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Conserved domains on  [gi|1407423174|gb|AWW01307|]
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dissimilatory sulfite reductase subunit B, partial [uncultured Desulfatibacillum sp.]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dsrB super family cl31167
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 1-127 5.28e-59

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


The actual alignment was detected with superfamily member TIGR02066:

Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 185.04  E-value: 5.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407423174   1 NIVHTQGWIHCHTPASDASGTVKATMDVLFDDFKQHRMPAHLRVAMACCLNMCGAVHCSDVAILGYHRKPPMIDNEYVDK 80
Cdd:TIGR02066 103 NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGVHASDIAIVGIHRKPPKINHEAVRN 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1407423174  81 MCEIPLAIAACPTAAIRPSKvelpnGTQVNSVAIKQERCMFCGNCYT 127
Cdd:TIGR02066 183 VCEIPSVVAACPTGALKPRR-----DGKNKSLEVDVEKCIYCGNCYT 224
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 1-127 5.28e-59

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 185.04  E-value: 5.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407423174   1 NIVHTQGWIHCHTPASDASGTVKATMDVLFDDFKQHRMPAHLRVAMACCLNMCGAVHCSDVAILGYHRKPPMIDNEYVDK 80
Cdd:TIGR02066 103 NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGVHASDIAIVGIHRKPPKINHEAVRN 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1407423174  81 MCEIPLAIAACPTAAIRPSKvelpnGTQVNSVAIKQERCMFCGNCYT 127
Cdd:TIGR02066 183 VCEIPSVVAACPTGALKPRR-----DGKNKSLEVDVEKCIYCGNCYT 224
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 1-73 1.15e-17

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 73.84  E-value: 1.15e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407423174   1 NIVHTQGWIHCHTPASDASGTVKATMDVLFDDFKQHRMPAHLRVAMACCLNMCGAVHCSDVAILGYHRKPPMI 73
Cdd:pfam01077   6 NVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 62-127 5.89e-03

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 33.10  E-value: 5.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1407423174  62 AILGYHrkPPMIDNEyvdKMCEIPLAIAACPTAAIRPSKvelpngtqvNSVAIKQERCMFCGNCYT 127
Cdd:COG2221     3 GIIGTW--PPKIDEE---KCIGCGLCVAVCPTGAISLDD---------GKLVIDEEKCIGCGACIR 54
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 1-127 5.28e-59

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 185.04  E-value: 5.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407423174   1 NIVHTQGWIHCHTPASDASGTVKATMDVLFDDFKQHRMPAHLRVAMACCLNMCGAVHCSDVAILGYHRKPPMIDNEYVDK 80
Cdd:TIGR02066 103 NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGVHASDIAIVGIHRKPPKINHEAVRN 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1407423174  81 MCEIPLAIAACPTAAIRPSKvelpnGTQVNSVAIKQERCMFCGNCYT 127
Cdd:TIGR02066 183 VCEIPSVVAACPTGALKPRR-----DGKNKSLEVDVEKCIYCGNCYT 224
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 1-73 1.15e-17

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 73.84  E-value: 1.15e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407423174   1 NIVHTQGWIHCHTPASDASGTVKATMDVLFDDFKQHRMPAHLRVAMACCLNMCGAVHCSDVAILGYHRKPPMI 73
Cdd:pfam01077   6 NVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 62-127 5.89e-03

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 33.10  E-value: 5.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1407423174  62 AILGYHrkPPMIDNEyvdKMCEIPLAIAACPTAAIRPSKvelpngtqvNSVAIKQERCMFCGNCYT 127
Cdd:COG2221     3 GIIGTW--PPKIDEE---KCIGCGLCVAVCPTGAISLDD---------GKLVIDEEKCIGCGACIR 54
 
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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