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Conserved domains on  [gi|1693972343|gb|TPR78901|]
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ureidoglycolate lyase [Acinetobacter baumannii]

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;
10-173 2.20e-88

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 255.57  E-value: 2.20e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGE-AKAGISIFRnIKASVLPMEISMLERHPKG 88
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEgGRALISIFR-AQPRALPLEIRMLERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPLQEQKFLIIVAPALDEnipDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPH 168
Cdd:PRK03606   80 SQAFIPLNGRPFLVVVAPDGDG---DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPE 156

                  ....*
gi 1693972343 169 PIKIT 173
Cdd:PRK03606  157 DELII 161
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
10-173 2.20e-88

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 255.57  E-value: 2.20e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGE-AKAGISIFRnIKASVLPMEISMLERHPKG 88
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEgGRALISIFR-AQPRALPLEIRMLERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPLQEQKFLIIVAPALDEnipDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPH 168
Cdd:PRK03606   80 SQAFIPLNGRPFLVVVAPDGDG---DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPE 156

                  ....*
gi 1693972343 169 PIKIT 173
Cdd:PRK03606  157 DELII 161
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
10-172 6.00e-77

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: 226.71  E-value: 6.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEG-EAKAGISIFRNiKASVLPMEISMLERHPKG 88
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYqGGRAGISLFRA-QPRALPFEVKMLERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPLQEQKFLIIVAPALDEniPDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPH 168
Cdd:pfam04115  80 SQAFIPLGGSPYLVVVAPDGGG--PDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157

                  ....
gi 1693972343 169 PIKI 172
Cdd:pfam04115 158 PLTV 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
13-173 7.19e-77

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 226.67  E-value: 7.19e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  13 IQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGEAKAGISIFRnIKASVLPMEISMLERHPKGSQAF 92
Cdd:COG3194     7 LPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFR-AQPRALPLRITMLERHPLGSQAF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  93 IPLQEQKFLIIVAPalDENIPDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPHPIKI 172
Cdd:COG3194    86 IPLSGKPFLVVVAP--PGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163

                  .
gi 1693972343 173 T 173
Cdd:COG3194   164 E 164
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
62-154 3.58e-45

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: 143.83  E-value: 3.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  62 AGISIFRnIKASVLPMEISMLERHPKGSQAFIPLQEQKFLIIVAPALDENIPDISKLCAFVSDGKQSINYRAGTWHHPLL 141
Cdd:cd20298     1 PNLSIFR-AKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLI 79
                          90
                  ....*....|...
gi 1693972343 142 TFEAPSDFAVVDR 154
Cdd:cd20298    80 ALDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
10-173 2.20e-88

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 255.57  E-value: 2.20e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGE-AKAGISIFRnIKASVLPMEISMLERHPKG 88
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEgGRALISIFR-AQPRALPLEIRMLERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPLQEQKFLIIVAPALDEnipDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPH 168
Cdd:PRK03606   80 SQAFIPLNGRPFLVVVAPDGDG---DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPE 156

                  ....*
gi 1693972343 169 PIKIT 173
Cdd:PRK03606  157 DELII 161
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
10-172 6.00e-77

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: 226.71  E-value: 6.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEG-EAKAGISIFRNiKASVLPMEISMLERHPKG 88
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYqGGRAGISLFRA-QPRALPFEVKMLERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPLQEQKFLIIVAPALDEniPDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPH 168
Cdd:pfam04115  80 SQAFIPLGGSPYLVVVAPDGGG--PDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157

                  ....
gi 1693972343 169 PIKI 172
Cdd:pfam04115 158 PLTV 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
13-173 7.19e-77

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 226.67  E-value: 7.19e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  13 IQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGEAKAGISIFRnIKASVLPMEISMLERHPKGSQAF 92
Cdd:COG3194     7 LPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGEGRAGISIFR-AQPRALPLRITMLERHPLGSQAF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  93 IPLQEQKFLIIVAPalDENIPDISKLCAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFPHPIKI 172
Cdd:COG3194    86 IPLSGKPFLVVVAP--PGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163

                  .
gi 1693972343 173 T 173
Cdd:COG3194   164 E 164
PRK13395 PRK13395
ureidoglycolate lyase;
10-173 3.92e-50

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 159.20  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  10 MKNIQIQPLTIENFQPFGEVICCDGHDFFHINDAHTERYHALVETEFEGEAK-AGISIFRNiKASVLPMEISMLERHPKG 88
Cdd:PRK13395    1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGrPLVSLFRA-QPRALPVAITMMERHPLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  89 SQAFIPL-QEQKFLIIVAPAlDENIPDISKlcAFVSDGKQSINYRAGTWHHPLLTFEAPSDFAVVDRIGGGTNCDIFQFP 167
Cdd:PRK13395   80 SQAFIPLaAVSRYAVVVAPA-GEFRPDEMR--AFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLD 156

                  ....*.
gi 1693972343 168 HPIKIT 173
Cdd:PRK13395  157 TPWRLE 162
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
62-154 3.58e-45

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: 143.83  E-value: 3.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693972343  62 AGISIFRnIKASVLPMEISMLERHPKGSQAFIPLQEQKFLIIVAPALDENIPDISKLCAFVSDGKQSINYRAGTWHHPLL 141
Cdd:cd20298     1 PNLSIFR-AKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLI 79
                          90
                  ....*....|...
gi 1693972343 142 TFEAPSDFAVVDR 154
Cdd:cd20298    80 ALDAPADFLVLDR 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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