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Conserved domains on  [gi|1933926105|ref|WP_195233158|]
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MULTISPECIES: adenine phosphoribosyltransferase [Holdemanella]

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
 1-172 5.40e-94

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 270.02  E-value: 5.40e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKP 80
Cdd:PRK02304    4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  81 GKLPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFK 160
Cdd:PRK02304   84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163

                         170
                  ....*....|..
gi 1933926105 161 DIPVCALTHYEG 172
Cdd:PRK02304  164 GYPVKSLVKFDG 175
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 1-172 5.40e-94

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 270.02  E-value: 5.40e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKP 80
Cdd:PRK02304    4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  81 GKLPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFK 160
Cdd:PRK02304   84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163

                         170
                  ....*....|..
gi 1933926105 161 DIPVCALTHYEG 172
Cdd:PRK02304  164 GYPVKSLVKFDG 175
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 1-170 1.18e-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: 1.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKP 80
Cdd:COG0503     1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  81 GKLPRETVSETYDLEYG-QDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKF 159
Cdd:COG0503    81 GKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                         170
                  ....*....|.
gi 1933926105 160 KDIPVCALTHY 170
Cdd:COG0503   161 RDYPVESLLTL 171
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 3-170 2.28e-82

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: 240.64  E-value: 2.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   3 LKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKPGK 82
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  83 LPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFKD- 161
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPn 160


                  ....*....
gi 1933926105 162 IPVCALTHY 170
Cdd:TIGR01090 161 VPVFSLLEY 169
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-162 6.69e-23

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: 88.22  E-value: 6.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  50 DVVIGPEARGFLFGVPVALENNVGFVPVRKPGKLPRETVSETYDLEYgqdelcvHADAILPGQKVVIIDDLLATGGTVEA 129
Cdd:cd06223    17 DVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLEL-------PLGGDVKGKRVLLVDDVIATGGTLLA 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1933926105 130 IIKMVERMQASVTGVAFVIELDDLKGREKFKDI 162
Cdd:cd06223    90 AIELLKEAGAKVVGVAVLLDKPEGGARELASPG 122
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 50-149 3.90e-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: 52.75  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  50 DVVIGPEARGFLFGVPVALENNVGFVPVRKPGKLPRETVSETYdleygqdelcVHADAILPGQKVVIIDDLLATGGTVEA 129
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKTVLIVDDILDTGGTLLK 100

                          90       100
                  ....*....|....*....|
gi 1933926105 130 IIKMVERMQASVTGVAFVIE 149
Cdd:pfam00156 101 VLELLKNVGPKEVKIAVLID 120
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 1-172 5.40e-94

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 270.02  E-value: 5.40e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKP 80
Cdd:PRK02304    4 EDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  81 GKLPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFK 160
Cdd:PRK02304   84 GKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE 163

                         170
                  ....*....|..
gi 1933926105 161 DIPVCALTHYEG 172
Cdd:PRK02304  164 GYPVKSLVKFDG 175
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 1-170 1.18e-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: 1.18e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKP 80
Cdd:COG0503     1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  81 GKLPRETVSETYDLEYG-QDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKF 159
Cdd:COG0503    81 GKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                         170
                  ....*....|.
gi 1933926105 160 KDIPVCALTHY 170
Cdd:COG0503   161 RDYPVESLLTL 171
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 3-170 2.28e-82

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: 240.64  E-value: 2.28e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   3 LKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKPGK 82
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  83 LPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFKD- 161
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPn 160


                  ....*....
gi 1933926105 162 IPVCALTHY 170
Cdd:TIGR01090 161 VPVFSLLEY 169
PLN02293 PLN02293
adenine phosphoribosyltransferase
 2-172 1.54e-60

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 186.03  E-value: 1.54e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   2 DLKDYIESIPGFPKEGIIFRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKPG 81
Cdd:PLN02293   16 GISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLRKPG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  82 KLPRETVSETYDLEYGQDELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFKD 161
Cdd:PLN02293   96 KLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREKLNG 175

