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Conserved domains on  [gi|446728845|ref|WP_000806158|]
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MULTISPECIES: orotate phosphoribosyltransferase [Enterobacteriaceae]

Protein Classification

orotate phosphoribosyltransferase( domain architecture ID 10011447)

orotate phosphoribosyltransferase catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)

CATH:  3.40.50.2020
EC:  2.4.2.-
Gene Ontology:  GO:0000287|GO:0004588|GO:0046132
PubMed:  11751055
SCOP:  4000253

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-213 4.71e-98

orotate phosphoribosyltransferase; Validated


:

Pssm-ID: 234771  Cd Length: 202  Bit Score: 283.20  E-value: 4.71e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   1 MKPYQRQFIEFALGKQVLKFGEFTLKSGRKSPYFFNAG-LFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIAT 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  80 TTAVAlaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQe 158
Cdd:PRK00455  81 AVARA------LDLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446728845 159 rgrgeiSAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-213 4.71e-98

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 283.20  E-value: 4.71e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   1 MKPYQRQFIEFALGKQVLKFGEFTLKSGRKSPYFFNAG-LFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIAT 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  80 TTAVAlaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQe 158
Cdd:PRK00455  81 AVARA------LDLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446728845 159 rgrgeiSAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
10-187 1.07e-84

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: 248.50  E-value: 1.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   10 EFALGKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIATTTAVALAEHH 89
Cdd:TIGR00336   1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   90 DlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERgrgeiSAIQ 168
Cdd:TIGR00336  81 G-DIPLCFNRKEAKDHGEGGNIEGELLEGdKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQ 154
                         170
                  ....*....|....*....
gi 446728845  169 EVERDYNCKVISIITLKDL 187
Cdd:TIGR00336 155 EFEKEYGLPVISLITLKDL 173
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
4-212 2.40e-77

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 230.81  E-value: 2.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   4 YQRQFIEFALGKQVLKFGEFTLKSGRKSPYFFNAGLFNT-GRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIATTTA 82
Cdd:COG0461    3 YKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  83 VALaehhdlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQErgr 161
Cdd:COG0461   83 RAL------GLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE--- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446728845 162 geiSAIQEVErDYNCKVISIITLKDLIAYLEEKPEMAE-HLAAVKAYREEFG 212
Cdd:COG0461  154 ---GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
49-166 1.41e-16

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: 72.81  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  49 LGRFYAEALVDSGIKFDLLFGPAYKGIPIATttavALAEHhdLDLPYCFNRKEAKDHGEGG-------NLVGSALQG-RV 120
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAA----ALARA--LGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGkRV 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446728845 121 MLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
39-175 1.05e-06

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: 46.59  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   39 LFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIAtttaVALAEHhdLDLPYCFNRKEAKDHGEGGNLVGSALQG 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFA----GILARR--LDVPLAFVRKVSYNPDTSEVMKTSSALP 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446728845  119 -----RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQE----------RGRGEISAIQEVERDYN 175
Cdd:pfam00156  79 dlkgkTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAgtepkdkydkRVDDWIVFVVGFGLDER 150
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-213 4.71e-98

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 283.20  E-value: 4.71e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   1 MKPYQRQFIEFALGKQVLKFGEFTLKSGRKSPYFFNAG-LFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIAT 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  80 TTAVAlaehhdLDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQe 158
Cdd:PRK00455  81 AVARA------LDLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446728845 159 rgrgeiSAIQEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREEFGV 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
10-187 1.07e-84

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: 248.50  E-value: 1.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   10 EFALGKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIATTTAVALAEHH 89
Cdd:TIGR00336   1 ELLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   90 DlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERgrgeiSAIQ 168
Cdd:TIGR00336  81 G-DIPLCFNRKEAKDHGEGGNIEGELLEGdKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQ 154
                         170
                  ....*....|....*....
gi 446728845  169 EVERDYNCKVISIITLKDL 187
Cdd:TIGR00336 155 EFEKEYGLPVISLITLKDL 173
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
4-212 2.40e-77

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 230.81  E-value: 2.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   4 YQRQFIEFALGKQVLKFGEFTLKSGRKSPYFFNAGLFNT-GRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIATTTA 82
Cdd:COG0461    3 YKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  83 VALaehhdlDLPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQErgr 161
Cdd:COG0461   83 RAL------GLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE--- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446728845 162 geiSAIQEVErDYNCKVISIITLKDLIAYLEEKPEMAE-HLAAVKAYREEFG 212
Cdd:COG0461  154 ---GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
49-166 1.41e-16

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: 72.81  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  49 LGRFYAEALVDSGIKFDLLFGPAYKGIPIATttavALAEHhdLDLPYCFNRKEAKDHGEGG-------NLVGSALQG-RV 120
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAA----ALARA--LGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGkRV 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446728845 121 MLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELAS 120
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
18-204 1.54e-11

