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MULTISPECIES: uracil phosphoribosyltransferase [Actinomycetaceae]

Protein Classification

uracil phosphoribosyltransferase( domain architecture ID 10011262)

uracil phosphoribosyltransferase catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate

EC:  2.4.2.9
Gene Ontology:  GO:0004845|GO:0006223
PubMed:  17384901|9628859

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 1-209 2.59e-110

uracil phosphoribosyltransferase; Reviewed


:

Pssm-ID: 234653  Cd Length: 209  Bit Score: 314.33  E-value: 2.59e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   1 MRLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAG 80
Cdd:PRK00129   2 MKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  81 LGMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCIL 160
Cdd:PRK00129  82 LGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497333066 161 AAPEGVATLE----------AAIgDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:PRK00129 162 AAPEGIKALEeahpdveiytAAI-D------------EKLNEHGYIVPGLGDAGDRLFG 207
 
Name Accession Description Interval E-value
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 1-209 2.59e-110

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 314.33  E-value: 2.59e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   1 MRLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAG 80
Cdd:PRK00129   2 MKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  81 LGMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCIL 160
Cdd:PRK00129  82 LGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497333066 161 AAPEGVATLE----------AAIgDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:PRK00129 162 AAPEGIKALEeahpdveiytAAI-D------------EKLNEHGYIVPGLGDAGDRLFG 207
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 2-209 3.84e-108

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 308.92  E-value: 3.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   2 RLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAGL 81
Cdd:COG0035    3 RVHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  82 GMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:COG0035   83 GMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAKDIKIVCLIA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497333066 162 APEGVATLE----------AAIgDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:COG0035  163 APEGIERVQeahpdvdiytAAI-D------------EELNEKGYIVPGLGDAGDRLFG 207
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 2-209 5.29e-84

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 247.93  E-value: 5.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066    2 RLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAGL 81
Cdd:TIGR01091   1 MVVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   82 GMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:TIGR01091  81 GMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPKKIKVLSIVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 497333066  162 APEGVATLEAAIGDradVNVVVAAVDECLNDKSYIVPGLGDAGDRLYG 209
Cdd:TIGR01091 161 APEGIEAVEKAHPD---VDIYTAAIDEKLNDNGYIVPGLGDAGDRAFG 205
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 7-209 6.60e-71

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 214.28  E-value: 6.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066    7 NHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPV-APTTGLTLSEPRPIVVPVLRAGLGMLE 85
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLgTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   86 GMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGA--KDVTCVCILAAP 163
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVpeENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 497333066  164 EGVATLEAAIGDradVNVVVAAVDECLNDKSYIVPGLGDAGDRLYG 209
Cdd:pfam14681 161 EGLHRLAAAFPD---VKIVTAAVDEELNENGYIVPGLGDAGDRLFG 203
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 71-176 9.87e-18

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: 75.90  E-value: 9.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  71 PIVVPVLRAGLGMLEGMTRLLPtAEVGFLGMRRDDNTLEIETYA---NRLPDDLSGRQCFVLDPMLATGHTMVAATNYLF 147
Cdd:cd06223   17 DVVVGILRGGLPLAAALARALG-LPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95

                         90       100
                 ....*....|....*....|....*....
gi 497333066 148 ERGAKDVTCVCILAAPEGVATLEAAIGDR 176
Cdd:cd06223   96 EAGAKVVGVAVLLDKPEGGARELASPGDP 124
 
Name Accession Description Interval E-value
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 1-209 2.59e-110

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 314.33  E-value: 2.59e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   1 MRLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAG 80
Cdd:PRK00129   2 MKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  81 LGMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCIL 160
Cdd:PRK00129  82 LGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497333066 161 AAPEGVATLE----------AAIgDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:PRK00129 162 AAPEGIKALEeahpdveiytAAI-D------------EKLNEHGYIVPGLGDAGDRLFG 207
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 2-209 3.84e-108

Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439805  Cd Length: 209  Bit Score: 308.92  E-value: 3.84e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   2 RLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAGL 81
Cdd:COG0035    3 RVHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRAGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  82 GMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:COG0035   83 GMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAKDIKIVCLIA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497333066 162 APEGVATLE----------AAIgDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:COG0035  163 APEGIERVQeahpdvdiytAAI-D------------EELNEKGYIVPGLGDAGDRLFG 207
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 2-209 5.29e-84

uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees separates this mostly prokaryotic set of uracil phosphoribosyltransferases from a mostly eukaryotic set that includes uracil phosphoribosyltransferase, uridine kinases, and other, uncharacterized proteins. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273438  Cd Length: 207  Bit Score: 247.93  E-value: 5.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066    2 RLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPVAPTTGLTLSEPRPIVVPVLRAGL 81
Cdd:TIGR01091   1 MVVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   82 GMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:TIGR01091  81 GMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPKKIKVLSIVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 497333066  162 APEGVATLEAAIGDradVNVVVAAVDECLNDKSYIVPGLGDAGDRLYG 209
Cdd:TIGR01091 161 APEGIEAVEKAHPD---VDIYTAAIDEKLNDNGYIVPGLGDAGDRAFG 205
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 7-209 6.60e-71

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 214.28  E-value: 6.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066    7 NHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDTPIETPV-APTTGLTLSEPRPIVVPVLRAGLGMLE 85
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLgTTYAGVLFDEKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   86 GMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGA--KDVTCVCILAAP 163
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVpeENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 497333066  164 EGVATLEAAIGDradVNVVVAAVDECLNDKSYIVPGLGDAGDRLYG 209
Cdd:pfam14681 161 EGLHRLAAAFPD---VKIVTAAVDEELNENGYIVPGLGDAGDRLFG 203
PLN02541 PLN02541
uracil phosphoribosyltransferase
 1-209 2.01e-49

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 161.11  E-value: 2.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   1 MRLHVANHPLIAHKLTVLRDRNTPSATFRQLVDELVTLLAYEATREVAVSDT-PIETPVAPTTgLTLSEPR-PI-VVPVL 77
Cdd:PLN02541  32 MLVFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIYEASRDWLPTMTgEVQTPMGVAD-VEFIDPRePVaVVPIL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  78 RAGLGMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDDLS-GRQCFVLDPMLATGHTMVAATNYLFERGA--KDV 154
Cdd:PLN02541 111 RAGLVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPeGSRVLVVDPMLATGGTIVAAIDELVSRGAsvEQI 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497333066 155 TCVCILAAPEGVATLE---------AAIGDradvnvvvaavdECLNDKSYIVPGLGDAGDRLYG 209
Cdd:PLN02541 191 RVVCAVAAPPALKKLSekfpglhvyAGIID------------EEVNEKGYIVPGLGDAGDRSFG 242
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 71-176 9.87e-18

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: 75.90  E-value: 9.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  71 PIVVPVLRAGLGMLEGMTRLLPtAEVGFLGMRRDDNTLEIETYA---NRLPDDLSGRQCFVLDPMLATGHTMVAATNYLF 147
Cdd:cd06223   17 DVVVGILRGGLPLAAALARALG-LPLAFIRKERKGPGRTPSEPYgleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95

                         90       100
                 ....*....|....*....|....*....
gi 497333066 148 ERGAKDVTCVCILAAPEGVATLEAAIGDR 176
Cdd:cd06223   96 EAGAKVVGVAVLLDKPEGGARELASPGDP 124
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 70-165 2.94e-09

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: 53.52  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066   70 RPIVVPVLRAGLGMLEGMTRLLPTAEVGFLGMRRDDNTLEIETYANRLPDdLSGRQCFVLDPMLATGHTMVAATNYLFER 149
Cdd:pfam00156  30 PDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPD-LKGKTVLIVDDILDTGGTLLKVLELLKNV 108

                          90
                  ....*....|....*.
gi 497333066  150 GAKDVTCVCILAAPEG 165
Cdd:pfam00156 109 GPKEVKIAVLIDKPAG 124
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 94-161 6.26e-09

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 54.59  E-value: 6.26e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497333066   94 AEVGFLGMRRDDNTLEIETyaNRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:TIGR01251 183 CPLAIIDKRRISATNEVEV--MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHG 248
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
102-166 2.85e-07

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 49.56  E-value: 2.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497333066 102 RRDDNTLEIETYANRLPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVtcvcILAAPEGV 166
Cdd:PRK03092 180 KTRDPTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV----IIAATHGV 240
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 120-159 3.98e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 43.36  E-value: 3.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 497333066 120 DLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCI 159
Cdd:PRK00934 201 DVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
102-172 1.12e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 39.15  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497333066 102 RRDDNTLEIetyanRLPDD--LSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA--APEGVATLEAA 172
Cdd:PRK07199 193 RHGDRDVEI-----SLPDAapWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVVHAlfAGDAYSALAAA 262
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 117-161 1.65e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 38.78  E-value: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 497333066 117 LPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILA 161
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAATFG 302
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 66-157 3.89e-03

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 36.76  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497333066  66 LSEPRPIVVPVLRAGL---GMLegMTRLLPTAEVGFLGMRRDDNtleiETYANRL-----PD-DLSGRQCFVLDPMLATG 136
Cdd:PRK09162  37 LADENPLVLCVMGGGLvftGQL--LPRLDFPLEFDYLHATRYRN----ETTGGELvwkvkPReSLKGRTVLVVDDILDEG 110

                         90       100
                 ....*....|....*....|..
gi 497333066 137 HTMVAATNYLFERGAKDV-TCV 157
Cdd:PRK09162 111 HTLAAIRDRCLEMGAAEVySAV 132
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 117-165 5.65e-03

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: 36.16  E-value: 5.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 497333066 117 LPDDLSGRQCFVLDPMLATGHTMVAATNYLFERGAKDVTCVCILAAPEG 165
Cdd:COG0634   85 LDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPER 133
 
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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