NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|757798254|ref|WP_043015456|]
View 

MULTISPECIES: ureidoglycolate lyase [Citrobacter]

Protein Classification

ureidoglycolate lyase( domain architecture ID 10012053)

ureidoglycolate lyase catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-160 1.09e-81

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 237.86  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   1 MKLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGTQ 79
Cdd:PRK03606   2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGgRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  80 AFMPMNGEAFVVIVALGEDKpDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGS-DNCDVESIPAHELC 158
Cdd:PRK03606  82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPgDNLEEHFFPEDELI 160

                 ..
gi 757798254 159 FA 160
Cdd:PRK03606 161 IA 162
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-160 1.09e-81

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 237.86  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   1 MKLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGTQ 79
Cdd:PRK03606   2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGgRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  80 AFMPMNGEAFVVIVALGEDKpDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGS-DNCDVESIPAHELC 158
Cdd:PRK03606  82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPgDNLEEHFFPEDELI 160

                 ..
gi 757798254 159 FA 160
Cdd:PRK03606 161 IA 162
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
2-153 1.70e-71

Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442427  Cd Length: 164  Bit Score: 212.42  E-value: 1.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   2 KLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQDRTLISINRAQPAAMPIVVHELERHPLGTQAF 81
Cdd:COG3194    6 TLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFRAQPRALPLRITMLERHPLGSQAF 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757798254  82 MPMNGEAFVVIVALGEDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGS-DNCDVESIP 153
Cdd:COG3194   86 IPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTgEDCEEHDLD 158
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-153 1.91e-60

Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ureidoglycolate, an intermediate of purine catabolism, releasing urea. The enzyme has in the past been wrongly assigned to EC:3.5.3.19, enzymes which release ammonia from ureidoglycolate.


Pssm-ID: 427721  Cd Length: 162  Bit Score: 184.34  E-value: 1.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254    1 MKLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGTQ 79
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGgRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757798254   80 AFMPMNGEAFVVIVALGEDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGSD-NCDVESIP 153
Cdd:pfam04115  82 AFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGpNCEEVAFD 156
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
52-141 3.08e-44

ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes the cupin-fold protein, ureidoglycolate hydrolase (AllA; EC 3.5.3.19), which is involved in the breakdown of allantoin under aerobic conditions. Allantoin is the key intermediate of nitrogen fixation in bacteria, and its degradation occurs in several steps. AllA is involved in the third step of this pathway which consists of hydrolysis of (S)-ureidoglycolate to yield glyoxylate, ammonia, and CO2. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380432  Cd Length: 92  Bit Score: 140.75  E-value: 3.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  52 TLISINRAQPAAMPIVVHELERHPLGTQAFMPMNGEAFVVIVALG--EDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFA 129
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPgdDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 757798254 130 WQTVTNFLTVDR 141
Cdd:cd20298   81 LDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-160 1.09e-81

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 237.86  E-value: 1.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   1 MKLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGTQ 79
Cdd:PRK03606   2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGgRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  80 AFMPMNGEAFVVIVALGEDKpDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGS-DNCDVESIPAHELC 158
Cdd:PRK03606  82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPgDNLEEHFFPEDELI 160

                 ..
gi 757798254 159 FA 160
Cdd:PRK03606 161 IA 162
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
2-153 1.70e-71

Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442427  Cd Length: 164  Bit Score: 212.42  E-value: 1.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   2 KLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQDRTLISINRAQPAAMPIVVHELERHPLGTQAF 81
Cdd:COG3194    6 TLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFRAQPRALPLRITMLERHPLGSQAF 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757798254  82 MPMNGEAFVVIVALGEDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGS-DNCDVESIP 153
Cdd:COG3194   86 IPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTgEDCEEHDLD 158
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-153 1.91e-60

Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ureidoglycolate, an intermediate of purine catabolism, releasing urea. The enzyme has in the past been wrongly assigned to EC:3.5.3.19, enzymes which release ammonia from ureidoglycolate.


Pssm-ID: 427721  Cd Length: 162  Bit Score: 184.34  E-value: 1.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254    1 MKLEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGTQ 79
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGgRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757798254   80 AFMPMNGEAFVVIVALGEDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGSD-NCDVESIP 153
Cdd:pfam04115  82 AFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGpNCEEVAFD 156
PRK13395 PRK13395
ureidoglycolate lyase;
1-156 3.24e-48

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 153.42  E-value: 3.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254   1 MK-LEVLPLNQQTFSAYGDVIEIHKRDFFHINDGLVERYHDLANVEILEQD-RTLISINRAQPAAMPIVVHELERHPLGT 78
Cdd:PRK13395   1 MKtLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGgRPLVSLFRAQPRALPVAITMMERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  79 QAFMPMNGEA-FVVIVALGED-KPDlsTLKAFISNGLQGVNYHRNVWHHPLFAWQTVTNFLTVDRGGSdNCDVESIPAHE 156
Cdd:PRK13395  81 QAFIPLAAVSrYAVVVAPAGEfRPD--EMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGP-QPNCDEIPLDT 157
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
52-141 3.08e-44

ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes the cupin-fold protein, ureidoglycolate hydrolase (AllA; EC 3.5.3.19), which is involved in the breakdown of allantoin under aerobic conditions. Allantoin is the key intermediate of nitrogen fixation in bacteria, and its degradation occurs in several steps. AllA is involved in the third step of this pathway which consists of hydrolysis of (S)-ureidoglycolate to yield glyoxylate, ammonia, and CO2. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380432  Cd Length: 92  Bit Score: 140.75  E-value: 3.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757798254  52 TLISINRAQPAAMPIVVHELERHPLGTQAFMPMNGEAFVVIVALG--EDKPDLSTLKAFISNGLQGVNYHRNVWHHPLFA 129
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPgdDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 757798254 130 WQTVTNFLTVDR 141
Cdd:cd20298   81 LDAPADFLVLDR 92
 
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