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Conserved domains on  [gi|446439683|ref|WP_000517538|]
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MULTISPECIES: uracil phosphoribosyltransferase [Bacillus]

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 7.66e-145

uracil phosphoribosyltransferase; Reviewed


:

Pssm-ID: 234653  Cd Length: 209  Bit Score: 401.39  E-value: 7.66e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   1 MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRA 80
Cdd:PRK00129   1 MMKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  81 GLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:PRK00129  81 GLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446439683 161 VAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:PRK00129 161 VAAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGTK 209
 
Name Accession Description Interval E-value
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 1-209 7.66e-145

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 401.39  E-value: 7.66e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   1 MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRA 80
Cdd:PRK00129   1 MMKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  81 GLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:PRK00129  81 GLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446439683 161 VAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:PRK00129 161 VAAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGTK 209
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 1-209 4.71e-141

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 392.12  E-value: 4.71e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   1 MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRA 80
Cdd:COG0035    1 MLRVHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  81 GLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:COG0035   81 GLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAKDIKIVCL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446439683 161 VAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:COG0035  161 IAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 3-209 2.50e-121

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: 341.92  E-value: 2.50e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683    3 KLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRAGL 82
Cdd:TIGR01091   1 MVVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   83 GMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCIVA 162
Cdd:TIGR01091  81 GMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPKKIKVLSIVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446439683  163 APEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:TIGR01091 161 APEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGTK 207
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 8-208 5.33e-103

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: 295.56  E-value: 5.33e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683    8 DHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAG-KKLGLIPILRAGLGMVD 86
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   87 GILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGA--KHIKLMCIVAAP 164
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVpeENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446439683  165 EGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGT 208
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 69-183 3.37e-16

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: 71.66  E-value: 3.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  69 GKKLGLIPILRAGLGMVDGILKLIPAaKVGHVGLYRDPKTLQPVEYYVK---LPTDVEERDFIVLDPMLATGGSAAEAIN 145
Cdd:cd06223   14 LEPDVVVGILRGGLPLAAALARALGL-PLAFIRKERKGPGRTPSEPYGLelpLGGDVKGKRVLLVDDVIATGGTLLAAIE 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446439683 146 SLKKRGAKHIKLMCIVAAPEGVKVVqEEHPDVDIYVAA 183
Cdd:cd06223   93 LLKEAGAKVVGVAVLLDKPEGGARE-LASPGDPVYSLF 129
 
Name Accession Description Interval E-value
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 1-209 7.66e-145

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 401.39  E-value: 7.66e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   1 MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRA 80
Cdd:PRK00129   1 MMKVHVVDHPLIQHKLTLLRDKNTSTKRFRELLEELGRLLAYEATRDLPLEEVEIETPLGKTTGKRIAGKKLVIVPILRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  81 GLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:PRK00129  81 GLGMVDGVLKLIPSARVGHIGLYRDEETLEPVEYYVKLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446439683 161 VAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:PRK00129 161 VAAPEGIKALEEAHPDVEIYTAAIDEKLNEHGYIVPGLGDAGDRLFGTK 209
Upp COG0035
Uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Uracil ...
 1-209 4.71e-141

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


Pssm-ID: 439805  Cd Length: 209  Bit Score: 392.12  E-value: 4.71e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   1 MGKLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRA 80
Cdd:COG0035    1 MLRVHVVDHPLIQHKLTLLRDKNTDTKEFRRLLEELGRLLAYEATRDLPLEEVEVETPLGKTTGKVLAGKKLVIVPILRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  81 GLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:COG0035   81 GLGMLDGVLDLLPSARVGHIGLYRDEETLEPVEYYFKLPEDLEGRTVIVLDPMLATGGSLVAAIDLLKKRGAKDIKIVCL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446439683 161 VAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:COG0035  161 IAAPEGIERVQEAHPDVDIYTAAIDEELNEKGYIVPGLGDAGDRLFGTK 209
upp TIGR01091
uracil phosphoribosyltransferase; A fairly deep split in phylogenetic and UPGMA trees ...
 3-209 2.50e-121

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: 341.92  E-value: 2.50e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683    3 KLYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAGKKLGLIPILRAGL 82
Cdd:TIGR01091   1 MVVVVDHPLIKHKLTLLRDKNTDTKEFRELLRELGRLLAYEATRDLELEEVEVETPLGETEGGRILGKKIVLVPILRAGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   83 GMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCIVA 162
Cdd:TIGR01091  81 GMVDGVLKLIPEAKVGHVGAYRNEETLKPVPYYSKLPEDIDERTVIVLDPMLATGGTMIAALDLLKKRGPKKIKVLSIVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 446439683  163 APEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGTK 209
Cdd:TIGR01091 161 APEGIEAVEKAHPDVDIYTAAIDEKLNDNGYIVPGLGDAGDRAFGTK 207
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 8-208 5.33e-103

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: 295.56  E-value: 5.33e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683    8 DHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRDLPLKDIEIETPVSKATTKVIAG-KKLGLIPILRAGLGMVD 86
Cdd:pfam14681   1 DHPLLKHLLTILRDKSTSGPDFRFASDRIGRLLAYEALRDLPTEEVTVETPLGTTYAGVLFDeKKICGVPILRAGEGMED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   87 GILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGA--KHIKLMCIVAAP 164
Cdd:pfam14681  81 GLRDLLPGARVGHIGIQRDEETLQPVEYYNKLPKDISDRTVILLDPMLATGGSAIAAIQVLREHGVpeENIVVLSVIAAP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446439683  165 EGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGT 208
Cdd:pfam14681 161 EGLHRLAAAFPDVKIVTAAVDEELNENGYIVPGLGDAGDRLFGT 204
PLN02541 PLN02541
uracil phosphoribosyltransferase
 4-208 1.48e-57

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 181.91  E-value: 1.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   4 LYVFDHPLIQHKITYIRDKNTGTKDFRELVDEVASLMAFEITRD-LPLKDIEIETPVSKATTKVI-AGKKLGLIPILRAG 81
Cdd:PLN02541  34 VFVPPHPLIKHWLSVLRNEQTPPPIFRSAMAELGRLLIYEASRDwLPTMTGEVQTPMGVADVEFIdPREPVAVVPILRAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  82 LGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPTDVEERD-FIVLDPMLATGGSAAEAINSLKKRGAKH--IKLM 158
Cdd:PLN02541 114 LVLLEHASSVLPATKTYHLGFVRDEETLQPSMYLNKLPDKFPEGSrVLVVDPMLATGGTIVAAIDELVSRGASVeqIRVV 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446439683 159 CIVAAPEGVKVVQEEHPDVDIYVAALDEKLNDHGYVVPGLGDAGDRLFGT 208
Cdd:PLN02541 194 CAVAAPPALKKLSEKFPGLHVYAGIIDEEVNEKGYIVPGLGDAGDRSFGT 243
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 69-183 3.37e-16

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: 71.66  E-value: 3.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683  69 GKKLGLIPILRAGLGMVDGILKLIPAaKVGHVGLYRDPKTLQPVEYYVK---LPTDVEERDFIVLDPMLATGGSAAEAIN 145
Cdd:cd06223   14 LEPDVVVGILRGGLPLAAALARALGL-PLAFIRKERKGPGRTPSEPYGLelpLGGDVKGKRVLLVDDVIATGGTLLAAIE 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446439683 146 SLKKRGAKHIKLMCIVAAPEGVKVVqEEHPDVDIYVAA 183
Cdd:cd06223   93 LLKEAGAKVVGVAVLLDKPEGGARE-LASPGDPVYSLF 129
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 121-160 4.30e-06

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 46.06  E-value: 4.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446439683 121 DVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:PRK00934 201 DVKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 118-163 1.19e-05

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 44.94  E-value: 1.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446439683 118 LPTDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIklmcIVAA 163
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKI----IVAA 299
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 120-167 2.24e-05

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: 44.19  E-value: 2.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446439683  120 TDVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIklmcIVAAPEGV 167
Cdd:TIGR01251 206 GDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRV----IAAATHGV 249
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
121-167 3.27e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 43.40  E-value: 3.27e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446439683 121 DVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIklmcIVAAPEGV 167
Cdd:PRK03092 198 DVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDV----IIAATHGV 240
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 74-171 4.07e-05

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: 41.97  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446439683   74 LIPILRAGLGMVDGILKLIPAAKVGHVGLYRDPKTLQPVEYYVKLPtDVEERDFIVLDPMLATGGSAAEAINSLKKRGAK 153
Cdd:pfam00156  33 VVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALP-DLKGKTVLIVDDILDTGGTLLKVLELLKNVGPK 111

                          90
                  ....*....|....*...
gi 446439683  154 HIKLMCIVAAPEGVKVVQ 171
Cdd:pfam00156 112 EVKIAVLIDKPAGTEPKD 129
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 121-160 4.42e-04

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 40.04  E-value: 4.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446439683 121 DVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHIKLMCI 160
Cdd:COG0462  208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAAT 247
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
121-155 9.32e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 36.25  E-value: 9.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446439683 121 DVEERDFIVLDPMLATGGSAAEAINSLKKRGAKHI 155
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSV 239
 
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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