NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1182682409|emb|SMF04661|]
View 

Cysteine dioxygenase [Bacillus subtilis]

Protein Classification

cysteine dioxygenase family protein( 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
 48-145 1.25e-31

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: 108.93  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  48 YGRNAIYRNNELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLNSIYRSTGEHAELSNSyFVHE--GECL-ISTKGLI 124
Cdd:cd10548     1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLSGEE-TLEEtpGDVTyINPDGGI 79

                          90       100
                  ....*....|....*....|.
gi 1182682409 125 HKMSNPTSERMVSLHVYSPPL 145
Cdd:cd10548    80 HRVENPSDEPAVSLHLYSPPL 100
 
Name Accession Description Interval E-value
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 48-145 1.25e-31

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: 108.93  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  48 YGRNAIYRNNELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLNSIYRSTGEHAELSNSyFVHE--GECL-ISTKGLI 124
Cdd:cd10548     1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLSGEE-TLEEtpGDVTyINPDGGI 79

                          90       100
                  ....*....|....*....|.
gi 1182682409 125 HKMSNPTSERMVSLHVYSPPL 145
Cdd:cd10548    80 HRVENPSDEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 43-152 1.48e-11

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 59.19  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  43 PDQYA------YGRNAIYRNNE--LEIIVINIPPNKETTVHDHGqSIGCAMVLEGKLLNSIYRSTGEHAEL--SNSYFVH 112
Cdd:COG5553    49 PAEFAepdpdrYARYLLYADPDgrFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDGARLepGGEVVLG 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1182682409 113 EGE-CLISTKGLIHKMSNPTSERMVSLHVYSPPLEDMTVFE 152
Cdd:COG5553   128 PGDvIALSPPGDIHQVENAGDEPAISLHVYGGNIGRLVRFV 168
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 44-154 2.82e-09

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: 53.11  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  44 DQYAYGRNAIYRNN-ELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLNSIYRSTGEHAELS----NSYFVHEGECLI 118
Cdd:pfam05995  53 DPEGYTRNLVDAGNgKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSdgvdRERRLSNGTGYA 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1182682409 119 STKGLIHKMSNPTSER-MVSLHVYSPPLEDMTVFEEQ 154
Cdd:pfam05995 133 NDRHGLHRVENESHDRhAVSLHLYYPPLPTCRAFDRR 169
 
Name Accession Description Interval E-value
cupin_CDO cd10548
cysteine dioxygenase, cupin domain; This family contains cysteine dioxygenase (CDO; EC 1.13.11. ...
 48-145 1.25e-31

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: 108.93  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  48 YGRNAIYRNNELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLNSIYRSTGEHAELSNSyFVHE--GECL-ISTKGLI 124
Cdd:cd10548     1 YTRNLLYRDPDFELLLLCWPPGQGSPIHDHGGSWCVVKVLEGELTETRYRRPDDGSLSGEE-TLEEtpGDVTyINPDGGI 79

                          90       100
                  ....*....|....*....|.
gi 1182682409 125 HKMSNPTSERMVSLHVYSPPL 145
Cdd:cd10548    80 HRVENPSDEPAVSLHLYSPPL 100
COG5553 COG5553
Predicted metal-dependent enzyme of the double-stranded beta helix superfamily [General ...
 43-152 1.48e-11

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


Pssm-ID: 444296  Cd Length: 179  Bit Score: 59.19  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  43 PDQYA------YGRNAIYRNNE--LEIIVINIPPNKETTVHDHGqSIGCAMVLEGKLLNSIYRSTGEHAEL--SNSYFVH 112
Cdd:COG5553    49 PAEFAepdpdrYARYLLYADPDgrFSVVAFVWGPGQKTPIHDHG-TWGVIGVLRGAEKNTRYRRTDDGARLepGGEVVLG 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1182682409 113 EGE-CLISTKGLIHKMSNPTSERMVSLHVYSPPLEDMTVFE 152
Cdd:COG5553   128 PGDvIALSPPGDIHQVENAGDEPAISLHVYGGNIGRLVRFV 168
CDO_I pfam05995
Cysteine dioxygenase type I; Cysteine dioxygenase type I (EC:1.13.11.20) converts cysteine to ...
 44-154 2.82e-09

