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Conserved domains on  [gi|334184709|ref|NP_001189686|]
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ureidoglycolate hydrolase [Arabidopsis thaliana]

Protein Classification

ureidoglycolate lyase( domain architecture ID 10007036)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
10-174 6.98e-29

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


:

Pssm-ID: 442427  Cd Length: 164  Bit Score: 104.95  E-value: 6.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  10 LIPIEATPENFAEYGQVIEASR-------DGAGFGPHDAQLDLS--RGTPRLYILRLKETPLGFF--KITHHAKVTQCLG 78
Cdd:COG3194    7 LPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAQPRALPLRitMLERHPLGSQAFI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  79 SIGGDVWYMGVAKPSliedddddgrsvdtvksksGHlyipPEVEEIRVFRFSGPKFVKLHRGTWHAGPLFSGsSFMDFYN 158
Cdd:COG3194   87 PLSGKPFLVVVAPPG-------------------GG----PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD-DPGDFLV 142

                        170
                 ....*....|....*.
gi 334184709 159 LELSNTNvVDHTSHDF 174
Cdd:COG3194  143 VDRSGTG-EDCEEHDL 157
 
Name Accession Description Interval E-value
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
10-174 6.98e-29

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 104.95  E-value: 6.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  10 LIPIEATPENFAEYGQVIEASR-------DGAGFGPHDAQLDLS--RGTPRLYILRLKETPLGFF--KITHHAKVTQCLG 78
Cdd:COG3194    7 LPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAQPRALPLRitMLERHPLGSQAFI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  79 SIGGDVWYMGVAKPSliedddddgrsvdtvksksGHlyipPEVEEIRVFRFSGPKFVKLHRGTWHAGPLFSGsSFMDFYN 158
Cdd:COG3194   87 PLSGKPFLVVVAPPG-------------------GG----PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD-DPGDFLV 142

                        170
                 ....*....|....*.
gi 334184709 159 LELSNTNvVDHTSHDF 174
Cdd:COG3194  143 VDRSGTG-EDCEEHDL 157
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
 118-156 6.04e-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: 6.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 334184709 118 PPEVEEIRVFRFSGPKFVKLHRGTWHAGPLFSGSSfMDF 156
Cdd:cd20298   50 KPDLSTLRAFVADGGQGVNYHAGVWHHPLIALDAP-ADF 87
 
Name Accession Description Interval E-value
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
10-174 6.98e-29

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 104.95  E-value: 6.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  10 LIPIEATPENFAEYGQVIEASR-------DGAGFGPHDAQLDLS--RGTPRLYILRLKETPLGFF--KITHHAKVTQCLG 78
Cdd:COG3194    7 LPAEPLTAEAFAPFGDVIEADGapdfpinDGTTERYHDLALVDFggEGRAGISIFRAQPRALPLRitMLERHPLGSQAFI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184709  79 SIGGDVWYMGVAKPSliedddddgrsvdtvksksGHlyipPEVEEIRVFRFSGPKFVKLHRGTWHAGPLFSGsSFMDFYN 158
Cdd:COG3194   87 PLSGKPFLVVVAPPG-------------------GG----PDPETLRAFLTPGGQGVNYHRGTWHHPLLALD-DPGDFLV 142

                        170
                 ....*....|....*.
gi 334184709 159 LELSNTNvVDHTSHDF 174
Cdd:COG3194  143 VDRSGTG-EDCEEHDL 157
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
 118-156 6.04e-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: 6.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 334184709 118 PPEVEEIRVFRFSGPKFVKLHRGTWHAGPLFSGSSfMDF 156
Cdd:cd20298   50 KPDLSTLRAFVADGGQGVNYHAGVWHHPLIALDAP-ADF 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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