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Conserved domains on  [gi|490578091|ref|WP_004443111|]
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MULTISPECIES: ureidoglycolate lyase [Rhizobium/Agrobacterium group]

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

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List of domain hits

Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
4-163 9.25e-96

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 273.68  E-value: 9.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   4 FLNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGSQS 83
Cdd:PRK03606   3 TLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  84 FSPLSGRPFLVVVAEDDGGRPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYVIAE 163
Cdd:PRK03606  83 FIPLNGRPFLVVVAPDGDGDPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDELIIA 162
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
4-163 9.25e-96

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 273.68  E-value: 9.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   4 FLNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGSQS 83
Cdd:PRK03606   3 TLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  84 FSPLSGRPFLVVVAEDDGGRPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYVIAE 163
Cdd:PRK03606  83 FIPLNGRPFLVVVAPDGDGDPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDELIIA 162
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
2-161 5.39e-83

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: 241.74  E-value: 5.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091    2 TDFLNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGS 81
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   82 QSFSPLSGRPFLVVVAEDDGGRP-GRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYV 160
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDlGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDEPLT 160

                  .
gi 490578091  161 I 161
Cdd:pfam04115 161 V 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-162 6.08e-78

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 228.98  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   1 MTDF--LNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGaRVILNIFRGQPRAFPHEIEMMERHP 78
Cdd:COG3194    1 MSTSatLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEG-RAGISIFRAQPRALPLRITMLERHP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  79 LGSQSFSPLSGRPFLVVVAEDDGG-RPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDR 157
Cdd:COG3194   80 LGSQAFIPLSGKPFLVVVAPPGGGpDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDT 159

                 ....*
gi 490578091 158 PYVIA 162
Cdd:COG3194  160 PLEIE 164
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
55-143 1.32e-41

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: 134.20  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  55 VILNIFRGQPRAFPHEIEMMERHPLGSQSFSPLSGRPFLVVVAE-DDGGRP--GRPRVFLARGDQGVNYRRNVWHYPLMP 131
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPpGDDGKPdlSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 490578091 132 LQAVSDFLVADR 143
Cdd:cd20298   81 LDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
4-163 9.25e-96

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 273.68  E-value: 9.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   4 FLNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGSQS 83
Cdd:PRK03606   3 TLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  84 FSPLSGRPFLVVVAEDDGGRPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYVIAE 163
Cdd:PRK03606  83 FIPLNGRPFLVVVAPDGDGDPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDELIIA 162
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
2-161 5.39e-83

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: 241.74  E-value: 5.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091    2 TDFLNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGS 81
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   82 QSFSPLSGRPFLVVVAEDDGGRP-GRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYV 160
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDlGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDEPLT 160

                  .
gi 490578091  161 I 161
Cdd:pfam04115 161 V 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-162 6.08e-78

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 228.98  E-value: 6.08e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   1 MTDF--LNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGaRVILNIFRGQPRAFPHEIEMMERHP 78
Cdd:COG3194    1 MSTSatLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEG-RAGISIFRAQPRALPLRITMLERHP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  79 LGSQSFSPLSGRPFLVVVAEDDGG-RPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDR 157
Cdd:COG3194   80 LGSQAFIPLSGKPFLVVVAPPGGGpDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDT 159

                 ....*
gi 490578091 158 PYVIA 162
Cdd:COG3194  160 PLEIE 164
PRK13395 PRK13395
ureidoglycolate lyase;
5-162 5.86e-64

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 193.87  E-value: 5.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091   5 LNIQPLTKEAFASFGDVIETTPSSMRYINGGQTERHHALAAPEAAGEGARVILNIFRGQPRAFPHEIEMMERHPLGSQSF 84
Cdd:PRK13395   4 LRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGSQAF 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490578091  85 SPLSGR-PFLVVVAEDDGGRPGRPRVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADRDGPGNNLEEYFFDRPYVIA 162
Cdd:PRK13395  84 IPLAAVsRYAVVVAPAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPWRLE 162
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
55-143 1.32e-41

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: 134.20  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490578091  55 VILNIFRGQPRAFPHEIEMMERHPLGSQSFSPLSGRPFLVVVAE-DDGGRP--GRPRVFLARGDQGVNYRRNVWHYPLMP 131
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPpGDDGKPdlSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 490578091 132 LQAVSDFLVADR 143
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.
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