NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1543104142|ref|WP_126009338|]
View 

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

Protein Classification

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase( domain architecture ID 10014418)

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase catalyzes the decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) into S(+)-allantoin, the third step of the conversion of uric acid (a purine derivative) to allantoin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
7-166 7.16e-56

putative OHCU decarboxylase; Provisional


:

Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 173.22  E-value: 7.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLstlskkyaATAQKA 86
Cdd:PRK13798   12 NALPERQAVHALFECCHSTAWARRLAAARPFADHDALLAAADEALAGLSEADIDEALAGHPRIGER--------PASKAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  87 GHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESLL 166
Cdd:PRK13798   84 AREQAGVADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDPETERKVVREELAKINRLRLERLL 163
 
Name Accession Description Interval E-value
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
7-166 7.16e-56

putative OHCU decarboxylase; Provisional


Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 173.22  E-value: 7.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLstlskkyaATAQKA 86
Cdd:PRK13798   12 NALPERQAVHALFECCHSTAWARRLAAARPFADHDALLAAADEALAGLSEADIDEALAGHPRIGER--------PASKAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  87 GHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESLL 166
Cdd:PRK13798   84 AREQAGVADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDPETERKVVREELAKINRLRLERLL 163
UraD_2 TIGR03180
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
7-166 2.21e-53

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: 166.48  E-value: 2.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAqka 86
Cdd:TIGR03180   2 NSLSKDEASATLAPCCAIPAWAETLVAARPFASREALLAAADQAMANLSEDDLNEALAGHPRIGEKPAGQAAHAATS--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  87 GHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESLL 166
Cdd:TIGR03180  79 RREQAGVDGADEETRAALLEGNAAYEEKFGRIFLIRAAGRSAEEMLDALQARLQNDPEEELRIAAEQLREITRLRLSRLI 158
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
7-163 2.44e-47

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: 151.14  E-value: 2.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAQKa 86
Cdd:pfam09349   1 NALSREEFVAALGELFEHSPWVAELAAARPFASYDALIAAADEALRALSEEEQLELLRAHPRLGGKAAAAGTLSAESAR- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543104142  87 ghEQSGM--SKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLE 163
Cdd:pfam09349  80 --EQAGAglDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRLANDPETERAEALEELAKIARLRLE 156
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
1-166 1.55e-46

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: 149.54  E-value: 1.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   1 MSSLKINDLNAAQAHQALEHCCAAPNWVS-GMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKY 79
Cdd:COG3195     2 MTLDELNALSREEFVAALGGCFEHSPWVAeRAWAARPFASAEALHAAAARAVRAASEEEQLALLRAHPDLGGKAAGAGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  80 AATAQkagHEQSGMSKAN--EQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKI 157
Cdd:COG3195    82 TAEST---SEQAGAGLDDltDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAALERRLANDPETEFAEALAQIRRI 158

                  ....*....
gi 1543104142 158 TKIRLESLL 166
Cdd:COG3195   159 ARLRLEDLL 167
 
Name Accession Description Interval E-value
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
7-166 7.16e-56

putative OHCU decarboxylase; Provisional


Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 173.22  E-value: 7.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLstlskkyaATAQKA 86
Cdd:PRK13798   12 NALPERQAVHALFECCHSTAWARRLAAARPFADHDALLAAADEALAGLSEADIDEALAGHPRIGER--------PASKAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  87 GHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESLL 166
Cdd:PRK13798   84 AREQAGVADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDPETERKVVREELAKINRLRLERLL 163
UraD_2 TIGR03180
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
7-166 2.21e-53

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: 166.48  E-value: 2.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAqka 86
Cdd:TIGR03180   2 NSLSKDEASATLAPCCAIPAWAETLVAARPFASREALLAAADQAMANLSEDDLNEALAGHPRIGEKPAGQAAHAATS--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  87 GHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESLL 166
Cdd:TIGR03180  79 RREQAGVDGADEETRAALLEGNAAYEEKFGRIFLIRAAGRSAEEMLDALQARLQNDPEEELRIAAEQLREITRLRLSRLI 158
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
7-163 2.44e-47

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: 151.14  E-value: 2.44e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   7 NDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAQKa 86
Cdd:pfam09349   1 NALSREEFVAALGELFEHSPWVAELAAARPFASYDALIAAADEALRALSEEEQLELLRAHPRLGGKAAAAGTLSAESAR- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543104142  87 ghEQSGM--SKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLE 163
Cdd:pfam09349  80 --EQAGAglDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRLANDPETERAEALEELAKIARLRLE 156
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
1-166 1.55e-46

