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Conserved domains on  [gi|1063705861|ref|NP_001325071|]
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ureidoglycolate hydrolase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AllA super family cl42124
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
91-262 1.17e-23

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


The actual alignment was detected with superfamily member COG3194:

Pssm-ID: 442427  Cd Length: 164  Bit Score: 94.16  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861  91 MAKSPvevKLIPIEATPENFADYGQVIEASR-------DGAGFGPNDAQLDLS--RGIPRFYIMRI--RDTPFDFSVLTH 159
Cdd:COG3194     1 MSTSA---TLPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAqpRALPLRITMLER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 160 HASVTQCLGSIGGHVWYLGVAKPtliedgDDGkmvdklksrsghlyapPAVEEIRVFRVSGPKFIKLNHGTWHVGPLFSD 239
Cdd:COG3194    78 HPLGSQAFIPLSGKPFLVVVAPP------GGG----------------PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD 135
                         170       180
                  ....*....|....*....|...
gi 1063705861 240 SYMDFYNLELSNTNaVDRTTYDF 262
Cdd:COG3194   136 DPGDFLVVDRSGTG-EDCEEHDL 157
 
Name Accession Description Interval E-value
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
91-262 1.17e-23

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 94.16  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861  91 MAKSPvevKLIPIEATPENFADYGQVIEASR-------DGAGFGPNDAQLDLS--RGIPRFYIMRI--RDTPFDFSVLTH 159
Cdd:COG3194     1 MSTSA---TLPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAqpRALPLRITMLER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 160 HASVTQCLGSIGGHVWYLGVAKPtliedgDDGkmvdklksrsghlyapPAVEEIRVFRVSGPKFIKLNHGTWHVGPLFSD 239
Cdd:COG3194    78 HPLGSQAFIPLSGKPFLVVVAPP------GGG----------------PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD 135
                         170       180
                  ....*....|....*....|...
gi 1063705861 240 SYMDFYNLELSNTNaVDRTTYDF 262
Cdd:COG3194   136 DPGDFLVVDRSGTG-EDCEEHDL 157
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
101-244 3.99e-04

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: 39.89  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 101 IPIEA-TPENFADYGQVIEASrDGAGFGPNDAQ----LDLSR-------GIPRFYIMRI--RDTPFDFSVLTHHASVTQC 166
Cdd:pfam04115   4 LTAEPlTAEAFAPFGDVIEAD-GAPSVIINQGTaeryHDLARvdnnyqgGRAGISLFRAqpRALPFEVKMLERHPLGSQA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705861 167 LGSIGGHVWYLGVAkptliEDGDdgkmvdklksrsghlyaPPAVEEIRVFRVSGPKFIKLNHGTWHvGPLFS-DSYMDF 244
Cdd:pfam04115  83 FIPLGGSPYLVVVA-----PDGG-----------------GPDLGTLRAFLAAGGQGVNYGRGTWH-HPLLVlGAPSDF 138
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
131-244 8.94e-03

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: 34.82  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 131 AQLDLSRGIPRfyimrirDTPFDFSVLTHHASVTQCLGSIGGHVWYLGVAKPtliedGDDGKmvdklksrsghlyapPAV 210
Cdd:cd20298     1 PNLSIFRAKPR-------PLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPP-----GDDGK---------------PDL 53
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063705861 211 EEIRVFRVSGPKFIKLNHGTWHVGPLFSDSYMDF 244
Cdd:cd20298    54 STLRAFVADGGQGVNYHAGVWHHPLIALDAPADF 87
 
Name Accession Description Interval E-value
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
91-262 1.17e-23

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 94.16  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861  91 MAKSPvevKLIPIEATPENFADYGQVIEASR-------DGAGFGPNDAQLDLS--RGIPRFYIMRI--RDTPFDFSVLTH 159
Cdd:COG3194     1 MSTSA---TLPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAqpRALPLRITMLER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 160 HASVTQCLGSIGGHVWYLGVAKPtliedgDDGkmvdklksrsghlyapPAVEEIRVFRVSGPKFIKLNHGTWHVGPLFSD 239
Cdd:COG3194    78 HPLGSQAFIPLSGKPFLVVVAPP------GGG----------------PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD 135
                         170       180
                  ....*....|....*....|...
gi 1063705861 240 SYMDFYNLELSNTNaVDRTTYDF 262
Cdd:COG3194   136 DPGDFLVVDRSGTG-EDCEEHDL 157
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
101-244 3.99e-04

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: 39.89  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 101 IPIEA-TPENFADYGQVIEASrDGAGFGPNDAQ----LDLSR-------GIPRFYIMRI--RDTPFDFSVLTHHASVTQC 166
Cdd:pfam04115   4 LTAEPlTAEAFAPFGDVIEAD-GAPSVIINQGTaeryHDLARvdnnyqgGRAGISLFRAqpRALPFEVKMLERHPLGSQA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705861 167 LGSIGGHVWYLGVAkptliEDGDdgkmvdklksrsghlyaPPAVEEIRVFRVSGPKFIKLNHGTWHvGPLFS-DSYMDF 244
Cdd:pfam04115  83 FIPLGGSPYLVVVA-----PDGG-----------------GPDLGTLRAFLAAGGQGVNYGRGTWH-HPLLVlGAPSDF 138
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
131-244 8.94e-03

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: 34.82  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705861 131 AQLDLSRGIPRfyimrirDTPFDFSVLTHHASVTQCLGSIGGHVWYLGVAKPtliedGDDGKmvdklksrsghlyapPAV 210
Cdd:cd20298     1 PNLSIFRAKPR-------PLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPP-----GDDGK---------------PDL 53
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063705861 211 EEIRVFRVSGPKFIKLNHGTWHVGPLFSDSYMDF 244
Cdd:cd20298    54 STLRAFVADGGQGVNYHAGVWHHPLIALDAPADF 87
 
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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