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Conserved domains on  [gi|522174095|ref|WP_020682644|]
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ureidoglycolate lyase [Marinobacterium rhizophilum]

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;
1-162 2.15e-92

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 265.20  E-value: 2.15e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVET-GSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:PRK03606   1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVaGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  80 QAFIPMRGNPFLILVAPPGDDlTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSEE 159
Cdd:PRK03606  81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                 ...
gi 522174095 160 IML 162
Cdd:PRK03606 160 IIA 162
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-162 2.15e-92

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 265.20  E-value: 2.15e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVET-GSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:PRK03606   1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVaGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  80 QAFIPMRGNPFLILVAPPGDDlTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSEE 159
Cdd:PRK03606  81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                 ...
gi 522174095 160 IML 162
Cdd:PRK03606 160 IIA 162
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
2-160 6.14e-85

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 246.70  E-value: 6.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   2 QRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVETGSEGTPIISIFRAQTLPMPLRVRMMERHPLGSQA 81
Cdd:COG3194    5 ATLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFRAQPRALPLRITMLERHPLGSQA 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522174095  82 FIPMRGNPFLILVAPPGDDLTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSEEI 160
Cdd:COG3194   85 FIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-156 1.88e-82

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: 240.20  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095    1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVE-TGSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDnNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522174095   80 QAFIPMRGNPFLILVAPPGDDLTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFAD 156
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
53-142 7.16e-46

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: 144.98  E-value: 7.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  53 PIISIFRAQTLPMPLRVRMMERHPLGSQAFIPMRGNPFLILVAPPGDDLTS--SQLRAFYSDGSQGVNYRPGVWHHPILA 130
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDGKPdlSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 522174095 131 LTDQDEFLVVDR 142
Cdd:cd20298   81 LDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-162 2.15e-92

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 265.20  E-value: 2.15e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVET-GSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:PRK03606   1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVaGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  80 QAFIPMRGNPFLILVAPPGDDlTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSEE 159
Cdd:PRK03606  81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                 ...
gi 522174095 160 IML 162
Cdd:PRK03606 160 IIA 162
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
2-160 6.14e-85

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 246.70  E-value: 6.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   2 QRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVETGSEGTPIISIFRAQTLPMPLRVRMMERHPLGSQA 81
Cdd:COG3194    5 ATLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFRAQPRALPLRITMLERHPLGSQA 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522174095  82 FIPMRGNPFLILVAPPGDDLTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSEEI 160
Cdd:COG3194   85 FIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-156 1.88e-82

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: 240.20  E-value: 1.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095    1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVE-TGSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDnNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522174095   80 QAFIPMRGNPFLILVAPPGDDLTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFAD 156
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157
PRK13395 PRK13395
ureidoglycolate lyase;
1-166 5.79e-62

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 188.86  E-value: 5.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095   1 MQRLKIEALSKEAFAPFGDLIASEGHDFFMINNGSTRRYHRLAEVE-TGSEGTPIISIFRAQTLPMPLRVRMMERHPLGS 79
Cdd:PRK13395   1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDvTGDGGRPLVSLFRAQPRALPVAITMMERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  80 QAFIPMRG-NPFLILVApPGDDLTSSQLRAFYSDGSQGVNYRPGVWHHPILALTDQDEFLVVDRAGPGNNCDEFFFADSE 158
Cdd:PRK13395  81 QAFIPLAAvSRYAVVVA-PAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPW 159

                 ....*...
gi 522174095 159 EIMLDPKH 166
Cdd:PRK13395 160 RLEFEDAT 167
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
53-142 7.16e-46

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: 144.98  E-value: 7.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522174095  53 PIISIFRAQTLPMPLRVRMMERHPLGSQAFIPMRGNPFLILVAPPGDDLTS--SQLRAFYSDGSQGVNYRPGVWHHPILA 130
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDGKPdlSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                         90
                 ....*....|..
gi 522174095 131 LTDQDEFLVVDR 142
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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