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hydroxyisourate hydrolase [Phytobacter diazotrophicus]

Protein Classification

hydroxyisourate hydrolase( domain architecture ID 10006399)

hydroxyisourate hydrolase catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) in the second step of a three-step ureide pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-107 2.16e-47

5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism];


:

Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   1 MSSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF-PVPLTPGRYRLVAQTGEWFAKQDVATLFPC 75
Cdd:COG2351     1 MGRLSTHVLDTARGRPAAGVRVELYRLDgdgwTLLAEGVTNADGRIDALgGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819469880  76 AQIDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:COG2351    81 VPVRFGIAD-PEEHYHVPLLLSPWGYSTYRGS 111
 
Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-107 2.16e-47

5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism];


Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   1 MSSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF-PVPLTPGRYRLVAQTGEWFAKQDVATLFPC 75
Cdd:COG2351     1 MGRLSTHVLDTARGRPAAGVRVELYRLDgdgwTLLAEGVTNADGRIDALgGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819469880  76 AQIDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:COG2351    81 VPVRFGIAD-PEEHYHVPLLLSPWGYSTYRGS 111
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 4-106 3.95e-42

HIUase/Transthyretin family; This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyze the conversion of 5-hydroxyisourate (HIU) to OHCU. HIU hydrolysis is the original function of the family and is conserved from bacteria to mammals; transthyretins arose by gene duplications in the vertebrate lineage. HIUases are distinguished in the alignment from the conserved C-terminal YRGS sequence.


Pssm-ID: 459857  Cd Length: 108  Bit Score: 133.72  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   4 LSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAFPVP---LTPGRYRLVAQTGEWFAKQDVATLFPCA 76
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDgdgwTLLAEGTTNADGRCDDLLLEgeaLEPGTYRLVFDTGAYFAARGVESFYPEV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1819469880  77 QIDFMVAqgAEEHFHLPFLIAPGGWSTYRG 106
Cdd:pfam00576  81 EVRFGIT--DAEHYHVPLLLSPFGYSTYRG 108
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 2-107 2.35e-41

HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway in which 5-hydroxyisourate (HIU), a product of the uricase (urate oxidase) reaction, is hydrolyzed to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). HIUase has high sequence similarity with transthyretins and is a member of the transthyretin-like protein (TLP) family. HIUase is distinguished from transthyretins by a conserved signature motif at its C-terminus that forms part of the active site. In HIUase, this motif is YRGS, while transthyretins have a conserved TAVV sequence in the same location. Most HIUases are cytosolic but in plants and slime molds, they are peroxisomal based on the presence of N-terminal periplasmic localization sequences. HIUase forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits.


Pssm-ID: 100114  Cd Length: 112  Bit Score: 131.89  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   2 SSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAFPVP---LTPGRYRLVAQTGEWFAKQDVATLFP 74
Cdd:cd05822     1 GPLSTHVLDTATGKPAAGVAVTLYRLDgngwTLLATGVTNADGRCDDLLPPgaqLAAGTYKLTFDTGAYFAARGQESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819469880  75 CAQIDFMVAqGAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:cd05822    81 EVEVRFTIT-DPTEHYHVPLLLSPFGYSTYRGS 112
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 2-107 1.27e-38

hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274364  Cd Length: 112  Bit Score: 124.97  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   2 SSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF---PVPLTPGRYRLVAQTGEWFAKQDVATLFP 74
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLYRLDgggwTPLATGVTNADGRCDGPlpeGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819469880  75 CAQIDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:TIGR02962  81 EVEVVFTIAD-PGQHYHVPLLLSPYGYSTYRGS 112
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 4-107 1.73e-27

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 97.75  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   4 LSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF--PVPLTPGRYRLVAQTGEWFAKQDVATLFPCAQ 77
Cdd:PRK15036   29 LSVHILNQQTGKPAADVTVTLEKKAdngwLQLNTAKTDKDGRIKALwpEQTATTGDYRVVFKTGDYFKKQNLESFFPEIP 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 1819469880  78 IDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:PRK15036  109 VEFHINK-VNEHYHVPLLLSQYGYSTYRGS 137
 
Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-107 2.16e-47

5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism];


Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   1 MSSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF-PVPLTPGRYRLVAQTGEWFAKQDVATLFPC 75
Cdd:COG2351     1 MGRLSTHVLDTARGRPAAGVRVELYRLDgdgwTLLAEGVTNADGRIDALgGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1819469880  76 AQIDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:COG2351    81 VPVRFGIAD-PEEHYHVPLLLSPWGYSTYRGS 111
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 4-106 3.95e-42

HIUase/Transthyretin family; This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyze the conversion of 5-hydroxyisourate (HIU) to OHCU. HIU hydrolysis is the original function of the family and is conserved from bacteria to mammals; transthyretins arose by gene duplications in the vertebrate lineage. HIUases are distinguished in the alignment from the conserved C-terminal YRGS sequence.


Pssm-ID: 459857  Cd Length: 108  Bit Score: 133.72  E-value: 3.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   4 LSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAFPVP---LTPGRYRLVAQTGEWFAKQDVATLFPCA 76
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDgdgwTLLAEGTTNADGRCDDLLLEgeaLEPGTYRLVFDTGAYFAARGVESFYPEV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1819469880  77 QIDFMVAqgAEEHFHLPFLIAPGGWSTYRG 106
Cdd:pfam00576  81 EVRFGIT--DAEHYHVPLLLSPFGYSTYRG 108
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 2-107 2.35e-41

HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway in which 5-hydroxyisourate (HIU), a product of the uricase (urate oxidase) reaction, is hydrolyzed to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). HIUase has high sequence similarity with transthyretins and is a member of the transthyretin-like protein (TLP) family. HIUase is distinguished from transthyretins by a conserved signature motif at its C-terminus that forms part of the active site. In HIUase, this motif is YRGS, while transthyretins have a conserved TAVV sequence in the same location. Most HIUases are cytosolic but in plants and slime molds, they are peroxisomal based on the presence of N-terminal periplasmic localization sequences. HIUase forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits.


Pssm-ID: 100114  Cd Length: 112  Bit Score: 131.89  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   2 SSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAFPVP---LTPGRYRLVAQTGEWFAKQDVATLFP 74
Cdd:cd05822     1 GPLSTHVLDTATGKPAAGVAVTLYRLDgngwTLLATGVTNADGRCDDLLPPgaqLAAGTYKLTFDTGAYFAARGQESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819469880  75 CAQIDFMVAqGAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:cd05822    81 EVEVRFTIT-DPTEHYHVPLLLSPFGYSTYRGS 112
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 2-107 1.27e-38

hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274364  Cd Length: 112  Bit Score: 124.97  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   2 SSLSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF---PVPLTPGRYRLVAQTGEWFAKQDVATLFP 74
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLYRLDgggwTPLATGVTNADGRCDGPlpeGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1819469880  75 CAQIDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:TIGR02962  81 EVEVVFTIAD-PGQHYHVPLLLSPYGYSTYRGS 112
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 4-107 1.73e-27

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 97.75  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   4 LSTHILDISTGKPAPGVTVFLARDE----YVLAQGITDANGRIGAF--PVPLTPGRYRLVAQTGEWFAKQDVATLFPCAQ 77
Cdd:PRK15036   29 LSVHILNQQTGKPAADVTVTLEKKAdngwLQLNTAKTDKDGRIKALwpEQTATTGDYRVVFKTGDYFKKQNLESFFPEIP 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 1819469880  78 IDFMVAQgAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:PRK15036  109 VEFHINK-VNEHYHVPLLLSQYGYSTYRGS 137
Transthyretin_like cd05469
Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family ...
 2-107 4.05e-18

Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family which includes transthyretin (TTR) and a transthyretin-related protein called 5-hydroxyisourate hydrolase (HIUase). TTR and HIUase are homotetrameric proteins with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits. TTR transports thyroid hormones and retinol in the blood serum of vertebrates while HIUase catalyzes the second step in a three-step ureide pathway. TTRs are highly conserved and found only in vertebrates while the HIUases are found in a wide range of bacterial, plant, fungal, slime mold and vertebrate organisms.


