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Conserved domains on  [gi|1330561802|ref|WP_102479032|]
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MULTISPECIES: ureidoglycolate lyase [Vibrio]

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;
6-162 1.15e-94

ureidoglycolate lyase;


:

Pssm-ID: 179606  Cd Length: 162  Bit Score: 272.14  E-value: 1.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   6 RRLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQ 85
Cdd:PRK03606    2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330561802  86 AFVPLLGQPYLIVVAPKGDNpTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFDND 162
Cdd:PRK03606   82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPED 157
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
6-162 1.15e-94

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 272.14  E-value: 1.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   6 RRLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQ 85
Cdd:PRK03606    2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330561802  86 AFVPLLGQPYLIVVAPKGDNpTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFDND 162
Cdd:PRK03606   82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPED 157
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
6-160 4.85e-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: 252.52  E-value: 4.85e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   6 RRLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQ 85
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330561802  86 AFVPLLGQPYLIVVAPKGDNPTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFD 160
Cdd:pfam04115  82 AFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFD 156
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-160 1.86e-81

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 238.61  E-value: 1.86e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   1 MSNGIRrLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQdGEAIISIFQATPLSYPLTIEMLERH 80
Cdd:COG3194     1 MSTSAT-LPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGE-GRAGISIFRAQPRALPLRITMLERH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802  81 PLGSQAFVPLLGQPYLIVVAPKGDNPTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFD 160
Cdd:COG3194    79 PLGSQAFIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLD 158
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
58-147 6.36e-44

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: 141.13  E-value: 6.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802  58 AIISIFQATPLSYPLTIEMLERHPLGSQAFVPLLGQPYLIVVAPKGDN--PTLANSRAFLSNGRQGVNYHKGVWHHPVLA 135
Cdd:cd20298     1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDgkPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                          90
                  ....*....|..
gi 1330561802 136 LTDQDQFLIVDR 147
Cdd:cd20298    81 LDAPADFLVLDR 92
 
Name Accession Description Interval E-value
PRK03606 PRK03606
ureidoglycolate lyase;
6-162 1.15e-94

ureidoglycolate lyase;


Pssm-ID: 179606  Cd Length: 162  Bit Score: 272.14  E-value: 1.15e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   6 RRLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQ 85
Cdd:PRK03606    2 RTLQIEPLTKEAFAPFGDVIETDGADFFHINNGTTERYHDLARVEVAGEGGRALISIFRAQPRALPLEIRMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330561802  86 AFVPLLGQPYLIVVAPKGDNpTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFDND 162
Cdd:PRK03606   82 AFIPLNGRPFLVVVAPDGDG-DPGTPRAFVTNGRQGVNYHRGVWHHPLLALGEVSDFLVVDRGGPGDNLEEHFFPED 157
Ureidogly_lyase pfam04115
Ureidoglycolate lyase; Ureidoglycolate lyase (EC:4.3.2.3) is one of the enzymes that acts upon ...
6-160 4.85e-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: 252.52  E-value: 4.85e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   6 RRLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQ 85
Cdd:pfam04115   2 RTLTAEPLTAEAFAPFGDVIEADGAPSVIINQGTAERYHDLARVDNNYQGGRAGISLFRAQPRALPFEVKMLERHPLGSQ 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330561802  86 AFVPLLGQPYLIVVAPKGDNPTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFD 160
Cdd:pfam04115  82 AFIPLGGSPYLVVVAPDGGGPDLGTLRAFLAAGGQGVNYGRGTWHHPLLVLGAPSDFAVVDRVGEGPNCEEVAFD 156
AllA COG3194
Ureidoglycolate hydrolase (allantoin degradation) [Nucleotide transport and metabolism];
1-160 1.86e-81

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


Pssm-ID: 442427  Cd Length: 164  Bit Score: 238.61  E-value: 1.86e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   1 MSNGIRrLSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQdGEAIISIFQATPLSYPLTIEMLERH 80
Cdd:COG3194     1 MSTSAT-LPAEPLTAEAFAPFGDVIEADGAPDFPINDGTTERYHDLALVDFGGE-GRAGISIFRAQPRALPLRITMLERH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802  81 PLGSQAFVPLLGQPYLIVVAPKGDNPTLANSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFD 160
Cdd:COG3194    79 PLGSQAFIPLSGKPFLVVVAPPGGGPDPETLRAFLTPGGQGVNYHRGTWHHPLLALDDPGDFLVVDRSGTGEDCEEHDLD 158
PRK13395 PRK13395
ureidoglycolate lyase;
8-172 5.69e-64

ureidoglycolate lyase;


Pssm-ID: 237375  Cd Length: 171  Bit Score: 194.64  E-value: 5.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802   8 LSIEPLTKQAFAEFGDVIESDNSDFFMINSGSTRRYHKLATTDVQDQDGEAIISIFQATPLSYPLTIEMLERHPLGSQAF 87
Cdd:PRK13395    4 LRAERLTREAFAPFGDVIELDGARHFPINGGTTERFHDLATIDVTGDGGRPLVSLFRAQPRALPVAITMMERHPLGSQAF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802  88 VPLLGQ-PYLIVVAPKGD-NPTlaNSRAFLSNGRQGVNYHKGVWHHPVLALTDQDQFLIVDRGGEGHNCDEVYFDnDRVA 165
Cdd:PRK13395   84 IPLAAVsRYAVVVAPAGEfRPD--EMRAFLAEGWQGVNYAKGVWHHPLLALDAVSDFVVVDRGGPQPNCDEIPLD-TPWR 160

                  ....*..
gi 1330561802 166 LHLEDMP 172
Cdd:PRK13395  161 LEFEDAT 167
cupin_UAH cd20298
ureidoglycolate amidohydrolase (UAH) and related proteins, cupin domain; This family includes ...
58-147 6.36e-44

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: 141.13  E-value: 6.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330561802  58 AIISIFQATPLSYPLTIEMLERHPLGSQAFVPLLGQPYLIVVAPKGDN--PTLANSRAFLSNGRQGVNYHKGVWHHPVLA 135
Cdd:cd20298     1 PNLSIFRAKPRPLPLRVRLLERHPFSSQAFIPLGGGRYLVVVAPPGDDgkPDLSTLRAFVADGGQGVNYHAGVWHHPLIA 80
                          90
                  ....*....|..
gi 1330561802 136 LTDQDQFLIVDR 147
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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