NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|676330013|gb|AIM38514|]
View 

phosphoribosyltransferase [Sphingobacterium sp. ML3W]

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
PyrR super family cl42780
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
 3-164 3.14e-33

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


The actual alignment was detected with superfamily member COG2065:

Pssm-ID: 441668  Cd Length: 178  Bit Score: 115.92  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   3 SKKTLILDKEQIKQKSIRIAYQILEDNFEEDTLVLVGIADRGYVFAQRLQKILAEISDKNIEL--LKVTM------NKTS 74
Cdd:COG2065    1 KKKKEILDAADIDRALTRIAHEIIERNKGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVgsLDITLyrddlrRRPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  75 RSLKAETDYPIEtVKNKTLILVDDVLNSGRT--------LAYGLgvflnvPiKKMRTAVLIDRSHPKFPIVSDYYGLKLS 146
Cdd:COG2065   81 RPVVNETEIPFD-IDGKTVVLVDDVLYTGRTvraaldalMDFGR------P-AKIQLAVLVDRGHRELPIRADYVGKNVP 152

                        170
                 ....*....|....*...
gi 676330013 147 TILKEHVEVNLEGFEAED 164
Cdd:COG2065  153 TSRSERVEVRLKEIDGED 170
 
Name Accession Description Interval E-value
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
 3-164 3.14e-33

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441668  Cd Length: 178  Bit Score: 115.92  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   3 SKKTLILDKEQIKQKSIRIAYQILEDNFEEDTLVLVGIADRGYVFAQRLQKILAEISDKNIEL--LKVTM------NKTS 74
Cdd:COG2065    1 KKKKEILDAADIDRALTRIAHEIIERNKGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVgsLDITLyrddlrRRPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  75 RSLKAETDYPIEtVKNKTLILVDDVLNSGRT--------LAYGLgvflnvPiKKMRTAVLIDRSHPKFPIVSDYYGLKLS 146
Cdd:COG2065   81 RPVVNETEIPFD-IDGKTVVLVDDVLYTGRTvraaldalMDFGR------P-AKIQLAVLVDRGHRELPIRADYVGKNVP 152

                        170
                 ....*....|....*...
gi 676330013 147 TILKEHVEVNLEGFEAED 164
Cdd:COG2065  153 TSRSERVEVRLKEIDGED 170
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
4-164 4.39e-29

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 105.21  E-value: 4.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   4 KKTLILDKEQIKQKSIRIAYQILEDNFEEDTLVLVGIADRGYVFAQRLQKILAEISDKNIEL--LKVTM------NKTSR 75
Cdd:PRK05205   2 MKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGIKTRGVWLAERLAERLEQLEGVDVPVgeLDITLyrddltKKGLH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  76 SLKAETDYPIEtVKNKTLILVDDVLNSGRT--------LAYGLgvflnvPiKKMRTAVLIDRSHPKFPIVSDYYGLKLST 147
Cdd:PRK05205  82 PQVKPTDIPFD-IEGKRVILVDDVLYTGRTiraaldalFDYGR------P-ARVQLAVLVDRGHRELPIRADYVGKNIPT 153

                        170
                 ....*....|....*..
gi 676330013 148 ILKEHVEVNLEGFEAED 164
Cdd:PRK05205 154 SRDERVVVRLAEVDGRD 170
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 8-144 1.56e-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: 67.00  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013    8 ILDKEQIKQKSIRIAYQILEDNFEEDTlVLVGIADRGYVFAQRLQKILaeisdkniELLKVTMNKTSR----SLKAETDY 83
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPD-VVVGILRGGLPFAGILARRL--------DVPLAFVRKVSYnpdtSEVMKTSS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 676330013   84 PIETVKNKTLILVDDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHPKFPIVSDYYGLK 144
Cdd:pfam00156  76 ALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVD 136
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-144 1.92e-12

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: 60.87  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  20 RIAYQILEDNFEEDtlVLVGIADRGYVFAQrlqkILAEISDKNIELLKVT---MNKTSRSLKAETDYPIETVKNKTLILV 96
Cdd:cd06223    4 LLAEEIREDLLEPD--VVVGILRGGLPLAA----ALARALGLPLAFIRKErkgPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 676330013  97 DDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHP-----KFPIVSDYYGLK 144
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgarelASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PyrR COG2065
Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide ...
 3-164 3.14e-33

Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase [Nucleotide transport and metabolism]; Pyrimidine operon attenuation protein PyrR/uracil phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 441668  Cd Length: 178  Bit Score: 115.92  E-value: 3.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   3 SKKTLILDKEQIKQKSIRIAYQILEDNFEEDTLVLVGIADRGYVFAQRLQKILAEISDKNIEL--LKVTM------NKTS 74
Cdd:COG2065    1 KKKKEILDAADIDRALTRIAHEIIERNKGLEDLVLVGIQTRGVPLAERLAERIEEIEGVKVPVgsLDITLyrddlrRRPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  75 RSLKAETDYPIEtVKNKTLILVDDVLNSGRT--------LAYGLgvflnvPiKKMRTAVLIDRSHPKFPIVSDYYGLKLS 146
Cdd:COG2065   81 RPVVNETEIPFD-IDGKTVVLVDDVLYTGRTvraaldalMDFGR------P-AKIQLAVLVDRGHRELPIRADYVGKNVP 152

