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Conserved domains on  [gi|1002983264|ref|WP_061427934|]
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MULTISPECIES: orotate phosphoribosyltransferase [Clostridium]

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

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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 1.77e-81

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 TIGR01367:

Pssm-ID: 444823  Cd Length: 187  Bit Score: 239.69  E-value: 1.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   7 MVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAYELGRQL 84
Cdd:TIGR01367   1 DVLDIYKQAGALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDygLKVDFIVGPAMGGVILGYEVARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  85 GKPAIFTERENGEMTLRRGFTIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVTDF--PMYSSI 162
Cdd:TIGR01367  81 SVRSIFAEREGGGMKLRRGFAVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGKPDSgvPLMSLK 160

                         170       180
                  ....*....|....*....|....*..
gi 1002983264 163 KLDIESFEAENCPLCKEGVPYIKPGSR 189
Cdd:TIGR01367 161 ELEFPTYDSHECPLCLAGIPAEKPGSR 187
 
Name Accession Description Interval E-value
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 7-189 1.77e-81

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: 239.69  E-value: 1.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   7 MVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAYELGRQL 84
Cdd:TIGR01367   1 DVLDIYKQAGALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDygLKVDFIVGPAMGGVILGYEVARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  85 GKPAIFTERENGEMTLRRGFTIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVTDF--PMYSSI 162
Cdd:TIGR01367  81 SVRSIFAEREGGGMKLRRGFAVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGKPDSgvPLMSLK 160

                         170       180
                  ....*....|....*....|....*..
gi 1002983264 163 KLDIESFEAENCPLCKEGVPYIKPGSR 189
Cdd:TIGR01367 161 ELEFPTYDSHECPLCLAGIPAEKPGSR 187
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 1-192 5.18e-76

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 226.58  E-value: 5.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   1 MKNTDAMVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAY 78
Cdd:PRK00455    1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDsgIEFDVVAGPATGGIPLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  79 ELGRQLGKPAIFTERE------NGEMTLRRGFtiekGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPG- 151
Cdd:PRK00455   81 AVARALDLPAIFVRKEakdhgeGGQIEGRRLF----GKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAa 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002983264 152 ----NVTDFPMYSSIKLDIESFEAENCPLCKEGVPYIKPGSRNIK 192
Cdd:PRK00455  157 qevfADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYG 201
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 2-165 1.59e-62

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 192.29  E-value: 1.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   2 KNTDAMVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAYE 79
Cdd:COG0461     1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKElgPEFDAVAGPATGGIPLAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  80 LGRQLGKPAIFTERE---NGEMTLRRGFtIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVTDF 156
Cdd:COG0461    81 VARALGLPAIFVRKEakdHGTGGQIEGG-LLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENL 159

                         170
                  ....*....|....
gi 1002983264 157 -----PMYSSIKLD 165
Cdd:COG0461   160 eeagvPLHSLLTLD 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-152 4.47e-20

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: 81.29  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  50 VLKVVADQLKD--IDFDLVVGPAMGGVIVAYELGRQLGKPAIFTERENGEMTLRRGFTIE---------KGQKVVITEDV 118
Cdd:cd06223     1 AGRLLAEEIREdlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGlelplggdvKGKRVLLVDDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002983264 119 VTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGN 152
Cdd:cd06223    81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG 114
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 39-148 9.04e-15

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: 68.16  E-value: 9.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  39 QLLKHPEKAEKVLKVVADQLKDIDF--DLVVGPAMGGVIVAYELGRQLGKP------AIFTERENGEMTLRRGFTIEKGQ 110
Cdd:pfam00156   4 EILDNPAILKAVARLAAQINEDYGGkpDVVVGILRGGLPFAGILARRLDVPlafvrkVSYNPDTSEVMKTSSALPDLKGK 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002983264 111 KVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDR 148
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
 
Name Accession Description Interval E-value
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 7-189 1.77e-81

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: 239.69  E-value: 1.77e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   7 MVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAYELGRQL 84
Cdd:TIGR01367   1 DVLDIYKQAGALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDygLKVDFIVGPAMGGVILGYEVARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  85 GKPAIFTERENGEMTLRRGFTIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVTDF--PMYSSI 162
Cdd:TIGR01367  81 SVRSIFAEREGGGMKLRRGFAVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGKPDSgvPLMSLK 160

                         170       180
                  ....*....|....*....|....*..
gi 1002983264 163 KLDIESFEAENCPLCKEGVPYIKPGSR 189
Cdd:TIGR01367 161 ELEFPTYDSHECPLCLAGIPAEKPGSR 187
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 1-192 5.18e-76

