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Conserved domains on  [gi|1080386880|gb|OFL74241|]
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orotate phosphoribosyltransferase [Corynebacterium sp. HMSC077C02]

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
 14-176 1.61e-64

orotate phosphoribosyltransferase; Validated


:

Pssm-ID: 234771  Cd Length: 202  Bit Score: 196.92  E-value: 1.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  14 QRLAELVKELAVV-HGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDW--DYAHVGGLTLGADPVATSVMHA 90
Cdd:PRK00455    6 REFIEFLLEIGALlFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  91 EGrpIDAFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAE 170
Cdd:PRK00455   86 LD--LPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFADA 163


                  ....*.
gi 1080386880 171 GLDYRY 176
Cdd:PRK00455  164 GVPLIS 169
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 14-176 1.61e-64

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 196.92  E-value: 1.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  14 QRLAELVKELAVV-HGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDW--DYAHVGGLTLGADPVATSVMHA 90
Cdd:PRK00455    6 REFIEFLLEIGALlFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  91 EGrpIDAFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAE 170
Cdd:PRK00455   86 LD--LPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFADA 163


                  ....*.
gi 1080386880 171 GLDYRY 176
Cdd:PRK00455  164 GVPLIS 169
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 16-176 1.12e-56

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 177.27  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  16 LAELVKELAVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDW--DYAHVGGLTLGADPVATSVMHAEGR 93
Cdd:COG0461     8 AELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELgpEFDAVAGPATGGIPLAAAVARALGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  94 PidAFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAEGLD 173
Cdd:COG0461    88 P--AIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVP 165


                  ...
gi 1080386880 174 YRY 176
Cdd:COG0461   166 LHS 168
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 24-174 2.41e-33

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: 116.76  E-value: 2.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  24 AVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGD-WDYAHVGGLTLGADPVATSV---MHAEGRPIDAFV 99
Cdd:TIGR00336   8 ALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKShLEFDVIAGPALGGIPIATAVsvkLAKPGGDIPLCF 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080386880 100 VRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDR--ATGADEVIKAEGLDY 174
Cdd:TIGR00336  88 NRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRqeRSAGQEFEKEYGLPV 164
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-173 1.73e-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: 72.04  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  53 ASRLIGSLLRELTGDWDYahVGGLTLGADPVATSVMHAEGRPIDafVVRKEAKKHGMQRR-------IEGPDIVGKKVLV 125
Cdd:cd06223     1 AGRLLAEEIREDLLEPDV--VVGILRGGLPLAAALARALGLPLA--FIRKERKGPGRTPSepyglelPLGGDVKGKRVLL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1080386880 126 VEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAEGLD 173
Cdd:cd06223    77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDP 124
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 116-168 6.19e-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: 49.67  E-value: 6.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1080386880 116 PDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIK 168
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDK 130
 
Name Accession Description Interval E-value
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 14-176 1.61e-64

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 196.92  E-value: 1.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  14 QRLAELVKELAVV-HGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDW--DYAHVGGLTLGADPVATSVMHA 90
Cdd:PRK00455    6 REFIEFLLEIGALlFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSgiEFDVVAGPATGGIPLAAAVARA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  91 EGrpIDAFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAE 170
Cdd:PRK00455   86 LD--LPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFADA 163


                  ....*.
gi 1080386880 171 GLDYRY 176
Cdd:PRK00455  164 GVPLIS 169
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 16-176 1.12e-56

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 177.27  E-value: 1.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  16 LAELVKELAVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDW--DYAHVGGLTLGADPVATSVMHAEGR 93
Cdd:COG0461     8 AELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELgpEFDAVAGPATGGIPLAAAVARALGL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  94 PidAFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAEGLD 173
Cdd:COG0461    88 P--AIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVP 165


                  ...
gi 1080386880 174 YRY 176
Cdd:COG0461   166 LHS 168
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 24-174 2.41e-33

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: 116.76  E-value: 2.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  24 AVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGD-WDYAHVGGLTLGADPVATSV---MHAEGRPIDAFV 99
Cdd:TIGR00336   8 ALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKShLEFDVIAGPALGGIPIATAVsvkLAKPGGDIPLCF 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080386880 100 VRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDR--ATGADEVIKAEGLDY 174
Cdd:TIGR00336  88 NRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRqeRSAGQEFEKEYGLPV 164
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-173 1.73e-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: 72.04  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  53 ASRLIGSLLRELTGDWDYahVGGLTLGADPVATSVMHAEGRPIDafVVRKEAKKHGMQRR-------IEGPDIVGKKVLV 125
Cdd:cd06223     1 AGRLLAEEIREDLLEPDV--VVGILRGGLPLAAALARALGLPLA--FIRKERKGPGRTPSepyglelPLGGDVKGKRVLL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1080386880 126 VEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAEGLD 173
Cdd:cd06223    77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDP 124
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
5-171 4.61e-13

