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Conserved domains on  [gi|492089579|ref|WP_005744851|]
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MULTISPECIES: orotate phosphoribosyltransferase [Pseudomonas]

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 2.71e-93

orotate phosphoribosyltransferase; Validated


:

Pssm-ID: 234771  Cd Length: 202  Bit Score: 271.26  E-value: 2.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   1 MQAYQRDFIRFAIDRGVLRFGEFTLKSGRTSPYFFNAG-LFNTGSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLAS 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  80 ATAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQe 158
Cdd:PRK00455  81 AVARAL------DLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492089579 159 rgngelSAIQEVERDFGIPVVSIVSLNQVLEFLADDPQLKQHLPAVEAYRAQYGI 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-213 2.71e-93

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 271.26  E-value: 2.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   1 MQAYQRDFIRFAIDRGVLRFGEFTLKSGRTSPYFFNAG-LFNTGSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLAS 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  80 ATAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQe 158
Cdd:PRK00455  81 AVARAL------DLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492089579 159 rgngelSAIQEVERDFGIPVVSIVSLNQVLEFLADDPQLKQHLPAVEAYRAQYGI 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
2-212 3.00e-75

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 225.42  E-value: 3.00e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   2 QAYQRDFIRFAIDRGVLRFGEFTLKSGRTSPYFFNAGLFNT-GSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLASA 80
Cdd:COG0461    1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  81 TAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQEr 159
Cdd:COG0461   81 VARAL------GLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492089579 160 gngelSAIQEVErDFGIPVVSIVSLNQVLEFLADDPQLKQ-HLPAVEAYRAQYG 212
Cdd:COG0461  154 -----GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
11-187 1.04e-69

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: 210.36  E-value: 1.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   11 FAIDRGVLRFGEFTLKSGRTSPYFFNAGLFNTGSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLASATAVALAEHHD 90
Cdd:TIGR00336   2 LLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   91 rDLPWCFNRKEAKAHGEGGSLVGSPLAGN-VLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERgngelSAIQE 169
Cdd:TIGR00336  82 -DIPLCFNRKEAKDHGEGGNIEGELLEGDkVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQE 155
                         170
                  ....*....|....*...
gi 492089579  170 VERDFGIPVVSIVSLNQV 187
Cdd:TIGR00336 156 FEKEYGLPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
49-183 1.72e-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: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  49 LGRFYAAAVVESGIAFDVLFGPAYKGIPLASATAVALaehhdrDLPWCFNRKEAKAHGEGGSL-------VGSPLAG-NV 120
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARAL------GLPLAFIRKERKGPGRTPSEpyglelpLGGDVKGkRV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492089579 121 LIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERGngelsaiQEVERDFGIPVVSIVS 183
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG-------ARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
45-145 2.40e-08

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: 51.21  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   45 ALAQLGRFYAAAVVES-GIAFDVLFGPAYKGIPLASATAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAGN---- 119
Cdd:pfam00156  10 AILKAVARLAAQINEDyGGKPDVVVGILRGGLPFAGILARRL------DVPLAFVRKVSYNPDTSEVMKTSSALPDlkgk 83
                          90       100
                  ....*....|....*....|....*..
gi 492089579  120 -VLIIDDVITAGTAIREVMQIIKDQNA 145
Cdd:pfam00156  84 tVLIVDDILDTGGTLLKVLELLKNVGP 110
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-213 2.71e-93

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 271.26  E-value: 2.71e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   1 MQAYQRDFIRFAIDRGVLRFGEFTLKSGRTSPYFFNAG-LFNTGSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLAS 79
Cdd:PRK00455   1 MKMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRkLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  80 ATAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQe 158
Cdd:PRK00455  81 AVARAL------DLPAIFVRKEAKDHGEGGQIEGRRLFGkRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492089579 159 rgngelSAIQEVERDFGIPVVSIVSLNQVLEFLADDPQLKQHLPAVEAYRAQYGI 213
Cdd:PRK00455 154 ------SAAQEVFADAGVPLISLITLDDLLEYAEEGPLCKEGLPAVKAYRRNYGV 202
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
2-212 3.00e-75

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 225.42  E-value: 3.00e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   2 QAYQRDFIRFAIDRGVLRFGEFTLKSGRTSPYFFNAGLFNT-GSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLASA 80
Cdd:COG0461    1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSyPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  81 TAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQEr 159
Cdd:COG0461   81 VARAL------GLPAIFVRKEAKDHGTGGQIEGGLLPGeRVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE- 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492089579 160 gngelSAIQEVErDFGIPVVSIVSLNQVLEFLADDPQLKQ-HLPAVEAYRAQYG 212
Cdd:COG0461  154 -----GAAENLE-EAGVPLHSLLTLDDLLELLKEKGYIDPeELEALEAYREKPG 201
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
11-187 1.04e-69

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: 210.36  E-value: 1.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   11 FAIDRGVLRFGEFTLKSGRTSPYFFNAGLFNTGSALAQLGRFYAAAVVESGIAFDVLFGPAYKGIPLASATAVALAEHHD 90
Cdd:TIGR00336   2 LLLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVKLAKPGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   91 rDLPWCFNRKEAKAHGEGGSLVGSPLAGN-VLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERgngelSAIQE 169
Cdd:TIGR00336  82 -DIPLCFNRKEAKDHGEGGNIEGELLEGDkVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQER-----SAGQE 155
                         170
                  ....*....|....*...
gi 492089579  170 VERDFGIPVVSIVSLNQV 187
Cdd:TIGR00336 156 FEKEYGLPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
49-183 1.72e-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: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  49 LGRFYAAAVVESGIAFDVLFGPAYKGIPLASATAVALaehhdrDLPWCFNRKEAKAHGEGGSL-------VGSPLAG-NV 120
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARAL------GLPLAFIRKERKGPGRTPSEpyglelpLGGDVKGkRV 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492089579 121 LIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERGngelsaiQEVERDFGIPVVSIVS 183
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG-------ARELASPGDPVYSLFT 130
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
59-187 3.49e-10

