Conserved Protein Domain Family
TLP_HIUase

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cd05822: TLP_HIUase 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 100114
View PSSM: cd05822
Aligned: 68 rows
Threshold Bit Score: 127.657
Threshold Setting Gi: 70733029
Created: 28-Jan-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitehomotetramer
Conserved site includes 7 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:2H0F_A; Bacillus subtilis HIUase binds 8-azaxanthine (AZX). Contacts determined at 3.5 Angstroms.
    View structure with Cn3D
  • Comment:The homotetrameric thyretin structure contains two independent binding sites within the central core of the tetramer, each formed by a pair of monomers.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1             # #                                   #                                    
2H0F_A         9 GKLTTHILDLTCGKPAANVKIGLKRLge---siXKEVYTNNDGRVDVPLlageeLXSGEYVXEFHAGDYFasknxnaadq 85
gi 158423592   5 GGISIHGVDIAQGVAARGLQVKVYALdpe-rrlITEGVLGANGVFDDPIitgagITAGTYEVEFALGAWLkangygarea 83
gi 27378394   23 GGISIHAVDVASGRPAQGLRVEIWRIdpd-ssrIADGRLGANGVLDHPIvqgagVTAGEYEVLFHLGEFFads------d 95
gi 70733029    3 GGLSIHVVDVASGKVAEGMAVRVRRLgg---elLCAGRIAGNGLLSELAermasFGQGVYEVELEVAAFYreqgqalppv 79
gi 163733741  11 GGISIHAVDVSRGIPAYGLSVRLMRLdpd-pveIAGGACAANGHFIHPVtegagVIRGMYEVTLGVGNYYrqsgtevpdp 89
gi 149126193   4 GGISVHAVDVATGRPAAGLRVTVEALdpagrrlVAEGRIGPDGHLPHPIsggagVTAGIYEVTFDVGDYLapeg----gg 79
gi 152970218   2 STLSTHILDISTGTPAEGVTVSLSREge----tLANLVTNAQGRIATFSaa--pLPAGRYCLTAETGAWFarag----re 71
gi 72117150    2 AGISTHVLDVSLGKPVSGMQIELFDMgtqppklIARARTNSDGRTDTPMlpatqARTGDFELRFWVADYFktp------d 75
gi 149121874 174 GKLSTHVLDTHGGRPAAGVALRFYALgragrtlLDTRTTNADGRTDTPLlsgapLRVGRYEIEFDIGPYFrervarsvdt 253
gi 148260156   2 TDLTTHVLDTAHGIPAAGVRIRLFAAgaa-ggpLAEAETDANGRAKIVPangvaFDSGSYDLVFSVGAYFgakgaaepap 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
Feature 1                            # # #        #   
2H0F_A        86 pFLTIVTVRFQLadp-daHYHIPLLLSPFGYQVYRGS 121
gi 158423592  84 aFLDIVPFRFVVtrv-eeHYHLPFKFTPWGIQLFRGV 119
gi 27378394   96 gFLTVTPFRFRIknv-deHFHLPLKFTRWGYSLFRGA 131
gi 70733029   80 pFLEVLVYRFGLddp-rqHYHLPFKLTAWGVSCFRGG 115
gi 163733741  90 aFVEDAVFRFGVerv-seHFHLPFKFTPWGFSLFRGG 125
gi 149126193  80 rFLDRVPFRFTIedv-aaHVHLPLKFTRFGYALFRGA 115
gi 152970218  72 sVFTRAQIDFVIgeaaedHFHLPFLIAPGGWSTYRGS 108
gi 72117150   76 vFADIVPVRFTIada-aqHYHVPLLCSPWSFGTYRGS 111
gi 149121874 254 lFLETVPIRFGIdep-egHYHVAMIATPWSYTVYRGS 289
gi 148260156  81 rFLDDVVIRFGLrag-aaHLHVPLLISPFGYTTYRGQ 116

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