                        170
                 ....*....|....*...
gi 676330013 147 TILKEHVEVNLEGFEAED 164
Cdd:COG2065  153 TSRSERVEVRLKEIDGED 170
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
4-164 4.39e-29

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 105.21  E-value: 4.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   4 KKTLILDKEQIKQKSIRIAYQILEDNFEEDTLVLVGIADRGYVFAQRLQKILAEISDKNIEL--LKVTM------NKTSR 75
Cdd:PRK05205   2 MKKEILDAEALRRALTRIAHEIIERNKGLDNLVLVGIKTRGVWLAERLAERLEQLEGVDVPVgeLDITLyrddltKKGLH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  76 SLKAETDYPIEtVKNKTLILVDDVLNSGRT--------LAYGLgvflnvPiKKMRTAVLIDRSHPKFPIVSDYYGLKLST 147
Cdd:PRK05205  82 PQVKPTDIPFD-IEGKRVILVDDVLYTGRTiraaldalFDYGR------P-ARVQLAVLVDRGHRELPIRADYVGKNIPT 153

                        170
                 ....*....|....*..
gi 676330013 148 ILKEHVEVNLEGFEAED 164
Cdd:PRK05205 154 SRDERVVVRLAEVDGRD 170
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 1-147 6.02e-16

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: 70.65  E-value: 6.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   1 MSSKKTLILDKEQIKQKSIRIAYQILEDNFEEDtlVLVGIADRGYVFAqrlqKILAEISD-KNIELLKV----TMNKTSR 75
Cdd:COG2236    1 MDKFKKEYLSWDEIHELSRRLAEQILESGFRPD--VIVAIARGGLVPA----RILADALGvPDLASIRVssytGTAKRLE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 676330013  76 slKAETDYPI-ETVKNKTLILVDDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHPKFpiVSDYYGLKLST 147
Cdd:COG2236   75 --EPVVKGPLdEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSKF--KPDYYAEETDA 143
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 8-144 1.56e-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: 67.00  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013    8 ILDKEQIKQKSIRIAYQILEDNFEEDTlVLVGIADRGYVFAQRLQKILaeisdkniELLKVTMNKTSR----SLKAETDY 83
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPD-VVVGILRGGLPFAGILARRL--------DVPLAFVRKVSYnpdtSEVMKTSS 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 676330013   84 PIETVKNKTLILVDDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHPKFPIVSDYYGLK 144
Cdd:pfam00156  76 ALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVD 136
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-144 1.92e-12

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: 60.87  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013  20 RIAYQILEDNFEEDtlVLVGIADRGYVFAQrlqkILAEISDKNIELLKVT---MNKTSRSLKAETDYPIETVKNKTLILV 96
Cdd:cd06223    4 LLAEEIREDLLEPD--VVVGILRGGLPLAA----ALARALGLPLAFIRKErkgPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 676330013  97 DDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHP-----KFPIVSDYYGLK 144
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgarelASPGDPVYSLFT 130
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 4-143 5.54e-09

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: 52.34  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   4 KKTLILDKEQIKQKSIRIAYQILEDnFEEDTLVLVGIADRGYVFAQRLQKilaEIS-DKNIELLKVT--MNKTSRSLKAE 80
Cdd:COG0634    5 IAEVLISEEEIQARVKELAAQITAD-YAGKEPLVVGVLKGAFVFMADLLR---ALDfPLEIDFMHVSsyGGGTESSGEVR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 676330013  81 TDYPIET-VKNKTLILVDDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHP-KFPIVSDYYGL 143
Cdd:COG0634   81 ILKDLDEdIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERrKVDVPADYVGF 145
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 83-143 4.02e-05

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 41.77  E-value: 4.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 676330013  83 YPIETVKNKTLILVDDVLNSGRTLAYGLGVFLNVPIKKMRTAVLIDRSHPKF--PIVSDYYGL 143
Cdd:PRK09162  90 KPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKakPLKADFVGL 152
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 7-107 2.24e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 36.94  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676330013   7 LILDKEQIKQKSIRIAYQILEDnFEEDTLVLVGIADRGYVFAQRLqkiLAEISDKN----IELLKVT--MNKTSRSLKAE 80
Cdd:PLN02238  10 VLWTAEDISARVAELAAQIASD-YAGKSPVVLGVATGAFMFLADL---VRAIQPLPrgltVDFIRASsyGGGTESSGVAK 85

                         90       100
                 ....*....|....*....|....*....
gi 676330013  81 TDYPI--ETVKNKTLILVDDVLNSGRTLA 107
Cdd:PLN02238  86 VSGADlkIDVKGKHVLLVEDIVDTGNTLS 114
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 55-107 7.67e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 35.87  E-value: 7.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 676330013  55 LAEISDKNIELLKVTMNKTSRslkaETDYPIETVKNKTLILVDDVLNSGRTLA 107
Cdd:PRK02458 187 LAEYLDAPIAIIDYAQDDSER----EEGYIIGDVAGKKAILIDDILNTGKTFA 235
 
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