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 61.01  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  18 LKFGEFTLKSGRKSPYFFNAGLFNTGRDL-----ALLGRfyaeaLVDSgIKFDLLFGPAYKGIPIATttAVALAEhhdlD 92
Cdd:PRK13809  23 IKFGKFILASGEETPIYVDMRLVISSPEVlqtiaTLIWR-----LRPS-FNSSLLCGVPYTALTLAT--SISLKY----N 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  93 LPYCFNRKEAKDHGEGGNLVGSALQG---RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGrgeisaiQE 169
Cdd:PRK13809  91 IPMVLRRKELKNVDPSDAIKVEGLFTpgqTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGA-------CQ 163
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446728845 170 VERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAV 204
Cdd:PRK13809 164 PLGPQGIKLSSVFTVPDLIKSLISYGKLSSGDLTL 198
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
54-165 1.57e-08

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 52.56  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  54 AEALVD----SGIKFDLLFGPAYKGIPIATTTAVALaehhDLDLPYCFNRKEakDHGEGGNLVGS------ALQG-RVML 122
Cdd:PRK02277  72 ASAMADmlekEDEEVDVVVGIAKSGVPLATLVADEL----GKDLAIYHPKKW--DHGEGEKKTGSfsrnfaSVEGkRCVI 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446728845 123 VDDVITAGTAIRESMEIIQANGAT--LAGVLISldrqERGRGEIS 165
Cdd:PRK02277 146 VDDVITSGTTMKETIEYLKEHGGKpvAVVVLID----KSGIDEID 186
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
18-159 2.26e-08

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 53.15  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  18 LKFGEFTLKSGRKSPYFF-------NAGLFNTgrdlALLGrfYAEALvdSGIKFDLLFGPAYKGIPiaTTTAVALAEHHd 90
Cdd:PRK05500 300 LLFGEYVQASGATFSYYIdlrkiisNPQLFHQ----VLSA--YAEIL--KNLTFDRIAGIPYGSLP--TATGLALHLHH- 368
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  91 ldlPYCFNRKEAKDHGEGGNLVGSALQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQER 159
Cdd:PRK05500 369 ---PMIFPRKEVKAHGTRRLIEGNFHPGeTVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQG 435
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
39-175 1.05e-06

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: 46.59  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845   39 LFNTGRDLALLGRFYAEALVDSGIKFDLLFGPAYKGIPIAtttaVALAEHhdLDLPYCFNRKEAKDHGEGGNLVGSALQG 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFA----GILARR--LDVPLAFVRKVSYNPDTSEVMKTSSALP 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446728845  119 -----RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQE----------RGRGEISAIQEVERDYN 175
Cdd:pfam00156  79 dlkgkTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAgtepkdkydkRVDDWIVFVVGFGLDER 150
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
54-184 5.57e-06

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: 45.07  E-value: 5.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  54 AEALVD--SGIKFDLLFGPAYKGIPIATttAVALAehhdLDLPYCFNRKEAK------------DHGEGGNLV--GSALQ 117
Cdd:COG0503   37 GDELAErfADKGIDKVVGIEARGFILAA--ALAYA----LGVPFVPARKPGKlpgetvseeydlEYGTGDTLElhKDALK 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446728845 118 G--RVMLVDDVITAGTAIRESMEIIQANGATLAG--VLISLDRQErGRGEIsaiqeveRDYNckVISIITL 184
Cdd:COG0503  111 PgdRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGiaFLIELGFLG-GREKL-------RDYP--VESLLTL 171
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
63-169 1.54e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 40.73  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  63 KFDLLFGPAYKGIPIATttavALAEHhdLDLPYCFNRKEAKDH--------------GEGGNLV-----GSALQG-RVML 122
Cdd:PRK07322  52 EVDVLVTPETKGIPLAH----ALSRR--LGKPYVVARKSRKPYmqdpiiqevvsittGKPQLLVldgadAEKLKGkRVAI 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446728845 123 VDDVITAGTAIRESMEIIQANGATLAGVL-ISLDRQERGRGEISAIQE 169
Cdd:PRK07322 126 VDDVVSTGGTLTALERLVERAGGQVVAKAaIFAEGDASNRLDVIYLAH 173
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
33-184 5.20e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 39.98  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845  33 YFFNAGLFNTGRDLALLGRFYAEALvdSGIKFDLLFGPAYKGIPIAtttaVALAEHHDLDLPYCFNRKE--------AKD 104
Cdd:PRK08558  83 YVDNSSVVFDPSFLRLIAPVVAERF--MGLRVDVVLTAATDGIPLA----VAIASYFGADLVYAKKSKEtgvekfyeEYQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728845 105 HGEGGN-----LVGSALQ--GRVMLVDDVITAGTAIRESMEIIQANGATLAGV--LISldrqergRGEISaIQEVERDYN 175
Cdd:PRK08558 157 RLASGIevtlyLPASALKkgDRVLIVDDIIRSGETQRALLDLARQAGADVVGVffLIA-------VGEVG-IDRAREETD 228

                 ....*....
gi 446728845 176 CKVISIITL 184
Cdd:PRK08558 229 APVDALYTL 237
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
116-166 1.62e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 38.20  E-value: 1.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446728845 116 LQG-RVMLVDDVITAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISA 166
Cdd:PRK06031 152 LEGrRVALIDDVISSGASIVAGLRLLAACGIEPAGIGAAMLQSERWRESLAA 203
 
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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