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 226.58  E-value: 5.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   1 MKNTDAMVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAY 78
Cdd:PRK00455    1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDsgIEFDVVAGPATGGIPLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  79 ELGRQLGKPAIFTERE------NGEMTLRRGFtiekGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPG- 151
Cdd:PRK00455   81 AVARALDLPAIFVRKEakdhgeGGQIEGRRLF----GKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAa 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002983264 152 ----NVTDFPMYSSIKLDIESFEAENCPLCKEGVPYIKPGSRNIK 192
Cdd:PRK00455  157 qevfADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYG 201
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 2-165 1.59e-62

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 192.29  E-value: 1.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   2 KNTDAMVIDTLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD--IDFDLVVGPAMGGVIVAYE 79
Cdd:COG0461     1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKElgPEFDAVAGPATGGIPLAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  80 LGRQLGKPAIFTERE---NGEMTLRRGFtIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVTDF 156
Cdd:COG0461    81 VARALGLPAIFVRKEakdHGTGGQIEGG-LLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENL 159

                         170
                  ....*....|....
gi 1002983264 157 -----PMYSSIKLD 165
Cdd:COG0461   160 eeagvPLHSLLTLD 173
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 12-148 1.43e-24

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: 94.42  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  12 LKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKD-IDFDLVVGPAMGGVIVAYELGRQLGKP--- 87
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKShLEFDVIAGPALGGIPIATAVSVKLAKPggd 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002983264  88 --AIFTERE---NGEMTLRRGfTIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDR 148
Cdd:TIGR00336  83 ipLCFNRKEakdHGEGGNIEG-ELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDR 147
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-152 4.47e-20

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: 81.29  E-value: 4.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  50 VLKVVADQLKD--IDFDLVVGPAMGGVIVAYELGRQLGKPAIFTERENGEMTLRRGFTIE---------KGQKVVITEDV 118
Cdd:cd06223     1 AGRLLAEEIREdlLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGlelplggdvKGKRVLLVDDV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1002983264 119 VTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGN 152
Cdd:cd06223    81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG 114
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 58-163 7.54e-20

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 82.61  E-value: 7.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  58 LKDIDFDLVVGPAMGGV----IVAYELGRQLG----KPAIFTERENGEMTLRRGFTIEKGQKVVITEDVVTTGKSFKEAA 129
Cdd:PRK02277   81 KEDEEVDVVVGIAKSGVplatLVADELGKDLAiyhpKKWDHGEGEKKTGSFSRNFASVEGKRCVIVDDVITSGTTMKETI 160

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002983264 130 KVIEEQGGEVVAVVCIVDRTPGN-VTDFPMYSSIK 163
Cdd:PRK02277  161 EYLKEHGGKPVAVVVLIDKSGIDeIDGVPVYSLIR 195
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 40-147 4.73e-15

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: 69.33  E-value: 4.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  40 LLKHPEKAEKVLKVVADQLKDIDFDLVVGPAMGGVIVAYELGRQLGKPAIF---------------TERENG---EMTLR 101
Cdd:COG0503    26 LLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVParkpgklpgetvseeYDLEYGtgdTLELH 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002983264 102 RGFtIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVD 147
Cdd:COG0503   106 KDA-LKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIE 150
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 39-148 9.04e-15

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: 68.16  E-value: 9.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  39 QLLKHPEKAEKVLKVVADQLKDIDF--DLVVGPAMGGVIVAYELGRQLGKP------AIFTERENGEMTLRRGFTIEKGQ 110
Cdd:pfam00156   4 EILDNPAILKAVARLAAQINEDYGGkpDVVVGILRGGLPFAGILARRLDVPlafvrkVSYNPDTSEVMKTSSALPDLKGK 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1002983264 111 KVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDR 148
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDK 121
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 40-165 1.49e-13

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 65.48  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  40 LLKHPEKAEKVLKVVADQLKDIDFDLVVGP-AMG---GVIVAYELG------RQLGK-P----AIFTERENGEMTL---R 101
Cdd:PRK02304   29 LLADPEAFREVIDALVERYKDADIDKIVGIeARGfifGAALAYKLGigfvpvRKPGKlPretiSESYELEYGTDTLeihK 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002983264 102 RGftIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGN----VTDFPMYSSIKLD 165
Cdd:PRK02304  109 DA--IKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGgrekLEGYPVKSLVKFD 174
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
12-156 1.77e-12

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 64.70  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  12 LKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEKAEKVLKVVADQLKDIDFDLVVGPAMGGVIVAYELGRQLGKPAIFT 91
Cdd:PRK05500  294 LYDIGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNLTFDRIAGIPYGSLPTATGLALHLHHPMIFP 373

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002983264  92 ERENGEMTLRRGF--TIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPGnVTDF 156
Cdd:PRK05500  374 RKEVKAHGTRRLIegNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQG-VKDK 439
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 40-145 5.99e-10

