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Conserved domains on  [gi|447214735|ref|WP_001291991|]
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MULTISPECIES: xanthine phosphoribosyltransferase [Enterobacteriaceae]

Protein Classification

xanthine phosphoribosyltransferase( domain architecture ID 10793156)

xanthine phosphoribosyltransferase converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis

EC:  2.4.2.22
Gene Ontology:  GO:0016763|GO:0046110|GO:0043101|GO:0000310
PubMed:  9100006|11933250

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 1-152 2.53e-113

xanthine-guanine phosphoribosyltransferase; Validated


:

Pssm-ID: 236395  Cd Length: 156  Bit Score: 317.19  E-value: 2.53e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735   1 MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGD 80
Cdd:PRK09177   4 MSKKFPVSWDQLHRDARALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRLVDTVCISSYDHDNQGELKVLKRAEGD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447214735  81 GEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQNTWIEQPWDMGVVFVPPISGR 152
Cdd:PRK09177  84 GEGFLVVDDLVDTGGTARAVREMYPKAHFATVYAKPAGRPLVDTYVTDVPQDTWIEFPWDMGLTFVPPLADG 155
 
Name Accession Description Interval E-value
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 1-152 2.53e-113

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 317.19  E-value: 2.53e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735   1 MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGD 80
Cdd:PRK09177   4 MSKKFPVSWDQLHRDARALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRLVDTVCISSYDHDNQGELKVLKRAEGD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447214735  81 GEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQNTWIEQPWDMGVVFVPPISGR 152
Cdd:PRK09177  84 GEGFLVVDDLVDTGGTARAVREMYPKAHFATVYAKPAGRPLVDTYVTDVPQDTWIEFPWDMGLTFVPPLADG 155
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 1-141 1.31e-35

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 120.72  E-value: 1.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735   1 MSEKYIVTWDMLQIHARKLASRLMPSE-QWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQR-ELKVLKR-- 76
Cdd:COG2236    3 KFKKEYLSWDEIHELSRRLAEQILESGfRPDVIVAIARGGLVPARILADALGVPDLASIRVSSYTGTAKRlEEPVVKGpl 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447214735  77 -AEGDGEGFIVIDDLVDTGGTAVAIREMY-----PKAHFVTIFAKPAGRPLVDDYVVDIPqnTWIEQPWDM 141
Cdd:COG2236   83 dEDLAGKRVLIVDDVADTGRTLEAVRDLLkeagpAEVRTAVLYYKPSSKFKPDYYAEETD--AWIVFPWEL 151
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 6-145 1.11e-16

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 72.01  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735    6 IVTWDMLQIHARKLASRLMPSEQWKG--IIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEG 83
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPdvVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKT 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447214735   84 FIVIDDLVDTGGTAVA----IREMYPK-AHFVTIFAKPAGRPLVDDYVVDIPqnTWIEQPWDMGVVF 145
Cdd:pfam00156  85 VLIVDDILDTGGTLLKvlelLKNVGPKeVKIAVLIDKPAGTEPKDKYDKRVD--DWIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 32-129 1.49e-12

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 60.49  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735  32 IIAVSRGGLVPGALLARELGIRhVDTVCISSYDHDNQRELKVLKRAEGD----GEGFIVIDDLVDTGGTAVAIREMYPKA 107
Cdd:cd06223   19 VVGILRGGLPLAAALARALGLP-LAFIRKERKGPGRTPSEPYGLELPLGgdvkGKRVLLVDDVIATGGTLLAAIELLKEA 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447214735 108 -----HFVTIFAKPAGR------PLVDDYVVDI 129
Cdd:cd06223   98 gakvvGVAVLLDKPEGGarelasPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 1-152 2.53e-113

