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Conserved domains on  [gi|1214907123|ref|WP_088917129|]
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phosphoribosyltransferase [Granulosicoccus antarcticus]

Protein Classification

phosphoribosyltransferase( domain architecture ID 10006200)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 25-193 2.92e-43

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: 142.68  E-value: 2.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  25 EKHYVTETDLLQDAYRLGVQIAESGFRPTFIVGLWRGGSVVGIAVQECLQYIGIPTdhiaIRT-SYRGlasyqqmVDNPE 103
Cdd:COG2236     5 KKEYLSWDEIHELSRRLAEQILESGFRPDVIVAIARGGLVPARILADALGVPDLAS----IRVsSYTG-------TAKRL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123 104 TEIRIHGTqylLDTLDRDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPahnRTTLKPDYYVNTSDD 183
Cdd:COG2236    74 EEPVVKGP---LDEDLAGKRVLIVDDVADTGRTLEAVR----DLLKEAGPAEVRTAVLYYKP---SSKFKPDYYAEETDA 143

                         170
                  ....*....|
gi 1214907123 184 WLVMPYELSG 193
Cdd:COG2236   144 WIVFPWELDE 153
 
Name Accession Description Interval E-value
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 25-193 2.92e-43

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: 142.68  E-value: 2.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  25 EKHYVTETDLLQDAYRLGVQIAESGFRPTFIVGLWRGGSVVGIAVQECLQYIGIPTdhiaIRT-SYRGlasyqqmVDNPE 103
Cdd:COG2236     5 KKEYLSWDEIHELSRRLAEQILESGFRPDVIVAIARGGLVPARILADALGVPDLAS----IRVsSYTG-------TAKRL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123 104 TEIRIHGTqylLDTLDRDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPahnRTTLKPDYYVNTSDD 183
Cdd:COG2236    74 EEPVVKGP---LDEDLAGKRVLIVDDVADTGRTLEAVR----DLLKEAGPAEVRTAVLYYKP---SSKFKPDYYAEETDA 143

                         170
                  ....*....|
gi 1214907123 184 WLVMPYELSG 193
Cdd:COG2236   144 WIVFPWELDE 153
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 40-180 3.12e-10

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: 55.86  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  40 RLGVQIAESGFRPTFIVGLWRGGSVVGIAVQECLqyiGIPTDHIAIRTSYRGlasyqqmvdnpETEIRIHGTQYLLDTLD 119
Cdd:cd06223     4 LLAEEIREDLLEPDVVVGILRGGLPLAAALARAL---GLPLAFIRKERKGPG-----------RTPSEPYGLELPLGGDV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214907123 120 RDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPAHNRTTLK----PDYYVNT 180
Cdd:cd06223    70 KGKRVLLVDDVIATGGTLLAAI----ELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 34-184 9.33e-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: 52.37  E-value: 9.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  34 LLQDAYRLGVQIAES-GFRPTFIVGLWRGGSVVGIAVqecLQYIGIPTDhIAIRTSYRGlasyqqmvDNPETEIRIHGTQ 112
Cdd:pfam00156  11 ILKAVARLAAQINEDyGGKPDVVVGILRGGLPFAGIL---ARRLDVPLA-FVRKVSYNP--------DTSEVMKTSSALP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1214907123 113 YLldtldRDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPAhnrTTLKPDYYVNTSDDW 184
Cdd:pfam00156  79 DL-----KGKTVLIVDDILDTGGTLLKVL----ELLKNVGPKEVKIAVLIDKPA---GTEPKDKYDKRVDDW 138
 
Name Accession Description Interval E-value
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 25-193 2.92e-43

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: 142.68  E-value: 2.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  25 EKHYVTETDLLQDAYRLGVQIAESGFRPTFIVGLWRGGSVVGIAVQECLQYIGIPTdhiaIRT-SYRGlasyqqmVDNPE 103
Cdd:COG2236     5 KKEYLSWDEIHELSRRLAEQILESGFRPDVIVAIARGGLVPARILADALGVPDLAS----IRVsSYTG-------TAKRL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123 104 TEIRIHGTqylLDTLDRDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPahnRTTLKPDYYVNTSDD 183
Cdd:COG2236    74 EEPVVKGP---LDEDLAGKRVLIVDDVADTGRTLEAVR----DLLKEAGPAEVRTAVLYYKP---SSKFKPDYYAEETDA 143

                         170
                  ....*....|
gi 1214907123 184 WLVMPYELSG 193
Cdd:COG2236   144 WIVFPWELDE 153
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 40-180 3.12e-10

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: 55.86  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  40 RLGVQIAESGFRPTFIVGLWRGGSVVGIAVQECLqyiGIPTDHIAIRTSYRGlasyqqmvdnpETEIRIHGTQYLLDTLD 119
Cdd:cd06223     4 LLAEEIREDLLEPDVVVGILRGGLPLAAALARAL---GLPLAFIRKERKGPG-----------RTPSEPYGLELPLGGDV 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214907123 120 RDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPAHNRTTLK----PDYYVNT 180
Cdd:cd06223    70 KGKRVLLVDDVIATGGTLLAAI----ELLKEAGAKVVGVAVLLDKPEGGARELAspgdPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 34-184 9.33e-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: 52.37  E-value: 9.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  34 LLQDAYRLGVQIAES-GFRPTFIVGLWRGGSVVGIAVqecLQYIGIPTDhIAIRTSYRGlasyqqmvDNPETEIRIHGTQ 112
Cdd:pfam00156  11 ILKAVARLAAQINEDyGGKPDVVVGILRGGLPFAGIL---ARRLDVPLA-FVRKVSYNP--------DTSEVMKTSSALP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1214907123 113 YLldtldRDDSLLIVDDVFSSGLTSSAVIsrltSRLKNNMPSDVRIAVPWYKPAhnrTTLKPDYYVNTSDDW 184
Cdd:pfam00156  79 DL-----KGKTVLIVDDILDTGGTLLKVL----ELLKNVGPKEVKIAVLIDKPA---GTEPKDKYDKRVDDW 138
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 40-176 1.74e-04

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 40.78  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214907123  40 RLGVQIAE--SGFRPTFIVGLwrGGSVVGIAvqECLQYIGIPT--DHIAIrTSYR-GLASYQQM--VDNPETEIRihgtq 112
Cdd:COG0634    21 ELAAQITAdyAGKEPLVVGVL--KGAFVFMA--DLLRALDFPLeiDFMHV-SSYGgGTESSGEVriLKDLDEDIE----- 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1214907123 113 ylldtlDRDdsLLIVDDVFSSGLTSSAVISRLTSRlknnMPSDVRIAVPWYKPAHNRTTLKPDY 176
Cdd:COG0634    91 ------GRD--VLIVEDIIDTGLTLSYLLELLKSR----GPASVKIATLLDKPERRKVDVPADY 142
 
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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