                         170
                  ....*....|.
gi 1933926105 162 IPVCALTHYEG 172
Cdd:PLN02293  176 KPLFVLVESRG 186
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 1-160 1.67e-40

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 134.91  E-value: 1.67e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   1 MDLKDYIESIPGFPKEGII--FRDVTPILQNAsAMRYCVDQLNDFVkSVGADVVIGPEARGFLFGVPVALennVGFVPVR 78
Cdd:PRK12560    4 KNLYKNARVVNSGKALTTVneFTDQLPALRPK-VLKETAKEIIKYI-DKDIDKIVTEEDKGAPLATPVSL---LSGKPLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  79 KPGKLPRETVSETYD-LEYGQD--ELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKG 155
Cdd:PRK12560   79 MARWYPYSLSELNYNvVEIGSEyfEGVVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNG 158


                  ....*
gi 1933926105 156 REKFK 160
Cdd:PRK12560  159 RKKLF 163
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-162 6.69e-23

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: 88.22  E-value: 6.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  50 DVVIGPEARGFLFGVPVALENNVGFVPVRKPGKLPRETVSETYDLEYgqdelcvHADAILPGQKVVIIDDLLATGGTVEA 129
Cdd:cd06223    17 DVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLEL-------PLGGDVKGKRVLLVDDVIATGGTLLA 89

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1933926105 130 IIKMVERMQASVTGVAFVIELDDLKGREKFKDI 162
Cdd:cd06223    90 AIELLKEAGAKVVGVAVLLDKPEGGARELASPG 122
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 47-171 3.06e-10

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 56.32  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  47 VGADVVIGPEARGFLFGVPVALENNVGFVPVRKPGKlpretvsetydlEYGQDELCVhaDAILPGQKVVIIDDLLATGGT 126
Cdd:COG0461    62 PEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGTGGQIE--GGLLPGERVLVVEDVITTGGS 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1933926105 127 VEAIIKMVERMQASVTGVAFVIELDDlKGREKFKD--IPVCALTHYE 171
Cdd:COG0461   128 VLEAVEALREAGAEVVGVAVIVDREE-GAAENLEEagVPLHSLLTLD 173
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 20-171 1.06e-09

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 55.38  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  20 FRDVTPILQNASAMRYCVDQLNDFVKSVGADVVIGPEARGFLFGVPVALENNVGFVPVRKPgklpRETVSETYDLEYGQD 99
Cdd:PRK08558   83 YVDNSSVVFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKS----KETGVEKFYEEYQRL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105 100 E------LCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDlKGREKFK---DIPVCALTHY 170
Cdd:PRK08558  159 AsgievtLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGE-VGIDRAReetDAPVDALYTL 237


                  .
gi 1933926105 171 E 171
Cdd:PRK08558  238 E 238
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 50-149 3.90e-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: 52.75  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  50 DVVIGPEARGFLFGVPVALENNVGFVPVRKPGKLPRETVSETYdleygqdelcVHADAILPGQKVVIIDDLLATGGTVEA 129
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT----------SSALPDLKGKTVLIVDDILDTGGTLLK 100

                          90       100
                  ....*....|....*....|
gi 1933926105 130 IIKMVERMQASVTGVAFVIE 149
Cdd:pfam00156 101 VLELLKNVGPKEVKIAVLID 120
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 47-171 6.64e-09

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 52.85  E-value: 6.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  47 VGADVVIGPEARGFLFGVPVALENNVGFVPVRKPGKlpretvsetydlEYGQD---ELcvhadAILPGQKVVIIDDLLAT 123
Cdd:PRK00455   63 IEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEGgqiEG-----RRLFGKRVLVVEDVITT 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1933926105 124 GGTVEAIIKMVERMQASVTGVAfVIeLD-DLKGREKFKD--IPVCALTHYE 171
Cdd:PRK00455  126 GGSVLEAVEAIRAAGAEVVGVA-VI-VDrQSAAQEVFADagVPLISLITLD 174
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 86-167 1.09e-07