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 57.19  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  59 ESGIAFDVLFGPAYKGIPLASATA----VALAEHHDRDLpwcfnrKEAKAHGEGGSLVG--SPLAG-NVLIIDDVITAGT 131
Cdd:PRK02277  81 KEDEEVDVVVGIAKSGVPLATLVAdelgKDLAIYHPKKW------DHGEGEKKTGSFSRnfASVEGkRCVIVDDVITSGT 154
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492089579 132 AIREVMQIIKDQNAT--AAGVLIalnrQERGngelsaIQEVErdfGIPVVSIVSLNQV 187
Cdd:PRK02277 155 TMKETIEYLKEHGGKpvAVVVLI----DKSG------IDEID---GVPVYSLIRVVRV 199
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
5-135 9.24e-10

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 57.39  E-value: 9.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   5 QRDFIRFAIDRGVLRFGEFTLKSGRTSPYFF-------NAGLFNtgsalaQLGRFYAAAVveSGIAFDVLFGPAYKGIPl 77
Cdd:PRK05500 287 HQDLILQLYDIGCLLFGEYVQASGATFSYYIdlrkiisNPQLFH------QVLSAYAEIL--KNLTFDRIAGIPYGSLP- 357
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492089579  78 aSATAVALAEHHdrdlPWCFNRKEAKAHGEGGSLVGSPLAG-NVLIIDDVITAGTAIRE 135
Cdd:PRK05500 358 -TATGLALHLHH----PMIFPRKEVKAHGTRRLIEGNFHPGeTVVVVDDILITGKSVME 411
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
16-198 1.18e-08

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 52.92  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  16 GVLRFGEFTLKSGRTSPYFFNAGLFNTGSALAQLgrfYAAAVVESGIAF--DVLFGPAYKGIPLasATAVALaehhDRDL 93
Cdd:PRK13809  21 GAIKFGKFILASGEETPIYVDMRLVISSPEVLQT---IATLIWRLRPSFnsSLLCGVPYTALTL--ATSISL----KYNI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  94 PWCFNRKEAKAHGEGGSLVGSPL--AGNV-LIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERGngelsaiQEV 170
Cdd:PRK13809  92 PMVLRRKELKNVDPSDAIKVEGLftPGQTcLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGA-------CQP 164
                        170       180
                 ....*....|....*....|....*...
gi 492089579 171 ERDFGIPVVSIVSLNQVLEFLADDPQLK 198
Cdd:PRK13809 165 LGPQGIKLSSVFTVPDLIKSLISYGKLS 192
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
45-145 2.40e-08

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: 51.21  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579   45 ALAQLGRFYAAAVVES-GIAFDVLFGPAYKGIPLASATAVALaehhdrDLPWCFNRKEAKAHGEGGSLVGSPLAGN---- 119
Cdd:pfam00156  10 AILKAVARLAAQINEDyGGKPDVVVGILRGGLPFAGILARRL------DVPLAFVRKVSYNPDTSEVMKTSSALPDlkgk 83
                          90       100
                  ....*....|....*....|....*..
gi 492089579  120 -VLIIDDVITAGTAIREVMQIIKDQNA 145
Cdd:pfam00156  84 tVLIVDDILDTGGTLLKVLELLKNVGP 110
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
39-184 9.24e-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: 44.30  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  39 LFNTGSALAQLGRFYAAAVVESGIafDVLFGPAYKGIPLASATAVALaehhdrDLPWCFNRKEAKA------------HG 106
Cdd:COG0503   26 LLGDPELFRAAGDELAERFADKGI--DKVVGIEARGFILAAALAYAL------GVPFVPARKPGKLpgetvseeydleYG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579 107 EGGSLV--------GSplagNVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALnrqergngELSAIQEVERDFGIPV 178
Cdd:COG0503   98 TGDTLElhkdalkpGD----RVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLI--------ELGFLGGREKLRDYPV 165

                 ....*.
gi 492089579 179 VSIVSL 184
Cdd:COG0503  166 ESLLTL 171
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
64-154 1.19e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.12  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  64 FDVLFGPAYKGIPLASATAVALAehhdrdLPWCFNRKEAKAH--------------GEGGSLV-----GSPLAG-NVLII 123
Cdd:PRK07322  53 VDVLVTPETKGIPLAHALSRRLG------KPYVVARKSRKPYmqdpiiqevvsittGKPQLLVldgadAEKLKGkRVAIV 126
                         90       100       110
                 ....*....|....*....|....*....|.
gi 492089579 124 DDVITAGTAIREVMQIIKDQNATAAGVLIAL 154
Cdd:PRK07322 127 DDVVSTGGTLTALERLVERAGGQVVAKAAIF 157
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
51-185 2.47e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 40.75  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492089579  51 RFYAAAVVE--SGIAFDVLFGPAYKGIPLAsataVALAEHHDRDLPWcfnrkeAKAHGEGG----------SLVGSPL-- 116
Cdd:PRK08558  97 RLIAPVVAErfMGLRVDVVLTAATDGIPLA----VAIASYFGADLVY------AKKSKETGvekfyeeyqrLASGIEVtl 166
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492089579 117 --------AG-NVLIIDDVITAGTAIREVMQIIKDQNATAAGVLIALNRQERGngelsaIQEVERDFGIPVVSIVSLN 185
Cdd:PRK08558 167 ylpasalkKGdRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVG------IDRAREETDAPVDALYTLE 238
 
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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