NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|5822236]
View 

Chain A, ADENINE PHOSPHORIBOSYLTRANSFERASE

Protein Classification

type I phosphoribosyltransferase( domain architecture ID 27)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 7-189 1.67e-45

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.


The actual alignment was detected with superfamily member PLN02293:

Pssm-ID: 444823  Cd Length: 187  Bit Score: 150.21  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     7 PNSFLLDDSHALSQLLKKSYRWYsPVFSPRNVpRFADVSSITESPETLKAIRDFLVQRYRAMspAPTHILGFDARGFLFG 86
Cdd:PLN02293   2 FAMENGDQGDPRLQGISSAIRVV-PDFPKPGI-MFQDITTLLLDPKAFKDTIDLFVERYRDM--GISVVAGIEARGFIFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    87 PMIAVELEIPFVLMRKADKNAGLLIrSEPYEKEYkeaAPEVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDA 166
Cdd:PLN02293  78 PPIALAIGAKFVPLRKPGKLPGEVI-SEEYVLEY---GTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGA 153

                        170       180
                 ....*....|....*....|...
gi 5822236   167 VVVEMVSILSIPFLKAAEKIHST 189
Cdd:PLN02293 154 EVVECACVIELPELKGREKLNGK 176
 
Name Accession Description Interval E-value
PLN02293 PLN02293
adenine phosphoribosyltransferase
 7-189 1.67e-45

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 150.21  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     7 PNSFLLDDSHALSQLLKKSYRWYsPVFSPRNVpRFADVSSITESPETLKAIRDFLVQRYRAMspAPTHILGFDARGFLFG 86
Cdd:PLN02293   2 FAMENGDQGDPRLQGISSAIRVV-PDFPKPGI-MFQDITTLLLDPKAFKDTIDLFVERYRDM--GISVVAGIEARGFIFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    87 PMIAVELEIPFVLMRKADKNAGLLIrSEPYEKEYkeaAPEVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDA 166
Cdd:PLN02293  78 PPIALAIGAKFVPLRKPGKLPGEVI-SEEYVLEY---GTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGA 153

                        170       180
                 ....*....|....*....|...
gi 5822236   167 VVVEMVSILSIPFLKAAEKIHST 189
Cdd:PLN02293 154 EVVECACVIELPELKGREKLNGK 176
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 36-203 3.82e-33

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: 117.87  E-value: 3.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   36 RNVPR-------FADVSSITESPETLKAIRDFLVQRYRAMSPapTHILGFDARGFLFGPMIAVELEIPFVLMRKADKNAG 108
Cdd:COG0503   8 RDIPDfpkpgilFRDITPLLGDPELFRAAGDELAERFADKGI--DKVVGIEARGFILAAALAYALGVPFVPARKPGKLPG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236  109 LLIrSEPYEKEYKEAApeVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIhs 188
Cdd:COG0503  86 ETV-SEEYDLEYGTGD--TLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL-- 160

                       170
                ....*....|....*
gi 5822236  189 tansryKDIKFISLL 203
Cdd:COG0503 161 ------RDYPVESLL 169
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 59-187 3.29e-18

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 77.82  E-value: 3.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   59 DFLVQRYRAMSPAPTHILGFDARGFLFGPMIAVELEIPFVLMRKadknagllirsEPYEKEYKEAAPEVMTIRYGSIGKG 138
Cdd:cd06223   3 RLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGDVKG 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5822236  139 SRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIH 187
Cdd:cd06223  72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-196 3.35e-14

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: 67.39  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     43 DVSSITESPETLKAIRDFLVQRYRAMSPAPTHILGFDARGFLFGPMIAVELEIPFVLMRKadknagllirsepyEKEYKE 122
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRK--------------VSYNPD 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5822236    123 AAPEVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSIlsipflkaAEKIHSTANSRYKD 196
Cdd:pfam00156  67 TSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVL--------IDKPAGTEPKDKYD 132
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 34-208 2.24e-07

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: 49.35  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     34 SPRNVPRFADVSSITESPETLKAIRdflvqryRAMSPAPTHILGFDArgfLFGPMIAvelEIPF-----VLMRKADKNAG 108
Cdd:TIGR00336  18 SGRKSPYYFNIKLFNTGPELANLIA-------RYAAAIIKSHLEFDV---IAGPALG---GIPIatavsVKLAKPGGDIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    109 LLI-RSEPyeKEYKEAApevmtIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIh 187
Cdd:TIGR00336  85 LCFnRKEA--KDHGEGG-----NIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEF- 156

                         170       180
                  ....*....|....*....|.
gi 5822236    188 stanSRYKDIKFISLLSDDAL 208
Cdd:TIGR00336 157 ----EKEYGLPVISLITLKDL 173
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
21-174 2.63e-06

