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Conserved domains on  [gi|1400600318|gb|PYQ13983|]
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cysteine dioxygenase [Acidobacteria bacterium]

Protein Classification

COG5553 family protein( domain architecture ID 10009427)

COG5553 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 10-177 3.64e-53

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


:

Pssm-ID: 444296  Cd Length: 179  Bit Score: 167.81  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  10 PLKRFVRDLKELLASTPGERDRVFGVKHRLVSLLGTPDWLPEPCRAGDAACYARHLFYQDPEDGFVLVAMVWGPGQCTGI 89
Cdd:COG5553     9 RLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVWGPGQKTPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  90 HDHaGVWCVEGVYEGNIQVTRFDPVGEVGetvRFSPGEAIRAGVGACGALIPPVEYHQITNDTPGTAISVHVYGRDLKVC 169
Cdd:COG5553    89 HDH-GTWGVIGVLRGAEKNTRYRRTDDGA---RLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLHVYGGNIGRL 164

                         170
                  ....*....|
gi 1400600318 170 N--IFDPLGG 177
Cdd:COG5553   165 VrfVFDPETG 174
 
Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 10-177 3.64e-53

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 167.81  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  10 PLKRFVRDLKELLASTPGERDRVFGVKHRLVSLLGTPDWLPEPCRAGDAACYARHLFYQDPEDGFVLVAMVWGPGQCTGI 89
Cdd:COG5553     9 RLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVWGPGQKTPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  90 HDHaGVWCVEGVYEGNIQVTRFDPVGEVGetvRFSPGEAIRAGVGACGALIPPVEYHQITNDTPGTAISVHVYGRDLKVC 169
Cdd:COG5553    89 HDH-GTWGVIGVLRGAEKNTRYRRTDDGA---RLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLHVYGGNIGRL 164

                         170
                  ....*....|
gi 1400600318 170 N--IFDPLGG 177
Cdd:COG5553   165 VrfVFDPETG 174
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 61-166 6.15e-34

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 116.25  E-value: 6.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  61 YARHLFYQDPedGFVLVAMVWGPGQCTGIHDHAGVWCVEGVYEGNIQVTRFDPVgevgETVRFSPGEAIRAGVGACGALI 140
Cdd:cd10548     1 YTRNLLYRDP--DFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRP----DDGSLSGEETLEETPGDVTYIN 74

                          90       100
                  ....*....|....*....|....*.
gi 1400600318 141 PPVEYHQITNDTPGTAISVHVYGRDL 166
Cdd:cd10548    75 PDGGIHRVENPSDEPAVSLHLYSPPL 100
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 61-173 1.92e-07

Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to cysteinesulphinic acid and is the rate-limiting step in sulphate production.


Pssm-ID: 428713  Cd Length: 169  Bit Score: 48.87  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  61 YARHLFYQDPeDGFVLVAMVWGPGQCTGIHDHAGVWCVEGVYEGNIQVTRF-------DPVGEVGETVRFSPGeairagv 133
Cdd:pfam05995  57 YTRNLVDAGN-GKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALawplktlELSDGVDRERRLSNG------- 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1400600318 134 gaCGALIPPVEYHQITNDTPGT-AISVHVYGRDLKVCNIFD 173
Cdd:pfam05995 129 --TGYANDRHGLHRVENESHDRhAVSLHLYYPPLPTCRAFD 167
 
Name Accession Description Interval E-value
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 10-177 3.64e-53

Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General function prediction only];


Pssm-ID: 444296  Cd Length: 179  Bit Score: 167.81  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  10 PLKRFVRDLKELLASTPGERDRVFGVKHRLVSLLGTPDWLPEPCRAGDAACYARHLFYQDPEDGFVLVAMVWGPGQCTGI 89
Cdd:COG5553     9 RLRRFIAALRALVDRGPDEREILAAVRPLLRRLVASDDWLPAEFAEPDPDRYARYLLYADPDGRFSVVAFVWGPGQKTPI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  90 HDHaGVWCVEGVYEGNIQVTRFDPVGEVGetvRFSPGEAIRAGVGACGALIPPVEYHQITNDTPGTAISVHVYGRDLKVC 169
Cdd:COG5553    89 HDH-GTWGVIGVLRGAEKNTRYRRTDDGA---RLEPGGEVVLGPGDVIALSPPGDIHQVENAGDEPAISLHVYGGNIGRL 164

                         170
                  ....*....|
gi 1400600318 170 N--IFDPLGG 177
Cdd:COG5553   165 VrfVFDPETG 174
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 61-166 6.15e-34

cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380416 [Multi-domain]  Cd Length: 100  Bit Score: 116.25  E-value: 6.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  61 YARHLFYQDPedGFVLVAMVWGPGQCTGIHDHAGVWCVEGVYEGNIQVTRFDPVgevgETVRFSPGEAIRAGVGACGALI 140
Cdd:cd10548     1 YTRNLLYRDP--DFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRP----DDGSLSGEETLEETPGDVTYIN 74

                          90       100
                  ....*....|....*....|....*.
gi 1400600318 141 PPVEYHQITNDTPGTAISVHVYGRDL 166
Cdd:cd10548    75 PDGGIHRVENPSDEPAVSLHLYSPPL 100
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 61-173 1.92e-07

Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to cysteinesulphinic acid and is the rate-limiting step in sulphate production.


Pssm-ID: 428713  Cd Length: 169  Bit Score: 48.87  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  61 YARHLFYQDPeDGFVLVAMVWGPGQCTGIHDHAGVWCVEGVYEGNIQVTRF-------DPVGEVGETVRFSPGeairagv 133
Cdd:pfam05995  57 YTRNLVDAGN-GKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALawplktlELSDGVDRERRLSNG------- 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1400600318 134 gaCGALIPPVEYHQITNDTPGT-AISVHVYGRDLKVCNIFD 173
Cdd:pfam05995 129 --TGYANDRHGLHRVENESHDRhAVSLHLYYPPLPTCRAFD 167
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
69-162 8.92e-04

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 37.14  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400600318  69 DPEDGFVLVAMVWGPGQCTGIHDHAG---VWCVEGvyEGNIQVTrfdpvgevGETVRFSPGEAIragvgacgaLIPPVEY 145
Cdd:COG1917    18 DGEDELEVVRVTFEPGARTPWHSHPGeelIYVLEG--EGEVEVG--------GEEYELKPGDVV---------FIPPGVP 78

                          90
                  ....*....|....*..
gi 1400600318 146 HQITNDTPGTAISVHVY 162
Cdd:COG1917    79 HAFRNLGDEPAVLLVVF 95
 
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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