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Conserved domains on  [gi|227484185|emb|CAY20668|]
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dissimilatory sulfite reductase beta subunit, partial [bacterium enrichment culture clone Dan60S_dsr16E]

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 ...
 26-250 1.55e-140

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: 397.67  E-value: 1.55e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185   26 VIKENYGKWKYHEILEPGVLVHVSETGAEVYTVRVGAARLLSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQ 105
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  106 PLIDELKsrGNWFPIGGTGASVT-NIVHTQGWVHCHTPAIDASGIVKAVMDELFDYFGSHKLPAQVRISLACCLNMCGAV 184
Cdd:TIGR02066  81 PLIDELE--EVGFPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227484185  185 HCSDIAILGVHRKPPFVEHERVQNVCEIPLVIAACPTAAIKPKKVGDYKSIEINEKRCMFCGNCYT 250
Cdd:TIGR02066 159 HASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRRDGKNKSLEVDVEKCIYCGNCYT 224
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 26-250 1.55e-140

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: 397.67  E-value: 1.55e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185   26 VIKENYGKWKYHEILEPGVLVHVSETGAEVYTVRVGAARLLSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQ 105
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  106 PLIDELKsrGNWFPIGGTGASVT-NIVHTQGWVHCHTPAIDASGIVKAVMDELFDYFGSHKLPAQVRISLACCLNMCGAV 184
Cdd:TIGR02066  81 PLIDELE--EVGFPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227484185  185 HCSDIAILGVHRKPPFVEHERVQNVCEIPLVIAACPTAAIKPKKVGDYKSIEINEKRCMFCGNCYT 250
Cdd:TIGR02066 159 HASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRRDGKNKSLEVDVEKCIYCGNCYT 224
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 124-201 1.47e-20

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: 85.01  E-value: 1.47e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227484185  124 GASVTNIVHTQGWVHCHTPAIDASGIVKAVMDELFDYFGSHKLPAQVRISLACCLNMCGAVHCSDIAILGVHRKPPFV 201
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 66-197 9.17e-07

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: 49.35  E-value: 9.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  66 LSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQPLIDELKSRGnWFPIGGTGASVTNIV--HTQGwvHCHTPA 143
Cdd:COG0155   66 LTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVG-LTTIGACGDVVRNVTasPLAG--VDPDEL 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227484185 144 IDASGIVKAvmdeLFDYFGSH----KLPaqvR---ISLACCLNMCGAVHCSDIAILGVHRK 197
Cdd:COG0155  143 FDVRPYAEA----ISQHLLGHpeytYLP---RkfkIAFSGPPEDDADVEINDLGFIAVVKE 196
PLN02431 PLN02431
ferredoxin--nitrite reductase
 60-193 2.36e-04

ferredoxin--nitrite reductase


Pssm-ID: 178050 [Multi-domain]  Cd Length: 587  Bit Score: 42.07  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  60 VGAARLLSVDLiREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQPLIDE-LKSRGNWFPiggtGASVTNIVHTQGWVH 138
Cdd:PLN02431 402 VPVGRLQAADM-DELARLADEYGSGELRLTVEQNIIIPNVPNSKVEALLAEpLLQRFSPNP----GLLLKGLVACTGNQF 476

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 227484185 139 CHTPAIDASGIVKAVMDELFDYFgshKLPAQVRISLACCLNMCGAVHCSDIAILG 193
Cdd:PLN02431 477 CGQAIIETKARALKVTEELERLV---EVPRPVRMHWTGCPNSCGQVQVADIGFMG 528
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 218-248 3.05e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 36.61  E-value: 3.05e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 227484185 218 ACPTAAIKPKKVGDY-KSIEINEKRCMFCGNC 248
Cdd:cd10549   17 ACPTDAIELGPNGAIaRGPEIDEDKCVFCGAC 48
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 26-250 1.55e-140

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: 397.67  E-value: 1.55e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185   26 VIKENYGKWKYHEILEPGVLVHVSETGAEVYTVRVGAARLLSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQ 105
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  106 PLIDELKsrGNWFPIGGTGASVT-NIVHTQGWVHCHTPAIDASGIVKAVMDELFDYFGSHKLPAQVRISLACCLNMCGAV 184
Cdd:TIGR02066  81 PLIDELE--EVGFPVGGTGDAVKgNIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANMCGGV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227484185  185 HCSDIAILGVHRKPPFVEHERVQNVCEIPLVIAACPTAAIKPKKVGDYKSIEINEKRCMFCGNCYT 250
Cdd:TIGR02066 159 HASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPRRDGKNKSLEVDVEKCIYCGNCYT 224
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 124-201 1.47e-20