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 46.45  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    21 LLKKSYRwYSPVFSPRNVPRFadVSSITE-----SPETLKAIRDFLVqryRAMSPAPTHILGFDARGFLFGPMIAVELEI 95
Cdd:NF040646   4 KLKESLK-NAPVVKRGEYNYF--IHPITDgvplvEPELLREIADRII---KIADLDVDKIVTVEAMGIPIATALSLKTDI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    96 PFVLMRKadknagllirsepyeKEYK---EAAPEVMTiRYG-------SIGKGSRVVLIDDVLATGGTALSGLQLVEASD 165
Cdd:NF040646  78 PLVIIRK---------------RKYGlpgEVEVHQST-GYSkgelyinGINKGDRVLIVDDVISTGGTLIAVIKALEKAG 141


                 ....*....
gi 5822236   166 AVVVEMVSI 174
Cdd:NF040646 142 AEIKDVVVV 150
 
Name Accession Description Interval E-value
PLN02293 PLN02293
adenine phosphoribosyltransferase
 7-189 1.67e-45

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 150.21  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     7 PNSFLLDDSHALSQLLKKSYRWYsPVFSPRNVpRFADVSSITESPETLKAIRDFLVQRYRAMspAPTHILGFDARGFLFG 86
Cdd:PLN02293   2 FAMENGDQGDPRLQGISSAIRVV-PDFPKPGI-MFQDITTLLLDPKAFKDTIDLFVERYRDM--GISVVAGIEARGFIFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    87 PMIAVELEIPFVLMRKADKNAGLLIrSEPYEKEYkeaAPEVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDA 166
Cdd:PLN02293  78 PPIALAIGAKFVPLRKPGKLPGEVI-SEEYVLEY---GTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGA 153

                        170       180
                 ....*....|....*....|...
gi 5822236   167 VVVEMVSILSIPFLKAAEKIHST 189
Cdd:PLN02293 154 EVVECACVIELPELKGREKLNGK 176
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 19-204 8.62e-36

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 124.80  E-value: 8.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    19 SQLLKKSYRWYsPVFsPRNVPRFADVSSITESPETLKAIRDFLVQRYRAMSPapTHILGFDARGFLFGPMIAVELEIPFV 98
Cdd:PRK02304   3 LEDLKSSIRTI-PDF-PKPGILFRDITPLLADPEAFREVIDALVERYKDADI--DKIVGIEARGFIFGAALAYKLGIGFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    99 LMRKADKnagLL--IRSEPYEKEYKEAapeVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILS 176
Cdd:PRK02304  79 PVRKPGK---LPreTISESYELEYGTD---TLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIE 152

                        170       180
                 ....*....|....*....|....*...
gi 5822236   177 IPFLKAAEKIhstansryKDIKFISLLS 204
Cdd:PRK02304 153 LPDLGGREKL--------EGYPVKSLVK 172
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 36-203 3.82e-33

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: 117.87  E-value: 3.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   36 RNVPR-------FADVSSITESPETLKAIRDFLVQRYRAMSPapTHILGFDARGFLFGPMIAVELEIPFVLMRKADKNAG 108
Cdd:COG0503   8 RDIPDfpkpgilFRDITPLLGDPELFRAAGDELAERFADKGI--DKVVGIEARGFILAAALAYALGVPFVPARKPGKLPG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236  109 LLIrSEPYEKEYKEAApeVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIhs 188
Cdd:COG0503  86 ETV-SEEYDLEYGTGD--TLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL-- 160

                       170
                ....*....|....*
gi 5822236  189 tansryKDIKFISLL 203
Cdd:COG0503 161 ------RDYPVESLL 169
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 59-187 3.29e-18

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 77.82  E-value: 3.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   59 DFLVQRYRAMSPAPTHILGFDARGFLFGPMIAVELEIPFVLMRKadknagllirsEPYEKEYKEAAPEVMTIRYGSIGKG 138
Cdd:cd06223   3 RLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRK-----------ERKGPGRTPSEPYGLELPLGGDVKG 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5822236  139 SRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIH 187
Cdd:cd06223  72 KRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-196 3.35e-14

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: 67.39  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     43 DVSSITESPETLKAIRDFLVQRYRAMSPAPTHILGFDARGFLFGPMIAVELEIPFVLMRKadknagllirsepyEKEYKE 122
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRK--------------VSYNPD 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5822236    123 AAPEVMTIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSIlsipflkaAEKIHSTANSRYKD 196
Cdd:pfam00156  67 TSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVL--------IDKPAGTEPKDKYD 132
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 39-175 5.32e-13

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 65.56  E-value: 5.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   39 PRFADVSSITESPETLKAIRDFLVQRYRAmspaptHILGFDArgfLFGP---------MIAVELEIPFVLMRKADKNAGL 109
Cdd:COG0461  31 PYYIDCRLVLSYPEALELLGEALAELIKE------LGPEFDA---VAGPatggiplaaAVARALGLPAIFVRKEAKDHGT 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5822236  110 --LIRsepyekeykeaapevmtiryGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSIL 175
Cdd:COG0461 102 ggQIE--------------------GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIV 149
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 75-205 1.78e-10