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: 53.11  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  44 DQYAYGRNAIYRNN-ELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLNSIYRSTGEHAELS----NSYFVHEGECLI 118
Cdd:pfam05995  53 DPEGYTRNLVDAGNgKSNLMILCWGPGTGSSWHDHTDSHCFFKTLAGELKETALAWPLKTLELSdgvdRERRLSNGTGYA 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1182682409 119 STKGLIHKMSNPTSER-MVSLHVYSPPLEDMTVFEEQ 154
Cdd:pfam05995 133 NDRHGLHRVENESHDRhAVSLHLYYPPLPTCRAFDRR 169
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 53-138 3.22e-05

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 40.64  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  53 IYRNNELEIIVINIPPNKETTVHDHGQS-IGcaMVLEGKLLNSIYRSTGEHAELSNSYFVHEGEclistkglIHKMSNPT 131
Cdd:cd06975    13 FFVGSWTEIMLSYIPPGAKMPLHQHREEqIG--MILNGELEMTVGGEEQELEPLGDVYYAPPNV--------PHGAVNPS 82


                  ....*..
gi 1182682409 132 SERMVSL 138
Cdd:cd06975    83 DETAVLL 89
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 58-141 6.62e-05

Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380364 [Multi-domain]  Cd Length: 102  Bit Score: 39.78  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  58 ELEIIVINIPPNKETTVHDHgQSIGCAMVLEGKLlnSIYRSTGEhaelsnSYFVHEGECLISTKGLIHKMSNPTSERMVS 137
Cdd:cd02236    21 EITVLRITIPPGAELPWHTH-PVPNAGYVLSGEL--TVEYEDGK------KRTFKAGDAFVEAVNTWHRGRNGGDEPVEL 91


                  ....
gi 1182682409 138 LHVY 141
Cdd:cd02236    92 LVFY 95
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
53-145 7.20e-05

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 39.83  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  53 IYRNNELEIIVINIPPNKETTVHDHGQSIgCAMVLEGKLlnsIYRSTGEhaelsnSYFVHEGECLISTKGLIHKMSNPTS 132
Cdd:COG1917    17 ADGEDELEVVRVTFEPGARTPWHSHPGEE-LIYVLEGEG---EVEVGGE------EYELKPGDVVFIPPGVPHAFRNLGD 86

                          90
                  ....*....|...
gi 1182682409 133 ERMVSLHVYSPPL 145
Cdd:COG1917    87 EPAVLLVVFSPGL 99
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
56-144 1.50e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 39.35  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  56 NNELEIIVINIPPNKETTVHDHGQSIGCAMVLEGKLLnsIYrsTGEHaelsnSYFVHEGECLISTKGLIHKMSNPTSERM 135
Cdd:COG0662    24 GERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGE--VT--IGDE-----EVELKAGDSVYIPAGVPHRLRNPGDEPL 94


                  ....*....
gi 1182682409 136 VSLHVYSPP 144
Cdd:COG0662    95 ELLEVQAPA 103
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 63-141 3.54e-04

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 37.24  E-value: 3.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1182682409  63 VINIPPNKETTVHDHGQSIGCAMVLEGKLlnsiyRSTGEhaelSNSYFVHEGECLISTKGLIHKMSNPTSERMVSLHVY 141
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEG-----ELTVD----GEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 61-141 1.96e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 35.15  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  61 IIVINIPPNKETTVHDHGQSIGCAMVLEGKLLnsIYRSTGEHAELsnsyfvHEGECLISTKGLIHKMSNPTSERMVSLHV 140
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGE--LTLDDGETVEL------KAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72


                  .
gi 1182682409 141 Y 141
Cdd:cd02208    73 S 73
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
 53-140 3.52e-03

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 35.32  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1182682409  53 IYRNNELEIIVINIPPNKETTVHDHGQS-IGcaMVLEGKLLNSIYRSTGEHAELSNSYfvhegeclISTKGLIHKMSNPT 131
Cdd:cd20307    18 SFQCQDTVVQLSYIAPGAVVELHQHPESqIG--MVLSGELEMNVGGVKKVMEPLQDVY--------VAPPNVPHGAVNPS 87


                  ....*....
gi 1182682409 132 SERMVSLHV 140
Cdd:cd20307    88 SEEAVGLDI 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH