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Conserved domains on  [gi|488981313|ref|WP_002892145|]
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MULTISPECIES: adenine phosphoribosyltransferase [Klebsiella]

Protein Classification

purine phosphoribosyltransferase family protein( domain architecture ID 10011795)

purine phosphoribosyltransferase family protein similar to adenine phosphoribosyltransferase and hypoxanthine/guanine phosphoribosyltransferase

EC:  2.4.2.-
Gene Ontology:  GO:0106130|GO:0016757
PubMed:  11751055|7030616

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 6-182 1.80e-100

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 286.97  E-value: 1.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   6 QQLEYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPV 85
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  86 RKPRKLPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQ 165
Cdd:PRK02304  81 RKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGRE 160

                        170
                 ....*....|....*..
gi 488981313 166 RLEklGIHCYSLVPFPG 182
Cdd:PRK02304 161 KLE--GYPVKSLVKFDG 175
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 6-182 1.80e-100

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 286.97  E-value: 1.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   6 QQLEYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPV 85
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  86 RKPRKLPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQ 165
Cdd:PRK02304  81 RKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGRE 160

                        170
                 ....*....|....*..
gi 488981313 166 RLEklGIHCYSLVPFPG 182
Cdd:PRK02304 161 KLE--GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 11-180 1.60e-92

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 266.84  E-value: 1.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   11 LKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKPRK 90
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   91 LPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKL 170
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 488981313  171 gIHCYSLVPF 180
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 9-178 1.77e-82

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: 241.13  E-value: 1.77e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   9 EYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKP 88
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  89 RKLPRETIAETYELEYGTDQ-LEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRL 167
Cdd:COG0503   81 GKLPGETVSEEYDLEYGTGDtLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                        170
                 ....*....|.
gi 488981313 168 EKLGIHcySLV 178
Cdd:COG0503  161 RDYPVE--SLL 169
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 45-177 1.59e-25

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: 95.16  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  45 IELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLPRETIAETYeleygtdQLEIHVDAIKPGDKV 122
Cdd:cd06223    2 GRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGKRV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488981313 123 LVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDlGGEQRLEKLGIHCYSL 177
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSL 128
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
46-178 2.49e-14

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 67.25  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  46 ELLTE------RYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRK-PRKLPREtIAETYELEYGTDQLeiHVDAIKP 118
Cdd:NF040646  37 ELLREiadriiKIADLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE-VEVHQSTGYSKGEL--YINGINK 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313 119 GDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDlGGEQRLEKLGIHCYSLV 178
Cdd:NF040646 114 GDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERGE-GKKIVEEKTGYKVKTLV 172
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 30-155 3.35e-12

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: 61.23  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   30 DVTSLLEDPKAYALSIELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLPRETIAETYeleygtd 107
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488981313  108 qleIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGE-VHDAAFI 155
Cdd:pfam00156  74 ---SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKeVKIAVLI 119
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 6-182 1.80e-100

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 286.97  E-value: 1.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   6 QQLEYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPV 85
Cdd:PRK02304   1 MMLEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  86 RKPRKLPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQ 165
Cdd:PRK02304  81 RKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGRE 160

                        170
                 ....*....|....*..
gi 488981313 166 RLEklGIHCYSLVPFPG 182
Cdd:PRK02304 161 KLE--GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 11-180 1.60e-92

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 266.84  E-value: 1.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   11 LKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKPRK 90
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   91 LPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKL 170
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 488981313  171 gIHCYSLVPF 180
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 9-178 1.77e-82

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: 241.13  E-value: 1.77e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   9 EYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKP 88
Cdd:COG0503    1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  89 RKLPRETIAETYELEYGTDQ-LEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRL 167
Cdd:COG0503   81 GKLPGETVSEEYDLEYGTGDtLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                        170
                 ....*....|.
gi 488981313 168 EKLGIHcySLV 178
Cdd:COG0503  161 RDYPVE--SLL 169
PLN02293 PLN02293
adenine phosphoribosyltransferase
 7-178 8.81e-77

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 227.63  E-value: 8.81e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   7 QLEYLKNSIQSIEDYPKPGILFRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVR 86
Cdd:PLN02293  13 RLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  87 KPRKLPRETIAETYELEYGTDQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQR 166
Cdd:PLN02293  93 KPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREK 172

                        170
                 ....*....|..
gi 488981313 167 LEklGIHCYSLV 178
Cdd:PLN02293 173 LN--GKPLFVLV 182
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 8-178 7.60e-39

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 131.06  E-value: 7.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   8 LEYLKNSIQSIEDYPKPGIL--FRDVTSLLEdPKAYALSIELLTeRYKDAGITKVVGTEARGFLFGAPVALalgVGFVPV 85
Cdd:PRK12560   3 LKNLYKNARVVNSGKALTTVneFTDQLPALR-PKVLKETAKEII-KYIDKDIDKIVTEEDKGAPLATPVSL---LSGKPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  86 RKPRKLPRETIAETY-ELEYGTDQLE--IHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLG 162
Cdd:PRK12560  78 AMARWYPYSLSELNYnVVEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNN 157

                        170
                 ....*....|....*..
gi 488981313 163 GEQRL-EKLGIHCYSLV 178
Cdd:PRK12560 158 GRKKLfTQTGINVKSLV 174
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 45-177 1.59e-25

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: 95.16  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  45 IELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLPRETIAETYeleygtdQLEIHVDAIKPGDKV 122
Cdd:cd06223    2 GRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGKRV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488981313 123 LVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDlGGEQRLEKLGIHCYSL 177
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSL 128
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 34-178 5.05e-19

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 80.20  E-value: 5.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  34 LLEDPKAYALSIELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKlpretiaetyelEYGTD-QLE 110
Cdd:COG0461   39 VLSYPEALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGTGgQIE 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981313 111 ihvDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINlFDLGGEQRLEKLGIHCYSLV 178
Cdd:COG0461  107 ---GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVD-REEGAAENLEEAGVPLHSLL 170
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 34-178 1.61e-15

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 70.96  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  34 LLEDPKAYALSIELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKlpretiaetyelEYGTD-QLE 110
Cdd:PRK00455  40 LLSYPEALALLGRFLAEAIKDSGieFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEGgQIE 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488981313 111 IhvdAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDlGGEQRLEKLGIHCYSLV 178
Cdd:PRK00455 108 G---RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQS-AAQEVFADAGVPLISLI 171
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
46-178 2.49e-14

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 67.25  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  46 ELLTE------RYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRK-PRKLPREtIAETYELEYGTDQLeiHVDAIKP 118
Cdd:NF040646  37 ELLREiadriiKIADLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE-VEVHQSTGYSKGEL--YINGINK 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313 119 GDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDlGGEQRLEKLGIHCYSLV 178
Cdd:NF040646 114 GDRVLIVDDVISTGGTLIAVIKALEKAGAEIKDVVVVIERGE-GKKIVEEKTGYKVKTLV 172
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 50-177 1.12e-12

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 63.26  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  50 ERYKDAGITKVVGTEARGFlfgAP---VALALGVGFVPVRK--PRKLPRET-IAETYELeygTDQLEIHV----DAIKPG 119
Cdd:PRK09219  44 RRFKDEGITKILTIEASGI---APavmAALALGVPVVFAKKkkSLTLTDDVyTATVYSF---TKQVTSTVsvskKFLSEG 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488981313 120 DKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKLGIHCYSL 177
Cdd:PRK09219 118 DRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEEKGYRVESL 175
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 30-155 3.35e-12

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: 61.23  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   30 DVTSLLEDPKAYALSIELLTERYKDAG--ITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLPRETIAETYeleygtd 107
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGgkPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488981313  108 qleIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGE-VHDAAFI 155
Cdd:pfam00156  74 ---SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKeVKIAVLI 119
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 28-172 1.44e-11

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 60.78  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  28 FRDVTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLPRETIAETYE-LEYGT 106
Cdd:PRK08558  83 YVDNSSVVFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKSKETGVEKFYEEYQrLASGI 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981313 107 D-QLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKLGI 172
Cdd:PRK08558 163 EvTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDA 229
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 31-156 7.12e-08

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 50.55  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   31 VTSLLEDPKAYALSIELLTERYKDAGITKVVGTEARGFLFGAPVALALGVGFVPVRKPRKLpreTIAETYELEY--GT-- 106
Cdd:TIGR01743 103 LTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGIPLAYAVASVLNVPLVIVRKDSKV---TEGSTVSINYvsGSsn 179

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488981313  107 --DQLEIHVDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFII 156
Cdd:TIGR01743 180 riQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVAGIGVLI 231
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 32-163 1.50e-07

orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273579  Cd Length: 187  Bit Score: 49.01  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   32 TSLLEDPKAYALSIELLTERYKDAGIT--KVVGTEARGFLFGAPVALALGVGFVPVRKPRKlpretiaeTYELEYGTdql 109
Cdd:TIGR01367  32 ATLLEHPEALMELGGELAQKILDYGLKvdFIVGPAMGGVILGYEVARQLSVRSIFAEREGG--------GMKLRRGF--- 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488981313  110 eihvdAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGG 163
Cdd:TIGR01367 101 -----AVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGK 149
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 113-178 1.16e-05

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 43.57  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488981313  113 VDAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKL-GIHCYSLV 178
Cdd:TIGR00336 102 EGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEFEKEyGLPVISLI 168
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 60-149 1.03e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.12  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  60 VVGTEARGFLFGAPVALALGVGFVPVRKPRK------LPRETIAETYeleyGTDQLEI----HVDAIKpGDKVLVVDDLL 129
Cdd:PRK07322  56 LVTPETKGIPLAHALSRRLGKPYVVARKSRKpymqdpIIQEVVSITT----GKPQLLVldgaDAEKLK-GKRVAIVDDVV 130

                         90       100
                 ....*....|....*....|
gi 488981313 130 ATGGTIDATVKLIRRLGGEV 149
Cdd:PRK07322 131 STGGTLTALERLVERAGGQV 150
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 119-153 5.32e-04

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: 38.67  E-value: 5.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488981313 119 GDKVLVVDDLLATGGTIDATVKLIRRLG-GEVHDAA 153
Cdd:COG2236   88 GKRVLIVDDVADTGRTLEAVRDLLKEAGpAEVRTAV 123
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
117-180 6.04e-04

bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 39.67  E-value: 6.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488981313 117 KPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDaafIINLFDLGGE--QRLEKLGIHCYSLVPF 180
Cdd:PRK05500 391 HPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRD---IVVFIDHEQGvkDKLQSHGYQAYSVLTI 453
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 74-172 6.34e-04

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: 39.18  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313   74 VALALGVGFVPVRKPRKLPRETIAETyeleygtdQLEIHVDaikpGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAA 153
Cdd:TIGR01251 177 VADALGCPLAIIDKRRISATNEVEVM--------NLVGDVE----GKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAA 244

                          90
                  ....*....|....*....
gi 488981313  154 FIINLFDLGGEQRLEKLGI 172
Cdd:TIGR01251 245 ATHGVFSGPAIERIANAGV 263
PLN02541 PLN02541
uracil phosphoribosyltransferase
 98-151 7.23e-04

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 39.00  E-value: 7.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488981313  98 ETYELEYGTD----QLEIHV----DAIKPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHD 151
Cdd:PLN02541 128 KTYHLGFVRDeetlQPSMYLnklpDKFPEGSRVLVVDPMLATGGTIVAAIDELVSRGASVEQ 189
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 119-173 1.52e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 37.97  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488981313 119 GDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLFDLGGEQRLEKLGIH 173
Cdd:PRK00934 204 GKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVHPVLVGDAILKLYNAGVD 258
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 46-149 1.95e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 37.81  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313  46 ELLTERYKDAGITKVVGTEARGFLFGAPVALALGVG-FVPVRKPRKL-PRETIAETYE-LEYGTDQLEIHVD----AIKP 118
Cdd:PRK06031  74 EHLAEKARAFDPDVVAGLPTLGLTLAAAVARKLGHTrYVPLGTSRKFwYRDELSVPLSsITTPDQGKRLYIDprmlPLLE 153

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488981313 119 GDKVLVVDDLLATGGTIDATVKLIRRLGGEV 149
Cdd:PRK06031 154 GRRVALIDDVISSGASIVAGLRLLAACGIEP 184
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 103-181 1.98e-03

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 37.51  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981313 103 EYGTDQlEIHVDAI-KPGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFIINLfDLGGEQRLEKLGIHCYSLVPFP 181
Cdd:PRK13809 102 NVDPSD-AIKVEGLfTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDR-QKGACQPLGPQGIKLSSVFTVP 179
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 118-155 2.00e-03

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: 37.47  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 488981313  118 PGDKVLVVDDLLATGGTIDATVKLIRRLGGEVHDAAFI 155
Cdd:pfam14681 117 SDRTVILLDPMLATGGSAIAAIQVLREHGVPEENIVVL 154
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
122-146 6.14e-03

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 35.82  E-value: 6.14e-03
                         10        20
                 ....*....|....*....|....*
gi 488981313 122 VLVVDDLLATGGTIDATVKLIRRLG 146
Cdd:COG1926  124 VILVDDGIATGATMRAALRALRRQG 148
 
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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