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 55.75  E-value: 5.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  40 LLKHPEKAEKVLKVVADQLKDiDFDLVVGPAMGGVIVAYELGRQLGKPAIFT------------ERENGEMTLRR----- 102
Cdd:PRK07322   31 ILGDTELTEAAAEALAKRLPT-EVDVLVTPETKGIPLAHALSRRLGKPYVVArksrkpymqdpiIQEVVSITTGKpqllv 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002983264 103 --GFTIEK--GQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCI 145
Cdd:PRK07322  110 ldGADAEKlkGKRVAIVDDVVSTGGTLTALERLVERAGGQVVAKAAI 156
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 49-149 5.74e-09

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 53.25  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  49 KVLKVVADQLK---DIDFDLVVGP----AMGGVIVAYELGRQLGKPA---------------IFTERENGEMTLRrgfTI 106
Cdd:PRK12560   35 KVLKETAKEIIkyiDKDIDKIVTEedkgAPLATPVSLLSGKPLAMARwypyslselnynvveIGSEYFEGVVYLN---GI 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1002983264 107 EKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRT 149
Cdd:PRK12560  112 EKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKT 154
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 54-156 8.93e-09

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: 52.16  E-value: 8.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  54 VADQLKD--IDFDLVVGPAMGGVIVAYELGRQLGKPAIFT---------ERENGEMTLRRGFTIE-KGQKVVITEDVVTT 121
Cdd:COG2236    21 LAEQILEsgFRPDVIVAIARGGLVPARILADALGVPDLASirvssytgtAKRLEEPVVKGPLDEDlAGKRVLIVDDVADT 100

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002983264 122 GKSFKEAAKVIEEQGGEVVAVVCIVDRTPGNVT-DF 156
Cdd:COG2236   101 GRTLEAVRDLLKEAGPAEVRTAVLYYKPSSKFKpDY 136
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 108-150 1.10e-05

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 44.04  E-value: 1.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002983264 108 KGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVdRTP 150
Cdd:COG1040   154 AGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVLA-RTP 195
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 1-151 1.94e-05

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 43.67  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264   1 MKNTDAMVIdtLKEVGALLEGHFLLSSGRHSNRYCQCAQLLKHPEkaekVLKVVADQL----KDIDFDLVVGPAMGGVIV 76
Cdd:PRK13809    8 KLRDQAVAI--LYQIGAIKFGKFILASGEETPIYVDMRLVISSPE----VLQTIATLIwrlrPSFNSSLLCGVPYTALTL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002983264  77 AYELGRQLGKPAIFTERENGEMTLRRGFTIE----KGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVDRTPG 151
Cdd:PRK13809   82 ATSISLKYNIPMVLRRKELKNVDPSDAIKVEglftPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKG 160
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 65-142 2.06e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 43.96  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  65 LVVGPAMGGVIVAYELGRQLGKPAIFTERENGEMTLRRGFTIEK--GQKVVITEDVVTTGKSFKEAAKVIEEQGG-EVVA 141
Cdd:PRK02458  172 VVVSPKNSGIKRARSLAEYLDAPIAIIDYAQDDSEREEGYIIGDvaGKKAILIDDILNTGKTFAEAAKIVEREGAtEIYA 251


                  .
gi 1002983264 142 V 142
Cdd:PRK02458  252 V 252
PLN02293 PLN02293
adenine phosphoribosyltransferase
 40-146 6.54e-05

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 41.58  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  40 LLKHPEKAEKVLKVVADQLKDIDFDLVVGPAMGGVI----VAYELG------RQLGK---PAIF----TERENGEMTLRR 102
Cdd:PLN02293   40 LLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIfgppIALAIGakfvplRKPGKlpgEVISeeyvLEYGTDCLEMHV 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002983264 103 GfTIEKGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIV 146
Cdd:PLN02293  120 G-AVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVI 162
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 100-149 1.81e-04

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 40.79  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002983264 100 LRRGFTIE---KGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCIVdRT 149
Cdd:PRK11595  175 LKNAFRLElpvQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQVWCLC-RT 226
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 53-143 8.97e-04

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


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 38.89  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002983264  53 VVADQLKDIDFD--LVVGPAMGGVIVAYELGRQLGKP-AIFTERengemtlRRG-FTIE--------KGQKVVITEDVVT 120
Cdd:COG0462   150 LLADYIKSKDLEdlVVVSPDVGGVKRARAFAKRLGAPlAIIDKR-------RPGaNEVEvmniigdvEGKTCIIVDDMID 222

                          90       100
                  ....*....|....*....|....
gi 1002983264 121 TGKSFKEAAKVIEEQG-GEVVAVV 143
Cdd:COG0462   223 TGGTLVEAAEALKEAGaKSVYAAA 246
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 108-145 5.77e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 36.43  E-value: 5.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002983264 108 KGQKVVITEDVVTTGKSFKEAAKVIEEQGGEVVAVVCI 145
Cdd:PRK00934  203 KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVACV 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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