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Conserved domains on  [gi|490670268|ref|WP_004535257|]
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ureidoglycolate lyase [Burkholderia pseudomallei]

Protein Classification

ureidoglycolate lyase( domain architecture ID 10014221)

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
PRK13395 PRK13395
ureidoglycolate lyase;
4-174 8.87e-107

ureidoglycolate lyase;


:

Pssm-ID: 237375  Cd Length: 171  Bit Score: 302.50  E-value: 8.87e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   4 LHTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGS 83
Cdd:PRK13395   1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  84 QAFVPLAAVARYVLVVAPAGEFDPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWR 163
Cdd:PRK13395  81 QAFIPLAAVSRYAVVVAPAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPWR 160
                        170
                 ....*....|.
gi 490670268 164 LVTDDAHASAA 174
Cdd:PRK13395 161 LEFEDATASAE 171
 
Name Accession Description Interval E-value
PRK13395 PRK13395
ureidoglycolate lyase;
4-174 8.87e-107

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 302.50  E-value: 8.87e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   4 LHTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGS 83
Cdd:PRK13395   1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  84 QAFVPLAAVARYVLVVAPAGEFDPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWR 163
Cdd:PRK13395  81 QAFIPLAAVSRYAVVVAPAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPWR 160
                        170
                 ....*....|.
gi 490670268 164 LVTDDAHASAA 174
Cdd:PRK13395 161 LEFEDATASAE 171
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
5-164 5.06e-87

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: 252.14  E-value: 5.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268    5 HTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGSQ 84
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   85 AFVPLAAVArYVLVVAPAGEF-DPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWR 163
Cdd:pfam04115  82 AFIPLGGSP-YLVVVAPDGGGpDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDEPLT 160

                  .
gi 490670268  164 L 164
Cdd:pfam04115 161 V 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-164 2.17e-80

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 235.53  E-value: 2.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   1 MQTLHTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEaGGRPLVSLFRAQPRAWPIEIDMMERHP 80
Cdd:COG3194    1 MSTSATLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGG-EGRAGISIFRAQPRALPLRITMLERHP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  81 LGSQAFVPLAAVaRYVLVVAPAGEF-DPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALD 159
Cdd:COG3194   80 LGSQAFIPLSGK-PFLVVVAPPGGGpDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLD 158

                 ....*
gi 490670268 160 ARWRL 164
Cdd:COG3194  159 TPLEI 163
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
57-146 1.87e-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: 1.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  57 PLVSLFRAQPRAWPIEIDMMERHPLGSQAFVPLAAvARYVLVVAPAGEF---DPTRMRAFLAQGWQGVNYAKGVWHHPLL 133
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGG-GRYLVVVAPPGDDgkpDLSTLRAFVADGGQGVNYHAGVWHHPLI 79
                         90
                 ....*....|...
gi 490670268 134 ALDALSDFVVIDR 146
Cdd:cd20298   80 ALDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK13395 PRK13395
ureidoglycolate lyase;
4-174 8.87e-107

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 302.50  E-value: 8.87e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   4 LHTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGS 83
Cdd:PRK13395   1 MKTLRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  84 QAFVPLAAVARYVLVVAPAGEFDPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWR 163
Cdd:PRK13395  81 QAFIPLAAVSRYAVVVAPAGEFRPDEMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLDTPWR 160
                        170
                 ....*....|.
gi 490670268 164 LVTDDAHASAA 174
Cdd:PRK13395 161 LEFEDATASAE 171
PRK03606 PRK03606
ureidoglycolate lyase;
5-166 4.59e-89

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 257.12  E-value: 4.59e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   5 HTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGSQ 84
Cdd:PRK03606   2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  85 AFVPLAAvARYVLVVAPAGEFDPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWRL 164
Cdd:PRK03606  82 AFIPLNG-RPFLVVVAPDGDGDPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPEDELI 160

                 ..
gi 490670268 165 VT 166
Cdd:PRK03606 161 IA 162
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
5-164 5.06e-87

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: 252.14  E-value: 5.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268    5 HTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEAGGRPLVSLFRAQPRAWPIEIDMMERHPLGSQ 84
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   85 AFVPLAAVArYVLVVAPAGEF-DPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALDARWR 163
Cdd:pfam04115  82 AFIPLGGSP-YLVVVAPDGGGpDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFDEPLT 160

                  .
gi 490670268  164 L 164
Cdd:pfam04115 161 V 161
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-164 2.17e-80

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 235.53  E-value: 2.17e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268   1 MQTLHTLRLERLTREAFAPFGDVIELAGARRILINGGTTERFHDLASIDVTEaGGRPLVSLFRAQPRAWPIEIDMMERHP 80
Cdd:COG3194    1 MSTSATLPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGG-EGRAGISIFRAQPRALPLRITMLERHP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  81 LGSQAFVPLAAVaRYVLVVAPAGEF-DPTRMRAFLAQGWQGVNYAKGVWHHPLLALDALSDFVVIDRGGAQPNCDELALD 159
Cdd:COG3194   80 LGSQAFIPLSGK-PFLVVVAPPGGGpDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLD 158

                 ....*
gi 490670268 160 ARWRL 164
Cdd:COG3194  159 TPLEI 163
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
57-146 1.87e-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: 1.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490670268  57 PLVSLFRAQPRAWPIEIDMMERHPLGSQAFVPLAAvARYVLVVAPAGEF---DPTRMRAFLAQGWQGVNYAKGVWHHPLL 133
Cdd:cd20298    1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGG-GRYLVVVAPPGDDgkpDLSTLRAFVADGGQGVNYHAGVWHHPLI 79
                         90
                 ....*....|...
gi 490670268 134 ALDALSDFVVIDR 146
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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