NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490320761|ref|WP_004210246|]
View 

MULTISPECIES: phosphoribosyltransferase domain-containing protein [Enterobacteriaceae]

Protein Classification

phosphoribosyltransferase domain-containing protein( domain architecture ID 10634760)

phosphoribosyltransferase domain-containing protein may catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
33-220 1.61e-81

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


:

Pssm-ID: 434809  Cd Length: 189  Bit Score: 247.08  E-value: 1.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761   33 LFDIAERRNPKRAFLFVSKVLGRHIPVSPLVMRNVYTQLAEKFPGT---LDGPVVFIGMAETAVGLGAGVFDEVRkhhPD 109
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELradLPGPVLVIGFAETATGLGHGVADALA---GD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  110 CVYLTSTRHPV-DAELLCEFKEEHSHATDHLIYypvsAAMRKTVAEAQTLVLVDDEATTGKTFLNLLASLRAsgALRKvR 188
Cdd:pfam15609  78 ALYLHTTRRPVpGVPPLLEFEEEHSHATDHLLY----PEDRALLAGARPLVLVDDEISTGNTALNLIRALHA--KLPR-K 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490320761  189 RVIAVTLTDWSG-------EALSQNSPLPLHTVSLISGN 220
Cdd:pfam15609 151 RYVVVSLVDWRSpedraafAALAAELGIPIDVVSLLEGT 189
TRSP super family cl13881
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
274-370 1.76e-27

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


The actual alignment was detected with superfamily member pfam12500:

Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 104.97  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  274 GENILVLGTGEFVWEPFLLAERLEAAGaqVVFSSTTRSPIST----GYAIQSAIAFSDNYGLGIPNYVYNVAHQQFDRIL 349
Cdd:pfam12500  32 GERVLVLGTEEFMYIPLRIAAALGDGD--VRYQSTTRSPVLPvddpGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVV 109
                          90       100
                  ....*....|....*....|.
gi 490320761  350 ICCETPassVDPRLLEALSAV 370
Cdd:pfam12500 110 LVVERP---VDTEALGGLLDA 127
 
Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
33-220 1.61e-81

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434809  Cd Length: 189  Bit Score: 247.08  E-value: 1.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761   33 LFDIAERRNPKRAFLFVSKVLGRHIPVSPLVMRNVYTQLAEKFPGT---LDGPVVFIGMAETAVGLGAGVFDEVRkhhPD 109
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELradLPGPVLVIGFAETATGLGHGVADALA---GD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  110 CVYLTSTRHPV-DAELLCEFKEEHSHATDHLIYypvsAAMRKTVAEAQTLVLVDDEATTGKTFLNLLASLRAsgALRKvR 188
Cdd:pfam15609  78 ALYLHTTRRPVpGVPPLLEFEEEHSHATDHLLY----PEDRALLAGARPLVLVDDEISTGNTALNLIRALHA--KLPR-K 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490320761  189 RVIAVTLTDWSG-------EALSQNSPLPLHTVSLISGN 220
Cdd:pfam15609 151 RYVVVSLVDWRSpedraafAALAAELGIPIDVVSLLEGT 189
TRSP pfam12500
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
274-370 1.76e-27

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 104.97  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  274 GENILVLGTGEFVWEPFLLAERLEAAGaqVVFSSTTRSPIST----GYAIQSAIAFSDNYGLGIPNYVYNVAHQQFDRIL 349
Cdd:pfam12500  32 GERVLVLGTEEFMYIPLRIAAALGDGD--VRYQSTTRSPVLPvddpGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVV 109
                          90       100
                  ....*....|....*....|.
gi 490320761  350 ICCETPassVDPRLLEALSAV 370
Cdd:pfam12500 110 LVVERP---VDTEALGGLLDA 127
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
70-208 1.17e-06

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: 47.39  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  70 QLAEKFPGTLDGPVVFIGMAETAVGLGAGVFDEVRKhhpDCVYLtstrhpvdaellceFKEEHSHATDHLIYYPVSAAMR 149
Cdd:cd06223    4 LLAEEIREDLLEPDVVVGILRGGLPLAAALARALGL---PLAFI--------------RKERKGPGRTPSEPYGLELPLG 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490320761 150 KTVAEaQTLVLVDDEATTGKTFLNLLASLRASGAlRKVRrvIAVTLTDWSGEALSQNSP 208
Cdd:cd06223   67 GDVKG-KRVLLVDDVIATGGTLLAAIELLKEAGA-KVVG--VAVLLDKPEGGARELASP 121
 
Name Accession Description Interval E-value
PRTase_2 pfam15609
Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to ...
33-220 1.61e-81

Phosphoribosyl transferase; This PRTase family, and C-terminal TRSP domain, are related to OPRTases, and are predicted to use Orotate as substrate. These genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434809  Cd Length: 189  Bit Score: 247.08  E-value: 1.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761   33 LFDIAERRNPKRAFLFVSKVLGRHIPVSPLVMRNVYTQLAEKFPGT---LDGPVVFIGMAETAVGLGAGVFDEVRkhhPD 109
Cdd:pfam15609   1 LFGLAARRNPKRAFLFVSKVLGKHIPVRPSVMRDAGRLLAARVPELradLPGPVLVIGFAETATGLGHGVADALA---GD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  110 CVYLTSTRHPV-DAELLCEFKEEHSHATDHLIYypvsAAMRKTVAEAQTLVLVDDEATTGKTFLNLLASLRAsgALRKvR 188
Cdd:pfam15609  78 ALYLHTTRRPVpGVPPLLEFEEEHSHATDHLLY----PEDRALLAGARPLVLVDDEISTGNTALNLIRALHA--KLPR-K 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490320761  189 RVIAVTLTDWSG-------EALSQNSPLPLHTVSLISGN 220
Cdd:pfam15609 151 RYVVVSLVDWRSpedraafAALAAELGIPIDVVSLLEGT 189
TRSP pfam12500
TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly ...
274-370 1.76e-27

TRSP domain C terminus to PRTase_2; This domain occurs C-terminal to PRTase_2 and has highly conserved GXXE and TRSP signatures. It is found in bacteria. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 463612 [Multi-domain]  Cd Length: 128  Bit Score: 104.97  E-value: 1.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  274 GENILVLGTGEFVWEPFLLAERLEAAGaqVVFSSTTRSPIST----GYAIQSAIAFSDNYGLGIPNYVYNVAHQQFDRIL 349
Cdd:pfam12500  32 GERVLVLGTEEFMYIPLRIAAALGDGD--VRYQSTTRSPVLPvddpGYAIRTAFTFPSPDDPGIVNYVYNIPPGGYDEVV 109
                          90       100
                  ....*....|....*....|.
gi 490320761  350 ICCETPassVDPRLLEALSAV 370
Cdd:pfam12500 110 LVVERP---VDTEALGGLLDA 127
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
70-208 1.17e-06

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: 47.39  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490320761  70 QLAEKFPGTLDGPVVFIGMAETAVGLGAGVFDEVRKhhpDCVYLtstrhpvdaellceFKEEHSHATDHLIYYPVSAAMR 149
Cdd:cd06223    4 LLAEEIREDLLEPDVVVGILRGGLPLAAALARALGL---PLAFI--------------RKERKGPGRTPSEPYGLELPLG 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490320761 150 KTVAEaQTLVLVDDEATTGKTFLNLLASLRASGAlRKVRrvIAVTLTDWSGEALSQNSP 208
Cdd:cd06223   67 GDVKG-KRVLLVDDVIATGGTLLAAIELLKEAGA-KVVG--VAVLLDKPEGGARELASP 121
 
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