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 49.40  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  86 ETVSETYDLEYgqdELCVHADAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFKD--IP 163
Cdd:PRK09219   95 TVYSFTKQVTS---TVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEEkgYR 171


                  ....
gi 1933926105 164 VCAL 167
Cdd:PRK09219  172 VESL 175
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 48-169 1.30e-07

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 48.82  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  48 GADVVIGPEARGFLFGVPVALENNVGFVPVRKPGK------LPRETVSETYdleyGQDELCV----HADAILpGQKVVII 117
Cdd:PRK07322   52 EVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKpymqdpIIQEVVSITT----GKPQLLVldgaDAEKLK-GKRVAIV 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1933926105 118 DDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREkfkdiPVCALTH 169
Cdd:PRK07322  127 DDVVSTGGTLTALERLVERAGGQVVAKAAIFAEGDASNRL-----DVIYLAH 173
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 50-149 5.54e-07

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: 47.86  E-value: 5.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  50 DVVIGPEARGflfgVPVALEN----NVGFVPVRKPGKLPR-ETVSETYdLEYGQD---ELCVHADAILPGQKVVIIDDLL 121
Cdd:TIGR01743 130 DAVMTVATKG----IPLAYAVasvlNVPLVIVRKDSKVTEgSTVSINY-VSGSSNriqTMSLAKRSLKTGSKVLIIDDFM 204

                          90       100
                  ....*....|....*....|....*...
gi 1933926105 122 ATGGTVEAIIKMVERMQASVTGVAFVIE 149
Cdd:TIGR01743 205 KAGGTINGMINLLDEFDAEVAGIGVLID 232
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 32-149 3.08e-05

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: 42.47  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  32 AMRYCvDQLNDFVKSVGA--DVVIGPEARGFLFGVPVALENNVGFVPVRKPG---KLPRetvsetydleygqdelcvhAD 106
Cdd:TIGR01367  41 LMELG-GELAQKILDYGLkvDFIVGPAMGGVILGYEVARQLSVRSIFAEREGggmKLRR-------------------GF 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1933926105 107 AILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIE 149
Cdd:TIGR01367 101 AVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIID 143
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 34-170 2.06e-04

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: 39.72  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  34 RYCVDQLNDFVKsvgADVVIGPEARGFLFGVPVAL-----ENNVGFVPVRKPGKlpretvsetydlEYGQDELCVhaDAI 108
Cdd:TIGR00336  43 RYAAAIIKSHLE---FDVIAGPALGGIPIATAVSVklakpGGDIPLCFNRKEAK------------DHGEGGNIE--GEL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933926105 109 LPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIELDDLKGREKFK---DIPVCALTHY 170
Cdd:TIGR00336 106 LEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEFEkeyGLPVISLITL 170
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 8-167 3.55e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 39.47  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105   8 ESIPGFPKEgiIFRDVTPILQNASAMRYCVDQLNDFVKSVG--ADVVIGPEargfLFGVPVA------LENNVG-FVPVR 78
Cdd:PRK02277   45 LEKAPAPKD--IHIDWSSIGSSSSRLRYIASAMADMLEKEDeeVDVVVGIA----KSGVPLAtlvadeLGKDLAiYHPKK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933926105  79 ---KPGKLPRETVSETYdleygqdelcvhadAILPGQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFVIeldDLKG 155
Cdd:PRK02277  119 wdhGEGEKKTGSFSRNF--------------ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLI---DKSG 181

                         170
                  ....*....|..
gi 1933926105 156 REKFKDIPVCAL 167
Cdd:PRK02277  182 IDEIDGVPVYSL 193
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 111-147 9.34e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 35.66  E-value: 9.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1933926105 111 GQKVVIIDDLLATGGTVEAIIKMVERMQASVTGVAFV 147
Cdd:PRK00934  204 GKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 240
 
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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