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Conserved domains on  [gi|1698818900|gb|TQI06705|]
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ureidoglycolate lyase [Pseudomonas aeruginosa]

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;
1-163 3.37e-109

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 307.96  E-value: 3.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  81 QAFIPLLGNPFLVVVAPLGDVpVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDEQ 160
Cdd:PRK03606   81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                  ...
gi 1698818900 161 LLL 163
Cdd:PRK03606  160 IIA 162
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-163 3.37e-109

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 307.96  E-value: 3.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  81 QAFIPLLGNPFLVVVAPLGDVpVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDEQ 160
Cdd:PRK03606   81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                  ...
gi 1698818900 161 LLL 163
Cdd:PRK03606  160 IIA 162
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-157 3.02e-88

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: 254.83  E-value: 3.02e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698818900  81 QAFIPLLGNPFLVVVAPLGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTE 157
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
3-161 2.98e-86

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 250.17  E-value: 2.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   3 TLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAqPEDNAIISIFSAEKLEMPLRIRMLERHPLGSQA 82
Cdd:COG3194     6 TLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFG-GEGRAGISIFRAQPRALPLRITMLERHPLGSQA 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698818900  83 FIPLLGNPFLVVVAPLGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDEQL 161
Cdd:COG3194    85 FIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
54-143 9.39e-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: 9.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  54 AIISIFSAEKLEMPLRIRMLERHPLGSQAFIPLLGNPFLVVVAP--LGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLT 131
Cdd:cd20298     1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPpgDDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                          90
                  ....*....|..
gi 1698818900 132 IEKRDDFLVVDR 143
Cdd:cd20298    81 LDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
1-163 3.37e-109

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 307.96  E-value: 3.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:PRK03606    1 MRTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  81 QAFIPLLGNPFLVVVAPLGDVpVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDEQ 160
Cdd:PRK03606   81 QAFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDEL 159

                  ...
gi 1698818900 161 LLL 163
Cdd:PRK03606  160 IIA 162
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
1-157 3.02e-88

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: 254.83  E-value: 3.02e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:pfam04115   1 MRTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1698818900  81 QAFIPLLGNPFLVVVAPLGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTE 157
Cdd:pfam04115  81 QAFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDE 157
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
3-161 2.98e-86

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 250.17  E-value: 2.98e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   3 TLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAqPEDNAIISIFSAEKLEMPLRIRMLERHPLGSQA 82
Cdd:COG3194     6 TLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFG-GEGRAGISIFRAQPRALPLRITMLERHPLGSQA 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1698818900  83 FIPLLGNPFLVVVAPLGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDEQL 161
Cdd:COG3194    85 FIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLDTPLEI 163
PRK13395 PRK13395
ureidoglycolate lyase;
1-165 6.19e-69

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 206.58  E-value: 6.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900   1 MRTLKIEPLTKEAFAPFGDVIETAGSDYFMINNGSTRRYHKLATVETAQPEDNAIISIFSAEKLEMPLRIRMLERHPLGS 80
Cdd:PRK13395    1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  81 QAFIPLLG-NPFLVVVAPLGDVpVPGLVRAFLTNGRQGVNYHRGVWHHPVLTIEKRDDFLVVDRSGSGNNCDEHFFTEDE 159
Cdd:PRK13395   81 QAFIPLAAvSRYAVVVAPAGEF-RPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPW 159

                  ....*.
gi 1698818900 160 QLLLDP 165
Cdd:PRK13395  160 RLEFED 165
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
54-143 9.39e-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: 9.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1698818900  54 AIISIFSAEKLEMPLRIRMLERHPLGSQAFIPLLGNPFLVVVAP--LGDVPVPGLVRAFLTNGRQGVNYHRGVWHHPVLT 131
Cdd:cd20298     1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPpgDDGKPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                          90
                  ....*....|..
gi 1698818900 132 IEKRDDFLVVDR 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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