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Conserved domains on  [gi|18034344|gb|AAL57476|]
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dissimilatory sulfite reductase beta subunit, partial [Desulfosudis oleivorans Hxd3]

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 ...
 33-244 8.14e-106

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: 309.85  E-value: 8.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344    33 VIAKNKGKWAYHEILEPGILVHVSETGDEVYTVRVGGCRLMSVTHIREICEIADKHCDGYLRFTTRNNIEFMVDSKDKVE 112
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344   113 PLKKDLAGrkfAGgsfkFPIGGTGAGVT-NIIHTQGWIHCHTPATDASGPVKATMDALFDHFQSMDLPAQVRVSLACCLN 191
Cdd:TIGR02066  81 PLIDELEE---VG----FPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCAN 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18034344   192 MCGAVHCSDIAILGYHRKPPMIEDEYLDKMCEIPLAVAACPTAAIKPV----KKTLE 244
Cdd:TIGR02066 154 MCGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRrdgkNKSLE 210
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 33-244 8.14e-106

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: 309.85  E-value: 8.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344    33 VIAKNKGKWAYHEILEPGILVHVSETGDEVYTVRVGGCRLMSVTHIREICEIADKHCDGYLRFTTRNNIEFMVDSKDKVE 112
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344   113 PLKKDLAGrkfAGgsfkFPIGGTGAGVT-NIIHTQGWIHCHTPATDASGPVKATMDALFDHFQSMDLPAQVRVSLACCLN 191
Cdd:TIGR02066  81 PLIDELEE---VG----FPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCAN 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18034344   192 MCGAVHCSDIAILGYHRKPPMIEDEYLDKMCEIPLAVAACPTAAIKPV----KKTLE 244
Cdd:TIGR02066 154 MCGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRrdgkNKSLE 210
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 136-213 1.58e-18

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: 79.62  E-value: 1.58e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034344   136 GAGVTNIIHTQGWIHCHTPATDASGPVKATMDALFDHFQSMDLPAQVRVSLACCLNMCGAVHCSDIAILGYHRKPPMI 213
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 60-103 2.66e-05

Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439925 [Multi-domain]  Cd Length: 519  Bit Score: 44.72  E-value: 2.66e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18034344  60 DEVYTVRV---GGcrLMSVTHIREICEIADKHCDGYLRFTTRNNIEF 103
Cdd:COG0155  52 DGAFMLRVripGG--VLTPEQLRALADIAREYGRGYLHLTTRQNIQL 96
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 33-244 8.14e-106

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: 309.85  E-value: 8.14e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344    33 VIAKNKGKWAYHEILEPGILVHVSETGDEVYTVRVGGCRLMSVTHIREICEIADKHCDGYLRFTTRNNIEFMVDSKDKVE 112
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034344   113 PLKKDLAGrkfAGgsfkFPIGGTGAGVT-NIIHTQGWIHCHTPATDASGPVKATMDALFDHFQSMDLPAQVRVSLACCLN 191
Cdd:TIGR02066  81 PLIDELEE---VG----FPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCAN 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18034344   192 MCGAVHCSDIAILGYHRKPPMIEDEYLDKMCEIPLAVAACPTAAIKPV----KKTLE 244
Cdd:TIGR02066 154 MCGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRrdgkNKSLE 210
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 136-213 1.58e-18

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: 79.62  E-value: 1.58e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034344   136 GAGVTNIIHTQGWIHCHTPATDASGPVKATMDALFDHFQSMDLPAQVRVSLACCLNMCGAVHCSDIAILGYHRKPPMI 213
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 54-119 7.80e-15

Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.


Pssm-ID: 377044 [Multi-domain]  Cd Length: 67  Bit Score: 67.17  E-value: 7.80e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034344    54 HVSETGDEVYTVRVGGCRLmSVTHIREICEIADKHCDGYLRFTTRNNIEFMVDSKDKVEPLKKDLA 119
Cdd:pfam03460   1 HPQKDGDYMVRVRVPGGRL-TAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEELA 65
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 60-103 2.66e-05

Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439925 [Multi-domain]  Cd Length: 519  Bit Score: 44.72  E-value: 2.66e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18034344  60 DEVYTVRV---GGcrLMSVTHIREICEIADKHCDGYLRFTTRNNIEF 103
Cdd:COG0155  52 DGAFMLRVripGG--VLTPEQLRALADIAREYGRGYLHLTTRQNIQL 96
 
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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