Pssm-ID: 100112  Cd Length: 113  Bit Score: 72.95  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   2 SSLSTHILDISTGKPAPGVTVFLAR-----DEYVLAQGITDANGRIgafPVPLT-----PGRYRLVAQTGEWFAKQDVAT 71
Cdd:cd05469     1 CPLMVKVLDAVRGSPAANVAIKVFRktadgSWEIFATGKTNEDGEL---HGLITeeef*AGVYRVEFDTKSYWKALGITP 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1819469880  72 LFPCAQIDFMVAQGAEEHFHLPFLIAPGGWSTYRGS 107
Cdd:cd05469    78 FHEYAEVVFTANDSGHRHYTIALLLSPFSYSTTAVV 113
bMG3 pfam11974
Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial ...
 3-65 1.26e-06

Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial alpha2-macroglobulins.


Pssm-ID: 432232 [Multi-domain]  Cd Length: 102  Bit Score: 42.97  E-value: 1.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819469880   3 SLSTHILDISTGKPAPGVTV-FLARDEYVLAQGITDANGRIgAFPVPLTPGR----YRLVAQTGEWFA 65
Cdd:pfam11974  14 GLLVWVTSLDSGKPVAGVEVrLLDCNGQVLATGTTDAQGHA-RFEGPLTRDGgaapALVSARKDGDFA 80
YfaS COG2373
Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function ...
 3-62 2.75e-05

Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only];


Pssm-ID: 441940 [Multi-domain]  Cd Length: 1605  Bit Score: 41.22  E-value: 2.75e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819469880    3 SLSTHILDISTGKPAPGVTV-FLARDEYVLAQGITDANGRIgAFPVPLTPGRYR----LVAQTGE 62
Cdd:COG2373    277 GLLVFVTSLSTGKPVAGAEVeLYDRNGQVLATATTDADGLA-RFPAGDRGEGGRapalLVARKGG 340
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 4-103 1.21e-03

Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and retinol in vertebrates. TTR distributes the two thyroid hormones T3 (3,5,3'-triiodo-L-thyronine) and T4 (Thyroxin, or 3,5,3',5'-tetraiodo-L-thyronine), as well as retinol (vitamin A) through the formation of a macromolecular complex that includes each of these as well as retinol-binding protein. Misfolded forms of TTR are implicated in the amyloid diseases familial amyloidotic polyneuropathy and senile systemic amyloidosis. TTR forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits, which differ in their ligand binding affinity. A negative cooperativity has been observed for the binding of T4 and other TTR ligands. A fraction of plasma TTR is carried in high density lipoproteins by binding to apolipoprotein AI (apoA-I). TTR is able to proteolytically process apoA-I by cleaving its C-terminus; therefore TTR has protease activity in addition to its function in protein transport.


Pssm-ID: 100113  Cd Length: 121  Bit Score: 35.60  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819469880   4 LSTHILDISTGKPAPGVTVFLARDE-----YVLAQGITDANGRIGAFPV--PLTPGRYRLVAQTGEWFAKQDVATLFPCA 76
Cdd:cd05821     9 LMVKVLDAVRGSPAANVAVKVFKKTadgswEPFASGKTTETGEIHGLTTdeQFTEGVYKVEFDTKAYWKKLGISPFHEYA 88

                          90       100
                  ....*....|....*....|....*..
gi 1819469880  77 QIDFMVAQGAEEHFHLPFLIAPGGWST 103
Cdd:cd05821    89 EVVFTANDSGHRHYTIAALLSPYSYST 115
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
3-59 1.47e-03

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 34.56  E-value: 1.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1819469880   3 SLSTHILDiSTGKPAPGVTVFLARDEYVLAQG-ITDANGRigaFPVP-LTPGRYRLVAQ 59
Cdd:pfam13620   1 TISGTVTD-PSGAPVPGATVTVTNTDTGTVRTtTTDADGR---YRFPgLPPGTYTVTVS 55
COG5266 COG5266
Uncharacterized protein, contains GH25 family domain [General function prediction only];
14-58 2.18e-03

Uncharacterized protein, contains GH25 family domain [General function prediction only];


Pssm-ID: 444079 [Multi-domain]  Cd Length: 261  Bit Score: 35.83  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1819469880  14 GKPAPGVTV------FLARDEYVLAQGITDANGRIgAFPVPlTPGRYRLVA 58
Cdd:COG5266   187 GKPLAGAEVeveyggDRYPDDAGAQVLKTDADGKF-TFTLP-EAGLWLLAA 235
 
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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