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Conserved domains on  [gi|447098748|ref|WP_001176004|]
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MULTISPECIES: cysteine dioxygenase family protein [Bacillus]

Protein Classification

cysteine dioxygenase( domain architecture ID 14410663)

cysteine dioxygenase 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

CATH:  2.60.120.10
EC:  1.13.11.20
Gene Ontology:  GO:0017172|GO:0008198
PubMed:  18019494|37396540|19478949|14697267
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 48-140 4.57e-24

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: 89.28  E-value: 4.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  48 YGRNVIYQSEFVEILVLNFPSKAKTFVHDHGISVGCILIVNGTLQNITYENNSERIE------EFTEGNIFTV-KKDTVH 120
Cdd:cd10548    1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLsgeetlEETPGDVTYInPDGGIH 80

                         90       100
                 ....*....|....*....|
gi 447098748 121 KMYNATDSAVITFHVYSPPL 140
Cdd:cd10548   81 RVENPSDEPAVSLHLYSPPL 100
 
Name Accession Description Interval E-value
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 48-140 4.57e-24

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: 89.28  E-value: 4.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  48 YGRNVIYQSEFVEILVLNFPSKAKTFVHDHGISVGCILIVNGTLQNITYENNSERIE------EFTEGNIFTV-KKDTVH 120
Cdd:cd10548    1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLsgeetlEETPGDVTYInPDGGIH 80

                         90       100
                 ....*....|....*....|
gi 447098748 121 KMYNATDSAVITFHVYSPPL 140
Cdd:cd10548   81 RVENPSDEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 47-147 4.34e-08

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 49.56  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  47 EYGRNVIYQSE---FvEILVLNFPSKAKTFVHDHGiSVGCILIVNGTLQNITYENNS-------ERIEEFTEGNIFTVK- 115
Cdd:COG5553   59 RYARYLLYADPdgrF-SVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDdgarlepGGEVVLGPGDVIALSp 136

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447098748 116 KDTVHKMYNATDSAVITFHVYSPPLKDVQIYE 147
Cdd:COG5553  137 PGDIHQVENAGDEPAISLHVYGGNIGRLVRFV 168
 
Name Accession Description Interval E-value
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 48-140 4.57e-24

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: 89.28  E-value: 4.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  48 YGRNVIYQSEFVEILVLNFPSKAKTFVHDHGISVGCILIVNGTLQNITYENNSERIE------EFTEGNIFTV-KKDTVH 120
Cdd:cd10548    1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLsgeetlEETPGDVTYInPDGGIH 80

                         90       100
                 ....*....|....*....|
gi 447098748 121 KMYNATDSAVITFHVYSPPL 140
Cdd:cd10548   81 RVENPSDEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 47-147 4.34e-08

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 49.56  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  47 EYGRNVIYQSE---FvEILVLNFPSKAKTFVHDHGiSVGCILIVNGTLQNITYENNS-------ERIEEFTEGNIFTVK- 115
Cdd:COG5553   59 RYARYLLYADPdgrF-SVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDdgarlepGGEVVLGPGDVIALSp 136

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447098748 116 KDTVHKMYNATDSAVITFHVYSPPLKDVQIYE 147
Cdd:COG5553  137 PGDIHQVENAGDEPAISLHVYGGNIGRLVRFV 168
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
50-140 5.93e-03

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 34.44  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447098748  50 RNVIYQSEFVEILVLNFPSKAKTFVHDHGISVgCILIVNGTLqniTYENNSERIEeFTEGNIFTVKKDTVHKMYNATDSA 129
Cdd:COG1917   14 RVLADGEDELEVVRVTFEPGARTPWHSHPGEE-LIYVLEGEG---EVEVGGEEYE-LKPGDVVFIPPGVPHAFRNLGDEP 88

                         90
                 ....*....|.
gi 447098748 130 VITFHVYSPPL 140
Cdd:COG1917   89 AVLLVVFSPGL 99
 
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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