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 66.24  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880   5 TSNVNQEKLQRLAELVKEL----AVVHGKVTLSSGREADYYVDLRR----ATLHHEASRLIGSLLRELTGDwdyaHVGGL 76
Cdd:PRK05500  276 TPDVCLLNQHPHQDLILQLydigCLLFGEYVQASGATFSYYIDLRKiisnPQLFHQVLSAYAEILKNLTFD----RIAGI 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  77 TLGADPVATSVMHAEGRPIdaFVVRKEAKKHGMQRRIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATV 156
Cdd:PRK05500  352 PYGSLPTATGLALHLHHPM--IFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVF 429

                         170
                  ....*....|....*
gi 1080386880 157 VDRATGADEVIKAEG 171
Cdd:PRK05500  430 IDHEQGVKDKLQSHG 444
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 24-175 7.13e-12

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 61.39  E-value: 7.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  24 AVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLRELTGDWDYAHVGGLTLGADPVATSVMHAEGRPIdafVVRKE 103
Cdd:PRK13809   22 AIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRPSFNSSLLCGVPYTALTLATSISLKYNIPM---VLRRK 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080386880 104 AKKHGMQR---RIEGPDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIKAEGLDYR 175
Cdd:PRK13809   99 ELKNVDPSdaiKVEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLGPQGIKLS 173
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 24-163 8.67e-12

orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273579  Cd Length: 187  Bit Score: 60.96  E-value: 8.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  24 AVVHGKVTLSSGREADYYVDLRRATLHHEASRLIGSLLREL----TGDWDYA---HVGGLTLGadpvatsvmHAEGRPID 96
Cdd:TIGR01367  11 ALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKildyGLKVDFIvgpAMGGVILG---------YEVARQLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1080386880  97 AFVVRKEAKKHGMQRRiEGPDI-VGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGA 163
Cdd:TIGR01367  82 VRSIFAEREGGGMKLR-RGFAVkPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGG 148
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 116-168 6.19e-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: 49.67  E-value: 6.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1080386880 116 PDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRATGADEVIK 168
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDK 130
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 25-166 3.37e-07

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 48.33  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080386880  25 VVHGKVTLSSGREADYYVDLRraTLHHEASRL--IGS----LLRELTGDWDYahVGGLTLGADPVATSVMHAEGRPIDAF 98
Cdd:PRK02277   39 LTRAKKLEKAPAPKDIHIDWS--SIGSSSSRLryIASamadMLEKEDEEVDV--VVGIAKSGVPLATLVADELGKDLAIY 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080386880  99 VVRKEakKHGMQRRIEG------PDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDRaTGADEV 166
Cdd:PRK02277  115 HPKKW--DHGEGEKKTGsfsrnfASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK-SGIDEI 185
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 96-156 9.06e-05

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 41.35  E-value: 9.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080386880  96 DAFVVRKEAkkhgmqrriegpDIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATV 156
Cdd:COG1040   143 GAFAVRPPA------------RLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 117-159 1.33e-03

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 38.09  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1080386880 117 DIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDR 159
Cdd:PLN02238   94 DVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDK 136
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 120-159 1.75e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 37.36  E-value: 1.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1080386880 120 GKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATVVDR 159
Cdd:PRK02304  114 GDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIEL 153
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 120-158 2.57e-03

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: 36.98  E-value: 2.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1080386880 120 GKKVLVVEDTTTTGNsplTAVAA---LREAGAEVVGVATVVD 158
Cdd:COG0503   112 GDRVLIVDDLLATGG---TAKAAiklVEEAGAEVVGIAFLIE 150
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 107-167 5.65e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 36.44  E-value: 5.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080386880 107 HGMQRrieGPDIVGKKVLVvedtttTGNSP--LTAVAALREAGAEVVGVATVVD------RATGADEVI 167
Cdd:cd08232   156 HAVNR---AGDLAGKRVLV------TGAGPigALVVAAARRAGAAEIVATDLADaplavaRAMGADETV 215
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 117-156 8.86e-03

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: 35.21  E-value: 8.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1080386880 117 DIVGKKVLVVEDTTTTGNSPLTAVAALREAGAEVVGVATV 156
Cdd:COG2236    85 DLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVL 124
 
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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