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: 85.01  E-value: 1.47e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227484185  124 GASVTNIVHTQGWVHCHTPAIDASGIVKAVMDELFDYFGSHKLPAQVRISLACCLNMCGAVHCSDIAILGVHRKPPFV 201
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEI 78
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 47-112 1.35e-14

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: 66.40  E-value: 1.35e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227484185   47 HVSETGAevYTVRVGA-ARLLSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQPLIDELK 112
Cdd:pfam03460   1 HPQKDGD--YMVRVRVpGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEELA 65
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 66-197 9.17e-07

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: 49.35  E-value: 9.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  66 LSVDLIREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQPLIDELKSRGnWFPIGGTGASVTNIV--HTQGwvHCHTPA 143
Cdd:COG0155   66 LTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVG-LTTIGACGDVVRNVTasPLAG--VDPDEL 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227484185 144 IDASGIVKAvmdeLFDYFGSH----KLPaqvR---ISLACCLNMCGAVHCSDIAILGVHRK 197
Cdd:COG0155  143 FDVRPYAEA----ISQHLLGHpeytYLP---RkfkIAFSGPPEDDADVEINDLGFIAVVKE 196
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 190-250 1.89e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.58  E-value: 1.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227484185 190 AILGVHrkPPFVEHERVQNvCeiPLVIAACPTAAIKPKKvgdyKSIEINEKRCMFCGNCYT 250
Cdd:COG2221    3 GIIGTW--PPKIDEEKCIG-C--GLCVAVCPTGAISLDD----GKLVIDEEKCIGCGACIR 54
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 208-248 1.07e-04

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 39.34  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 227484185 208 NVCEiplviAACPTAAIKPKKVGDYKSIEINEKRCMFCGNC 248
Cdd:COG1143    8 GLCV-----RVCPVDAITIEDGEPGKVYVIDPDKCIGCGLC 43
PLN02431 PLN02431
ferredoxin--nitrite reductase
 60-193 2.36e-04

ferredoxin--nitrite reductase


Pssm-ID: 178050 [Multi-domain]  Cd Length: 587  Bit Score: 42.07  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185  60 VGAARLLSVDLiREICDIADKHCGGYVRWTTRNNIEFMVDDKSKVQPLIDE-LKSRGNWFPiggtGASVTNIVHTQGWVH 138
Cdd:PLN02431 402 VPVGRLQAADM-DELARLADEYGSGELRLTVEQNIIIPNVPNSKVEALLAEpLLQRFSPNP----GLLLKGLVACTGNQF 476

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 227484185 139 CHTPAIDASGIVKAVMDELFDYFgshKLPAQVRISLACCLNMCGAVHCSDIAILG 193
Cdd:PLN02431 477 CGQAIIETKARALKVTEELERLV---EVPRPVRMHWTGCPNSCGQVQVADIGFMG 528
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
176-248 1.58e-03

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 39.24  E-value: 1.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227484185 176 CCLNMCGAVHCSDIAILGVHRKPPFVEHERVQNVCEIP-LVIAACPTAAIKPkkvgDYKSIEINEKRCMFCGNC 248
Cdd:COG4624   59 CCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCyPCVRACPVKAIKV----DDGKAEIDEEKCISCGQC 128
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 218-248 3.05e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 36.61  E-value: 3.05e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 227484185 218 ACPTAAIKPKKVGDY-KSIEINEKRCMFCGNC 248
Cdd:cd10549   17 ACPTDAIELGPNGAIaRGPEIDEDKCVFCGAC 48
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 216-249 3.46e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 36.61  E-value: 3.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 227484185 216 IAACPTAAIK-----PKKVGDYKSIEINEKRCMFCGNCY 249
Cdd:cd10549   49 VEVCPTGAIEltpegKEYVPKEKEAEIDEEKCIGCGLCV 87
nirA PRK09567
NirA family protein;
1-95 3.74e-03

NirA family protein;


Pssm-ID: 236573 [Multi-domain]  Cd Length: 593  Bit Score: 38.07  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484185   1 FDPNDIMKDHITDIGPPKYDKFFppvikenygKWKYHEilepgvLVHVSETgAEVYTVRVG-AARLLSVDLIREICDIAD 79
Cdd:PRK09567  78 FDAWDRLKAQAAAGAFPKPADNF---------RWKYHG------LFYVAPA-QDSYMCRLRiPNGILTHWQFAGLADLAD 141

                         90
                 ....*....|....*.
gi 227484185  80 KHCGGYVRWTTRNNIE 95
Cdd:PRK09567 142 RHGGGYSHVTTRANLQ 157
 
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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