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Conserved domains on  [gi|974576762|ref|NP_001305857|]
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ribulose-phosphate 3-epimerase isoform 8 [Homo sapiens]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10087218)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

EC:  5.1.3.1
Gene Ontology:  GO:0046872|GO:0004750

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-197 1.06e-86

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


:

Pssm-ID: 238244  Cd Length: 211  Bit Score: 254.71  E-value: 1.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSV---------------------- 143
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVevlepyldevdlvlvmsvnpgf 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576762 144 -------------HWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:cd00429  141 ggqkfipevlekiRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-197 1.06e-86

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 254.71  E-value: 1.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSV---------------------- 143
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVevlepyldevdlvlvmsvnpgf 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576762 144 -------------HWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:cd00429  141 ggqkfipevlekiRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-199 1.50e-77

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 232.18  E-value: 1.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  87 GANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGT------------------------ 141
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTpvevlfplidtdlvdmvlvmtvep 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576762 142 -------------SVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 199
Cdd:PTZ00170 150 gfggqsfmhdmmpKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-203 2.84e-73

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 220.72  E-value: 2.84e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  85 VAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLR----------------- 147
Cdd:COG0036   79 EAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEyvlddvdlvlvmsvnpg 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576762 148 ---TQF-------------------PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 203
Cdd:COG0036  141 fggQKFipsvlekirrlrelidergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-183 1.81e-54

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 172.52  E-value: 1.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLRTQFPSLD----------- 154
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYLLDKLDlvllmsvnpgf 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576762  155 ----------------------------IEVDGGVGPDTVHKCAEAGANMIVSGSAI 183
Cdd:pfam00834 141 ggqsfipsvlekirkvrkmidergldtlIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-197 1.91e-54

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 172.85  E-value: 1.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   87 GANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSV----------------------- 143
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLefleyvlpdvdlvllmsvnpgfg 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  144 ----------------HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:TIGR01163 141 gqkfipdtlekirevrKMIDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-197 1.06e-86

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 254.71  E-value: 1.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSV---------------------- 143
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVevlepyldevdlvlvmsvnpgf 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576762 144 -------------HWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:cd00429  141 ggqkfipevlekiRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-199 1.50e-77

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 232.18  E-value: 1.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  87 GANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGT------------------------ 141
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTpvevlfplidtdlvdmvlvmtvep 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576762 142 -------------SVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 199
Cdd:PTZ00170 150 gfggqsfmhdmmpKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-206 1.64e-74

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 224.50  E-value: 1.64e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWV 80
Cdd:PLN02334   4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPEDYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  81 KPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVH-------------- 144
Cdd:PLN02334  82 PDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMK------------------AGVVLNPGTPVEavepvvekglvdmv 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762 145 -----------------------WLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCS 201
Cdd:PLN02334 144 lvmsvepgfggqsfipsmmdkvrALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVE 223


                 ....*
gi 974576762 202 EAAQK 206
Cdd:PLN02334 224 KAAVA 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-203 2.84e-73

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 220.72  E-value: 2.84e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  85 VAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLR----------------- 147
Cdd:COG0036   79 EAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEyvlddvdlvlvmsvnpg 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576762 148 ---TQF-------------------PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 203
Cdd:COG0036  141 fggQKFipsvlekirrlrelidergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 6-198 4.95e-67

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 205.03  E-value: 4.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPfFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK05581   5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLP-LDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLRTQFPSLD----------- 154
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIK------------------AGLVLNPATPLEPLEDVLDLLDlvllmsvnpgf 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974576762 155 ----------------------------IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRN 198
Cdd:PRK05581 145 ggqkfipevlekirelrklidergldilIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-183 1.81e-54

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 172.52  E-value: 1.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLRTQFPSLD----------- 154
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYLLDKLDlvllmsvnpgf 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576762  155 ----------------------------IEVDGGVGPDTVHKCAEAGANMIVSGSAI 183
Cdd:pfam00834 141 ggqsfipsvlekirkvrkmidergldtlIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-197 1.91e-54

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 172.85  E-value: 1.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   87 GANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSV----------------------- 143
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLefleyvlpdvdlvllmsvnpgfg 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  144 ----------------HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:TIGR01163 141 gqkfipdtlekirevrKMIDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 6-181 1.49e-24

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 96.22  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPfFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK09722   4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKP-LDVHLMVTDPQDYIDQLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEaTENPGA--LIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVHWLRTQFPSLD--------- 154
Cdd:PRK09722  81 AGADFITLHPE-TINGQAfrLIDEIRRAGMK------------------VGLVLNPETPVESIKYYIHLLDkitvmtvdp 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576762 155 ------------------------------IEVDGGVGPDTVHKCAEAGANMIVSGS 181
Cdd:PRK09722 142 gfagqpfipemldkiaelkalrerngleylIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-193 4.85e-16

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 73.53  E-value: 4.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   9 PSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSKPEQWVKPMAVAGA 88
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  89 NQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGT--------------------------- 141
Cdd:PRK08005  83 GWIFIHAESVQNPSEILADIRAIGAKA------------------GLALNPATpllpyrylalqldalmimtsepdgrgq 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762 142 --------SVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 193
Cdd:PRK08005 145 qfiaamceKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 6-155 7.73e-08

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 51.03  E-value: 7.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFEVAKACVA 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  86 AGANQYTFHLEATENPGALIKDIRENgmkscsvtqaevqwhsQGPLQVGLAIKPGTSVHWLRTQFPSLDI 155
Cdd:PRK08091  90 AGADIVTLQVEQTHDLALTIEWLAKQ----------------KTTVLIGLCLCPETPISLLEPYLDQIDL 143
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 159-203 5.16e-06

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 45.56  E-value: 5.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 974576762 159 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 203
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 124-193 8.77e-06

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 44.88  E-value: 8.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974576762 124 QWHSQGPLQVGL-------AIKPGTSVHWLRTQFPSLDIE--VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 193
Cdd:cd04726  121 KLLKLGVDIVILhrgidaqAAGGWWPEDDLKKVKKLLGVKvaVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 159-197 3.81e-05

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 42.89  E-value: 3.81e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 974576762 159 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 197
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
PRK14057 PRK14057
epimerase; Provisional
 34-187 5.43e-05

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 42.75  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762  34 LHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSkpEQWVKPMAVAGANQYTFHLEATEN------------- 100
Cdd:PRK14057  49 LHLDLMDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACVKAGAHCITLQAEGDihlhhtlswlgqq 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576762 101 ----PGALIKDIRenGMKSCSVTQAEVQWHSQGPLQV--GLAIKPG-------TSVHWLRTQFPSL--------DIEVDG 159
Cdd:PRK14057 123 tvpvIGGEMPVIR--GISLCPATPLDVIIPILSDVEViqLLAVNPGygskmrsSDLHERVAQLLCLlgdkregkIIVIDG 200

                        170       180
                 ....*....|....*....|....*...
gi 974576762 160 GVGPDTVHKCAEAGANMIVSGSAIMRSE 187
Cdd:PRK14057 201 SLTQDQLPSLIAQGIDRVVSGSALFRDD 228
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
157-193 2.27e-04

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 41.15  E-value: 2.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 974576762 157 VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 193
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
159-204 3.29e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 40.17  E-value: 3.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 974576762 159 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAA 204
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
163-193 6.28e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 36.51  E-value: 6.28e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 974576762  163 PDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 193
Cdd:pfam00218 220 PADVRELKEHGANAFLVGESLMRQEDVRAAI 250
 
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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