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: 149.54  E-value: 1.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   1 MSSLKINDLNAAQAHQALEHCCAAPNWVS-GMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKY 79
Cdd:COG3195     2 MTLDELNALSREEFVAALGGCFEHSPWVAeRAWAARPFASAEALHAAAARAVRAASEEEQLALLRAHPDLGGKAAGAGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  80 AATAQkagHEQSGMSKAN--EQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKI 157
Cdd:COG3195    82 TAEST---SEQAGAGLDDltDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAALERRLANDPETEFAEALAQIRRI 158

                  ....*....
gi 1543104142 158 TKIRLESLL 166
Cdd:COG3195   159 ARLRLEDLL 167
PRK13797 PRK13797
allantoicase;
6-166 1.35e-41

allantoicase;


Pssm-ID: 106738 [Multi-domain]  Cd Length: 516  Bit Score: 145.50  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   6 INDLNAAQAHQALEHCCAAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAQ- 84
Cdd:PRK13797  346 FDALTPDAAREELLACCGSEDWASAVAARRPFGTLAALLPAAEQEWWRLPESAWLEAFTAHPRIGERPTQAPAPPTSARa 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  85 ------KAGHEQSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKIT 158
Cdd:PRK13797  426 tvvsldAPRREQAAMDQAAEDVRAAFARGNAAYEERFGFIFLVRAAGRGAEEMLELLRARLAHDPEQELRIAAGQQAEIT 505

                  ....*...
gi 1543104142 159 KIRLESLL 166
Cdd:PRK13797  506 ALRLRHLI 513
UHCUDC TIGR03164
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
36-165 1.23e-15

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: 69.70  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  36 PFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLSKKYAATAQKaghEQS--GMSKANEQTLKKMIALNKEYLS 113
Cdd:TIGR03164  29 PFDSIEDLHAAMVGAVRAASPEQQLALIRAHPDLAGKLAVAGELTAESTS---EQAsaGLDQLSQEEFARFTRLNNAYRA 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1543104142 114 KFGFIFIVCASGKSAEQMLELIEQRIHNTRSTELNIAAGEQAKITKIRLESL 165
Cdd:TIGR03164 106 RFGFPFIMAVKGKTKQSILAAFEARLNNDRETEFARALREIERIARFRLRDL 157
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
3-162 4.29e-10

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 57.07  E-value: 4.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   3 SLKINDLNAAQAHQAL-------EHccaAPnWVSG-MLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLST 74
Cdd:PRK13590    2 ALTLEQLNAASAAEATalldglyEH---SP-WIAErALAQRPFRSLAQLKHALVQVVREAGRDAQLGLIRAHPELAGKAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  75 LSKkyAATAQKAgHEQS--GMSKANEQTLKKMIALNKEYLSKFGFIFIVC-----ASGKSAEQMLELIEQRIHNTRSTEL 147
Cdd:PRK13590   78 VAG--SLTAEST-HEQGkaGLTHCTPEEFARIQQLNADYNARFGFPFILAvrgprGLGLSRQEIIATFARRLDNHPDFEL 154
                         170
                  ....*....|....*
gi 1543104142 148 NIAAGEQAKITKIRL 162
Cdd:PRK13590  155 AEALRNIHRIAEIRL 169
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
4-166 2.28e-08

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


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 52.32  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142   4 LKINDLNAAQAHQAL-------EHccaAPNWVSGMLNIMPFENKDHLFSSAQSVWDSLGESDYLAAFEGHPQIGDLSTLS 76
Cdd:PRK13799    3 EQLEQLAAADLAAAAdlldgiyEH---SPWIAEAAAALGPFPSIAAIKQALAGVLDAADRAAKLDLIRAHPELAGKAAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543104142  77 KKYaaTAQKAGHE-QSGMSKANEQTLKKMIALNKEYLSKFGFIFIVCASGKSA-----EQMLELIEQRIHNTRSTELNIA 150
Cdd:PRK13799   80 GEL--TAESTGEQaKAGLNLCTPEEFAAIQKLNADYGKKFGFPFILAVKGARGaglakAEIIATFERRLHNHPDDELGEA 157
                         170
                  ....*....|....*.
gi 1543104142 151 AGEQAKITKIRLESLL 166
Cdd:PRK13799  158 LRNIGRIAEIRINDKF 173
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH