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Conserved domains on  [gi|37289281|gb|AAQ90844|]
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orotate phosphoribosyltransferase, partial [Bacillus sp. AH 645]

Protein Classification

orotate phosphoribosyltransferase( domain architecture ID 10785483)

orotate phosphoribosyltransferase catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)

CATH:  3.40.50.2020
EC:  2.4.2.-
Gene Ontology:  GO:0046132|GO:0004588|GO:0000287
PubMed:  11751055
SCOP:  4000253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-134 2.82e-66

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


:

Pssm-ID: 440229  Cd Length: 201  Bit Score: 199.22  E-value: 2.82e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:COG0461  22 FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAKDHGT 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37289281  91 GNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:COG0461 102 GGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
 
Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-134 2.82e-66

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 199.22  E-value: 2.82e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:COG0461  22 FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAKDHGT 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37289281  91 GNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:COG0461 102 GGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 7-134 8.83e-65

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 195.38  E-value: 8.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    7 PNDPFTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAK 86
Cdd:PRK00455  19 LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37289281   87 GHGKGNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:PRK00455  99 DHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGV 146
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 11-134 3.70e-47

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: 149.89  E-value: 3.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFpTVEVIAGTATAGIAHAAWVSDRM-----DLPMCYVRSKA 85
Cdd:TIGR00336  14 FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVKLakpggDIPLCFNRKEA 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 37289281    86 KGHGKGNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:TIGR00336  93 KDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGV 141
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 42-134 3.09e-21

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: 82.44  E-value: 3.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  42 LEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGKGNQIEGKAE-------KGQKVVVVEDLISTG 114
Cdd:cd06223   5 LAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLElplggdvKGKRVLLVDDVIATG 84

                        90       100
                ....*....|....*....|
gi 37289281 115 GSAITCVEALREAGCEVLGI 134
Cdd:cd06223  85 GTLLAAIELLKEAGAKVVGV 104
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 32-134 1.70e-11

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: 57.76  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    32 PKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGH-GKGNQIEGKAE---KGQKVVVV 107
Cdd:pfam00156   9 PAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPdTSEVMKTSSALpdlKGKTVLIV 88

                          90       100
                  ....*....|....*....|....*..
gi 37289281   108 EDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKI 115
 
Name Accession Description Interval E-value
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-134 2.82e-66

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 199.22  E-value: 2.82e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:COG0461  22 FTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAKDHGT 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 37289281  91 GNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:COG0461 102 GGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGV 145
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 7-134 8.83e-65

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 195.38  E-value: 8.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    7 PNDPFTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAK 86
Cdd:PRK00455  19 LFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37289281   87 GHGKGNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:PRK00455  99 DHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGV 146
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 11-134 3.70e-47

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: 149.89  E-value: 3.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFpTVEVIAGTATAGIAHAAWVSDRM-----DLPMCYVRSKA 85
Cdd:TIGR00336  14 FTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHL-EFDVIAGPALGGIPIATAVSVKLakpggDIPLCFNRKEA 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 37289281    86 KGHGKGNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:TIGR00336  93 KDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGV 141
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 42-134 3.09e-21

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: 82.44  E-value: 3.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  42 LEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGKGNQIEGKAE-------KGQKVVVVEDLISTG 114
Cdd:cd06223   5 LAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLElplggdvKGKRVLLVDDVIATG 84

                        90       100
                ....*....|....*....|
gi 37289281 115 GSAITCVEALREAGCEVLGI 134
Cdd:cd06223  85 GTLLAAIELLKEAGAKVVGV 104
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 11-131 4.47e-15

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 68.33  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEhFPTvEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:PRK13809  28 FILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRPS-FNS-SLLCGVPYTALTLATSISLKYNIPMVLRRKELKNVDP 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 37289281   91 GNQI--EGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEV 131
Cdd:PRK13809 106 SDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVV 148
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 11-134 1.72e-14

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: 66.35  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:TIGR01367  17 FLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDYGLKVDFIVGPAMGGVILGYEVARQLSVRSIFAEREGGGMKL 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 37289281    91 GNQIEgkAEKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:TIGR01367  97 RRGFA--VKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGL 138
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 29-134 4.85e-14

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: 64.71  E-value: 4.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281  29 LSYPKVRQAIAagleELIKEHFPT--VEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAK------------GHGKGNQI 94
Cdd:COG0503  27 LGDPELFRAAG----DELAERFADkgIDKVVGIEARGFILAAALAYALGVPFVPARKPGKlpgetvseeydlEYGTGDTL 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 37289281  95 E--GKA-EKGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:COG0503 103 ElhKDAlKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGI 145
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
11-131 1.19e-13

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 66.24  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   11 FTWSSGIKSPIYCDNRLTLSYPKVRQAIAAGLEELIKEHfpTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGK 90
Cdd:PRK05500 305 YVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNL--TFDRIAGIPYGSLPTATGLALHLHHPMIFPRKEVKAHGT 382

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 37289281   91 GNQIEGKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEV 131
Cdd:PRK05500 383 RRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNV 423
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 32-134 1.70e-11

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: 57.76  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281    32 PKVRQAIAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGH-GKGNQIEGKAE---KGQKVVVV 107
Cdd:pfam00156   9 PAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPdTSEVMKTSSALpdlKGKTVLIV 88

                          90       100
                  ....*....|....*....|....*..
gi 37289281   108 EDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKI 115
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 29-134 2.62e-11

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 57.78  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   29 LSYPKVRQAIAAGLEELIKEHfpTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKG----HGKGNQIE-GKAE---- 99
Cdd:PRK02304  30 LADPEAFREVIDALVERYKDA--DIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPGKLpretISESYELEyGTDTleih 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 37289281  100 -----KGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:PRK02304 108 kdaikPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGA 147
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 38-134 5.63e-09

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 51.79  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   38 IAAGLEELIKEHFPTVEVIAGTATAGIAHAAWVSDRMDLPMCYVRSKAKGHGKGNQIEG------KAEKGQKVVVVEDLI 111
Cdd:PRK02277  71 IASAMADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGsfsrnfASVEGKRCVIVDDVI 150

                         90       100
                 ....*....|....*....|...
gi 37289281  112 STGGSAITCVEALREAGCEVLGI 134
Cdd:PRK02277 151 TSGTTMKETIEYLKEHGGKPVAV 173
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 44-133 3.80e-07

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 46.51  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   44 ELIKEHFPT-VEVIAGTATAGI--AHAawVSDRMDLPMCYVRSKAKGH--------------GKGNQI--EGK-AEK--G 101
Cdd:PRK07322  43 EALAKRLPTeVDVLVTPETKGIplAHA--LSRRLGKPYVVARKSRKPYmqdpiiqevvsittGKPQLLvlDGAdAEKlkG 120

                         90       100       110
                 ....*....|....*....|....*....|..
gi 37289281  102 QKVVVVEDLISTGGSAITCVEALREAGCEVLG 133
Cdd:PRK07322 121 KRVAIVDDVVSTGGTLTALERLVERAGGQVVA 152
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 99-131 3.40e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 44.00  E-value: 3.40e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 37289281   99 EKGQKVVVVEDLISTGGSAITCVEALREAGCEV 131
Cdd:PRK12560 112 EKGDRVAIIDDTLSTGGTVIALIKAIENSGGIV 144
PLN02293 PLN02293
adenine phosphoribosyltransferase
 96-131 2.14e-04

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 39.27  E-value: 2.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 37289281   96 GKAEKGQKVVVVEDLISTGGSAITCVEALREAGCEV 131
Cdd:PLN02293 120 GAVEPGERALVIDDLIATGGTLCAAINLLERAGAEV 155
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 34-134 4.57e-04

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 38.58  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   34 VRQAIAAGLEELIKEHFPtvEVIAGTATAGIAHAAWVSDRMD----LPMCYVRS--------------KAKGHGKGNQIE 95
Cdd:PRK06031  68 VLDALAEHLAEKARAFDP--DVVAGLPTLGLTLAAAVARKLGhtryVPLGTSRKfwyrdelsvplssiTTPDQGKRLYID 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 37289281   96 GKAE---KGQKVVVVEDLISTGGSAITCVEALREAGCEVLGI 134
Cdd:PRK06031 146 PRMLpllEGRRVALIDDVISSGASIVAGLRLLAACGIEPAGI 187
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 100-128 5.62e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 38.36  E-value: 5.62e-04
                         10        20
                 ....*....|....*....|....*....
gi 37289281  100 KGQKVVVVEDLISTGGSAITCVEALREAG 128
Cdd:PRK00934 203 KGKDVLIVDDIISTGGTMATAIKILKEQG 231
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 95-128 2.14e-03

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 36.59  E-value: 2.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 37289281   95 EGKAEkGQKVVVVEDLISTGGSAITCVEALREAG 128
Cdd:PLN02297 225 EGNPA-GRHVVIVDDLVQSGGTLIECQKVLAAHG 257
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 37-128 4.60e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 35.40  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37289281   37 AIAAGLEEL---IKEHFPTVE-VIAGTATAGIAHAAWVSDRMDLPMCYVRS---KAKGHGKGNQIEGKAE---------- 99
Cdd:PLN02238  16 DISARVAELaaqIASDYAGKSpVVLGVATGAFMFLADLVRAIQPLPRGLTVdfiRASSYGGGTESSGVAKvsgadlkidv 95

                         90       100
                 ....*....|....*....|....*....
gi 37289281  100 KGQKVVVVEDLISTGGSAITCVEALREAG 128
Cdd:PLN02238  96 KGKHVLLVEDIVDTGNTLSALVAHLEAKG 124
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
101-128 6.83e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 35.30  E-value: 6.83e-03
                         10        20
                 ....*....|....*....|....*...
gi 37289281  101 GQKVVVVEDLISTGGSAITCVEALREAG 128
Cdd:PRK07199 211 GRTPVLVDDIVSTGRTLIEAARQLRAAG 238
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
88-128 8.31e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 34.92  E-value: 8.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 37289281   88 HGKGNQIEGKAEkGQKVVVVEDLISTGGSAITCVEALREAG 128
Cdd:PRK03092 189 QVVANRVVGDVE-GRTCVLVDDMIDTGGTIAGAVRALKEAG 228
 
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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