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 317.19  E-value: 2.53e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735   1 MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGD 80
Cdd:PRK09177   4 MSKKFPVSWDQLHRDARALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRLVDTVCISSYDHDNQGELKVLKRAEGD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447214735  81 GEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVVDIPQNTWIEQPWDMGVVFVPPISGR 152
Cdd:PRK09177  84 GEGFLVVDDLVDTGGTARAVREMYPKAHFATVYAKPAGRPLVDTYVTDVPQDTWIEFPWDMGLTFVPPLADG 155
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 1-141 1.31e-35

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 120.72  E-value: 1.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735   1 MSEKYIVTWDMLQIHARKLASRLMPSE-QWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQR-ELKVLKR-- 76
Cdd:COG2236    3 KFKKEYLSWDEIHELSRRLAEQILESGfRPDVIVAIARGGLVPARILADALGVPDLASIRVSSYTGTAKRlEEPVVKGpl 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447214735  77 -AEGDGEGFIVIDDLVDTGGTAVAIREMY-----PKAHFVTIFAKPAGRPLVDDYVVDIPqnTWIEQPWDM 141
Cdd:COG2236   83 dEDLAGKRVLIVDDVADTGRTLEAVRDLLkeagpAEVRTAVLYYKPSSKFKPDYYAEETD--AWIVFPWEL 151
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 6-145 1.11e-16

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 72.01  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735    6 IVTWDMLQIHARKLASRLMPSEQWKG--IIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEG 83
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPdvVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKT 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447214735   84 FIVIDDLVDTGGTAVA----IREMYPK-AHFVTIFAKPAGRPLVDDYVVDIPqnTWIEQPWDMGVVF 145
Cdd:pfam00156  85 VLIVDDILDTGGTLLKvlelLKNVGPKeVKIAVLIDKPAGTEPKDKYDKRVD--DWIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 32-129 1.49e-12

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 60.49  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735  32 IIAVSRGGLVPGALLARELGIRhVDTVCISSYDHDNQRELKVLKRAEGD----GEGFIVIDDLVDTGGTAVAIREMYPKA 107
Cdd:cd06223   19 VVGILRGGLPLAAALARALGLP-LAFIRKERKGPGRTPSEPYGLELPLGgdvkGKRVLLVDDVIATGGTLLAAIELLKEA 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447214735 108 -----HFVTIFAKPAGR------PLVDDYVVDI 129
Cdd:cd06223   98 gakvvGVAVLLDKPEGGarelasPGDPVYSLFT 130
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 13-130 2.34e-10

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 55.80  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735  13 QIHAR--KLASRLmpSEQWKG----IIAVSRGGLVPGALLARELGIRH-VDTVCISSYDHDNQ--RELKVLKRAEGDGEG 83
Cdd:COG0634   14 EIQARvkELAAQI--TADYAGkeplVVGVLKGAFVFMADLLRALDFPLeIDFMHVSSYGGGTEssGEVRILKDLDEDIEG 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447214735  84 --FIVIDDLVDTGGTAVAIREMY----PKA-HFVTIFAKPAGR--PLVDDYV-VDIP 130
Cdd:COG0634   92 rdVLIVEDIIDTGLTLSYLLELLksrgPASvKIATLLDKPERRkvDVPADYVgFEIP 148
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 16-130 1.35e-04

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 40.00  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447214735  16 ARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRH-VDTVCISSYDH--DNQRELKVLKRAEGD--GEGFIVIDDL 90
Cdd:PRK15423  22 GRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHeVDFMTASSYGSgmSTTRDVKILKDLDEDirGKDVLIVEDI 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447214735  91 VDTGGTAVAIREMY----PKAHFV-TIFAKPAGRPlvddyvVDIP 130
Cdd:PRK15423 102 IDSGNTLSKVREILslrePKSLAIcTLLDKPSRRE------VNVP 140
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 39-103 4.64e-04

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 38.52  E-value: 4.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447214735  39 GLVPGALLARELGIRHV----------DTVCISsYD--HDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREM 103
Cdd:COG0503   59 GFILAAALAYALGVPFVparkpgklpgETVSEE-YDleYGTGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKL 134
 
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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