDDVAAMRTLTPTHVV 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  81 FNGAVGALTGDKAMTAVVGEKVLIVHSQANRDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPG 160
Cdd:TIGR02376 193 FNGAVGALTGDNALTAGVGERVLFVHSQPNRDSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPG 272

                         170
                  ....*....|..
gi 1864317853 161 IYAYVNHNLIEA 172
Cdd:TIGR02376 273 VYAYVDHNLIEA 284
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 33-172 1.34e-39

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: 131.14  E-value: 1.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  33 YDKIYYVGEQDFYVPrdengkykkyEAPGDAYEDTVKVMRTLTPTHVVFNGAVGALTGDKAMTAVVGEKVLIVHSQA--N 110
Cdd:cd04208     1 VDREYYLVQSELYTG----------GDDGGVGLFDYAKMLDEKPDYVVFNGRVFAYTGTNPLQAKVGERVRIYVVNAgpN 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864317853 111 RDTRPHLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEA 172
Cdd:cd04208    71 LTSSFHVIGGIFDRVYPEGSNPNNPLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRA 132
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 35-172 3.06e-26

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 97.00  E-value: 3.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  35 KIYYVGEQDFYvPRDENGKYKKYEAPGDAYEDTvkvmrTLTPTHVVFNGAVGALTGDKAMTAVVGEKVLIVhSQANRDTR 114
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF-----PPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853 115 PHLIGGHGDY-VWATGKFNTPPDVDqeTWFIPGGAAGAAFYTFQQ-PGIYAYVNHNLIEA 172
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNPFTVD--SLDIFPGQRYSVLVTANQdPGNYWIVASPNIPA 131
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 73-169 5.45e-06

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 43.37  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864317853  73 TLTPTHVVFNGAVGALTGDKAMTAVVGEKVLIVHSQ-ANRDTRPHLIGGHGDYVWATGKFNTPpdvDQETWFIPGGAAGA 151
Cdd:cd00920     4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAMAGGANPG---LVNTLVIGPGESAE 80

                          90
                  ....*....|....*...
gi 1864317853 152 AFYTFQQPGIYAYVNHNL 169
Cdd:cd00920    81 VTFTTDQAGVYWFYCTIP 98
 
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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