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 58.26  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    75 ILGFDARGFLFGPMIAVeleIPFVLMRKADK---------NAGLLIRSEPYEKEykeaapevmtIRYGSIGKGSRVVLID 145
Cdd:PRK12560  55 IVTEEDKGAPLATPVSL---LSGKPLAMARWypyslselnYNVVEIGSEYFEGV----------VYLNGIEKGDRVAIID 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   146 DVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIHSTANSRYKDIKFISLLSD 205
Cdd:PRK12560 122 DTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRKKLFTQTGINVKSLVKIDVKPH 181
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 39-211 5.73e-10

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 57.09  E-value: 5.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    39 PRFADVSSITESPETLKAIRDFLVQRYRAmspaptHILGFDArgfLFGP---------MIAVELEIPFVLMRKADKNAGl 109
Cdd:PRK00455  32 PYYFDCRKLLSYPEALALLGRFLAEAIKD------SGIEFDV---VAGPatggiplaaAVARALDLPAIFVRKEAKDHG- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   110 lirsepyEKEYKEaapevmtiryGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSipFLKAAEKIHST 189
Cdd:PRK00455 102 -------EGGQIE----------GRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVD--RQSAAQEVFAD 162

                        170       180
                 ....*....|....*....|..
gi 5822236   190 ANsrykdIKFISLLSDDALTEE 211
Cdd:PRK00455 163 AG-----VPLISLITLDDLLEY 179
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 34-208 2.24e-07

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: 49.35  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236     34 SPRNVPRFADVSSITESPETLKAIRdflvqryRAMSPAPTHILGFDArgfLFGPMIAvelEIPF-----VLMRKADKNAG 108
Cdd:TIGR00336  18 SGRKSPYYFNIKLFNTGPELANLIA-------RYAAAIIKSHLEFDV---IAGPALG---GIPIatavsVKLAKPGGDIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    109 LLI-RSEPyeKEYKEAApevmtIRYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSIPFLKAAEKIh 187
Cdd:TIGR00336  85 LCFnRKEA--KDHGEGG-----NIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEF- 156

                         170       180
                  ....*....|....*....|.
gi 5822236    188 stanSRYKDIKFISLLSDDAL 208
Cdd:TIGR00336 157 ----EKEYGLPVISLITLKDL 173
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
21-174 2.63e-06

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 46.45  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    21 LLKKSYRwYSPVFSPRNVPRFadVSSITE-----SPETLKAIRDFLVqryRAMSPAPTHILGFDARGFLFGPMIAVELEI 95
Cdd:NF040646   4 KLKESLK-NAPVVKRGEYNYF--IHPITDgvplvEPELLREIADRII---KIADLDVDKIVTVEAMGIPIATALSLKTDI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    96 PFVLMRKadknagllirsepyeKEYK---EAAPEVMTiRYG-------SIGKGSRVVLIDDVLATGGTALSGLQLVEASD 165
Cdd:NF040646  78 PLVIIRK---------------RKYGlpgEVEVHQST-GYSkgelyinGINKGDRVLIVDDVISTGGTLIAVIKALEKAG 141


                 ....*....
gi 5822236   166 AVVVEMVSI 174
Cdd:NF040646 142 AEIKDVVVV 150
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 50-172 8.38e-05

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 42.43  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    50 SPETLKAIRDFLVQRYRAMSPAPthILGFDARGFLFGPMIAVELE----IPFVLMRKADKNAGLlirSEPYEKEYKEAAP 125
Cdd:PRK06031  65 SFEVLDALAEHLAEKARAFDPDV--VAGLPTLGLTLAAAVARKLGhtryVPLGTSRKFWYRDEL---SVPLSSITTPDQG 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 5822236   126 EVMTI--RYGSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMV 172
Cdd:PRK06031 140 KRLYIdpRMLPLLEGRRVALIDDVISSGASIVAGLRLLAACGIEPAGIG 188
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 137-175 1.16e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.50  E-value: 1.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 5822236   137 KGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSIL 175
Cdd:PRK07322 119 KGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAIF 157
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 41-177 4.55e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 40.36  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    41 FADVSSITESPETLKAIRDFLVQRYraMSPAPTHILGFDARGFLFGPMIAVELEIPFVLMRKAdKNAGLlirsEPYEKEY 120
Cdd:PRK08558  83 YVDNSSVVFDPSFLRLIAPVVAERF--MGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKS-KETGV----EKFYEEY 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236   121 KEAAPEVMTIRY---GSIGKGSRVVLIDDVLATGGTALSGLQLVEASDAVVVEMVSILSI 177
Cdd:PRK08558 156 QRLASGIEVTLYlpaSALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAV 215
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 118-222 1.43e-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: 38.63  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5822236    118 KEYKEAAPEVMTIRYgsigkgsrVVLIDDVLATGGTALSGLQ-LVEASdaVVVEMVSILSIpfLKAAEKIHsTANSRYKD 196
Cdd:pfam14681 106 VEYYNKLPKDISDRT--------VILLDPMLATGGSAIAAIQvLREHG--VPEENIVVLSV--IAAPEGLH-RLAAAFPD 172

                          90       100
                  ....*....|....*....|....*.
gi 5822236    197 IKFISLLSDDALTEencgdsKNYTGP 222
Cdd:pfam14681 173 VKIVTAAVDEELNE------NGYIVP 192
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH