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MULTISPECIES: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase [Pseudomonas]

Protein Classification

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase( domain architecture ID 10007037)

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13798 super family cl01251
putative OHCU decarboxylase; Provisional
12-171 2.91e-78

putative OHCU decarboxylase; Provisional


The actual alignment was detected with superfamily member TIGR03164:

Pssm-ID: 470134 [Multi-domain]  Cd Length: 157  Bit Score: 229.56  E-value: 2.91e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   12 LSREAFIEAFADIYEHSPWVAEKAYDLGIDDSlndIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASST 91
Cdd:TIGR03164   1 MDKADFVAALGDIFEHSPWIAERAWAQRPFDS---IEDLHAAMVGAVRAASPEQQLALIRAHPDLAGKLAVAGELTAEST 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   92 SEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:TIGR03164  78 SEQASAGLDQLSQEEFARFTRLNNAYRARFGFPFIMAVKGKTKQSILAAFEARLNNDRETEFARALREIERIARFRLRDL 157
 
Name Accession Description Interval E-value
UHCUDC TIGR03164
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
12-171 2.91e-78

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model.


Pssm-ID: 132208 [Multi-domain]  Cd Length: 157  Bit Score: 229.56  E-value: 2.91e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   12 LSREAFIEAFADIYEHSPWVAEKAYDLGIDDSlndIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASST 91
Cdd:TIGR03164   1 MDKADFVAALGDIFEHSPWIAERAWAQRPFDS---IEDLHAAMVGAVRAASPEQQLALIRAHPDLAGKLAVAGELTAEST 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   92 SEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:TIGR03164  78 SEQASAGLDQLSQEEFARFTRLNNAYRARFGFPFIMAVKGKTKQSILAAFEARLNNDRETEFARALREIERIARFRLRDL 157
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
8-171 5.15e-74

2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442428 [Multi-domain]  Cd Length: 169  Bit Score: 219.26  E-value: 5.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   8 TPASLSREAFIEAFADIYEHSPWVAEKAYDLGIDDSLndiEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELT 87
Cdd:COG3195    6 ELNALSREEFVAALGGCFEHSPWVAERAWAARPFASA---EALHAAAARAVRAASEEEQLALLRAHPDLGGKAAGAGRLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  88 ASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFR 167
Cdd:COG3195   83 AESTSEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAALERRLANDPETEFAEALAQIRRIARLR 162

                 ....
gi 496672267 168 LQQL 171
Cdd:COG3195  163 LEDL 166
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
11-169 3.54e-62

OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).


Pssm-ID: 462765 [Multi-domain]  Cd Length: 156  Bit Score: 188.89  E-value: 3.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   11 SLSREAFIEAFADIYEHSPWVAEKAYDLgiddSLNDIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASS 90
Cdd:pfam09349   2 ALSREEFVAALGELFEHSPWVAELAAAR----PFASYDALIAAADEALRALSEEEQLELLRAHPRLGGKAAAAGTLSAES 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496672267   91 TSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQ 169
Cdd:pfam09349  78 AREQAGAGLDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRLANDPETERAEALEELAKIARLRLE 156
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
6-168 2.88e-49

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 167.24  E-value: 2.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   6 TLTPASL---SREAFIEAFADIYEHSPWVAEKAYDLGIDDSLndiEGLHQRMADILLSASREAQLALINAHPDLAGKAAI 82
Cdd:PRK13590   2 ALTLEQLnaaSAAEATALLDGLYEHSPWIAERALAQRPFRSL---AQLKHALVQVVREAGRDAQLGLIRAHPELAGKAMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  83 RGELTASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGS-----NRHQILAAFEERIQHSADEEFATAL 157
Cdd:PRK13590  79 AGSLTAESTHEQGKAGLTHCTPEEFARIQQLNADYNARFGFPFILAVRGPrglglSRQEIIATFARRLDNHPDFELAEAL 158
                        170
                 ....*....|.
gi 496672267 158 AEINKIALFRL 168
Cdd:PRK13590 159 RNIHRIAEIRL 169
 
Name Accession Description Interval E-value
UHCUDC TIGR03164
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
12-171 2.91e-78

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model.


Pssm-ID: 132208 [Multi-domain]  Cd Length: 157  Bit Score: 229.56  E-value: 2.91e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   12 LSREAFIEAFADIYEHSPWVAEKAYDLGIDDSlndIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASST 91
Cdd:TIGR03164   1 MDKADFVAALGDIFEHSPWIAERAWAQRPFDS---IEDLHAAMVGAVRAASPEQQLALIRAHPDLAGKLAVAGELTAEST 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   92 SEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:TIGR03164  78 SEQASAGLDQLSQEEFARFTRLNNAYRARFGFPFIMAVKGKTKQSILAAFEARLNNDRETEFARALREIERIARFRLRDL 157
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
8-171 5.15e-74

2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442428 [Multi-domain]  Cd Length: 169  Bit Score: 219.26  E-value: 5.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   8 TPASLSREAFIEAFADIYEHSPWVAEKAYDLGIDDSLndiEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELT 87
Cdd:COG3195    6 ELNALSREEFVAALGGCFEHSPWVAERAWAARPFASA---EALHAAAARAVRAASEEEQLALLRAHPDLGGKAAGAGRLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  88 ASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFR 167
Cdd:COG3195   83 AESTSEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAALERRLANDPETEFAEALAQIRRIARLR 162

                 ....
gi 496672267 168 LQQL 171
Cdd:COG3195  163 LEDL 166
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
11-169 3.54e-62

OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).


Pssm-ID: 462765 [Multi-domain]  Cd Length: 156  Bit Score: 188.89  E-value: 3.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   11 SLSREAFIEAFADIYEHSPWVAEKAYDLgiddSLNDIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASS 90
Cdd:pfam09349   2 ALSREEFVAALGELFEHSPWVAELAAAR----PFASYDALIAAADEALRALSEEEQLELLRAHPRLGGKAAAAGTLSAES 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496672267   91 TSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQ 169
Cdd:pfam09349  78 AREQAGAGLDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRLANDPETERAEALEELAKIARLRLE 156
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
6-168 2.88e-49

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 167.24  E-value: 2.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   6 TLTPASL---SREAFIEAFADIYEHSPWVAEKAYDLGIDDSLndiEGLHQRMADILLSASREAQLALINAHPDLAGKAAI 82
Cdd:PRK13590   2 ALTLEQLnaaSAAEATALLDGLYEHSPWIAERALAQRPFRSL---AQLKHALVQVVREAGRDAQLGLIRAHPELAGKAMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  83 RGELTASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGS-----NRHQILAAFEERIQHSADEEFATAL 157
Cdd:PRK13590  79 AGSLTAESTHEQGKAGLTHCTPEEFARIQQLNADYNARFGFPFILAVRGPrglglSRQEIIATFARRLDNHPDFELAEAL 158
                        170
                 ....*....|.
gi 496672267 158 AEINKIALFRL 168
Cdd:PRK13590 159 RNIHRIAEIRL 169
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
16-171 8.19e-42

unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 147.08  E-value: 8.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  16 AFIEAFADIYEHSPWVAEKAYDLGiddSLNDIEGLHQRMADILLSASREAQLALINAHPDLAGKAAIRGELTASSTSEQA 95
Cdd:PRK13799  15 AAADLLDGIYEHSPWIAEAAAALG---PFPSIAAIKQALAGVLDAADRAAKLDLIRAHPELAGKAAEAGELTAESTGEQA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  96 GAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSN-----RHQILAAFEERIQHSADEEFATALAEINKIALFRLQQ 170
Cdd:PRK13799  92 KAGLNLCTPEEFAAIQKLNADYGKKFGFPFILAVKGARgaglaKAEIIATFERRLHNHPDDELGEALRNIGRIAEIRIND 171

                 .
gi 496672267 171 L 171
Cdd:PRK13799 172 K 172
UraD_2 TIGR03180
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
55-171 5.85e-13

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model. This model is a separate (but related) clade from that represented by TIGR3164. This model places a second homolog in streptomyces species which (are not in the vicinity of other urate catabolism associated genes) below the trusted cutoff.


Pssm-ID: 188295 [Multi-domain]  Cd Length: 158  Bit Score: 62.86  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267   55 ADILLSASREAQ--------LALINAHPDLAGKAAIRGELTASSTSEQAGagIHECSAEEFARFTELNDTYKARFGFPFI 126
Cdd:TIGR03180  35 REALLAAADQAManlseddlNEALAGHPRIGEKPAGQAAHAATSRREQAG--VDGADEETRAALLEGNAAYEEKFGRIFL 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 496672267  127 KAVKGSNRHQILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:TIGR03180 113 IRAAGRSAEEMLDALQARLQNDPEEELRIAAEQLREITRLRLSRL 157
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
55-171 2.93e-11

putative OHCU decarboxylase; Provisional


Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 58.43  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  55 ADILLSASREAQLALINAHPD--LAGKAAIrGELTASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGS 132
Cdd:PRK13798  45 HDALLAAADEALAGLSEADIDeaLAGHPRI-GERPASKASAREQAGVADADEAVMAALAAGNRAYEEKFGFVFLICATGR 123
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496672267 133 NRHQILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:PRK13798 124 SADEMLAALQQRLHNDPETERKVVREELAKINRLRLERL 162
PRK13797 PRK13797
allantoicase;
64-171 4.53e-09

allantoicase;


Pssm-ID: 106738 [Multi-domain]  Cd Length: 516  Bit Score: 54.21  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496672267  64 EAQLALINAHPDL--------AGKAAIRGELTASSTSEQAGAGIHECSAEEFARFTELNDTYKARFGFPFIKAVKGSNRH 135
Cdd:PRK13797 397 SAWLEAFTAHPRIgerptqapAPPTSARATVVSLDAPRREQAAMDQAAEDVRAAFARGNAAYEERFGFIFLVRAAGRGAE 476
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496672267 136 QILAAFEERIQHSADEEFATALAEINKIALFRLQQL 171
Cdd:PRK13797 477 EMLELLRARLAHDPEQELRIAAGQQAEITALRLRHL 512
 
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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