NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|974576755|ref|NP_001305855|]
View 

ribulose-phosphate 3-epimerase isoform 6 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-232 6.22e-119

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: 337.91  E-value: 6.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGF 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576755 166 GGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
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 ...
 6-232 6.22e-119

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: 337.91  E-value: 6.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGF 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576755 166 GGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
Cdd:cd00429  141 GGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-234 2.37e-107

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 309.22  E-value: 2.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  87 GANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP--WANQIDMALVMTVEP 163
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576755 164 GFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 234
Cdd:PTZ00170 150 GFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-238 1.52e-102

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: 296.60  E-value: 1.52e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  85 VAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPG 164
Cdd:COG0036   79 EAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEYVLDDVDLVLVMSVNPG 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576755 165 FGGQKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 238
Cdd:COG0036  141 FGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-218 3.40e-77

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: 231.45  E-value: 3.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGF 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576755  166 GGQKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 218
Cdd:pfam00834 141 GGQSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-232 4.80e-76

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: 229.08  E-value: 4.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   87 GANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFG 166
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFG 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  167 GQKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
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 ...
 6-232 6.22e-119

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: 337.91  E-value: 6.22e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:cd00429   79 AGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGF 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576755 166 GGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
Cdd:cd00429  141 GGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-234 2.37e-107

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 309.22  E-value: 2.37e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  87 GANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP--WANQIDMALVMTVEP 163
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576755 164 GFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 234
Cdd:PTZ00170 150 GFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-238 1.52e-102

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: 296.60  E-value: 1.52e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  85 VAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPG 164
Cdd:COG0036   79 EAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEYVLDDVDLVLVMSVNPG 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576755 165 FGGQKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 238
Cdd:COG0036  141 FGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-241 3.61e-101

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 293.45  E-value: 3.61e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWV 80
Cdd:PLN02334   4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPEDYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  81 KPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW--ANQIDMA 156
Cdd:PLN02334  82 PDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMK------------------AGVVLNPGTPVEAVEPVveKGLVDMV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755 157 LVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCS 236
Cdd:PLN02334 144 LVMSVEPGFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVE 223


                 ....*
gi 974576755 237 EAAQK 241
Cdd:PLN02334 224 KAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 6-233 4.22e-93

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 272.83  E-value: 4.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPfFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK05581   5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLP-LDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIK------------------AGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGF 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974576755 166 GGQKFMEDMMPKVHWLR----TQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRN 233
Cdd:PRK05581 145 GGQKFIPEVLEKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-218 3.40e-77

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: 231.45  E-value: 3.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   86 AGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGF 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576755  166 GGQKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 218
Cdd:pfam00834 141 GGQSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-232 4.80e-76

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: 229.08  E-value: 4.80e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   87 GANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFG 166
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFG 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  167 GQKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
Cdd:TIGR01163 141 GQKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 6-216 2.14e-42

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 143.98  E-value: 2.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPfFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK09722   4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKP-LDVHLMVTDPQDYIDQLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEaTENPGA--LIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPWANQIDMALVMTVEP 163
Cdd:PRK09722  81 AGADFITLHPE-TINGQAfrLIDEIRRAGMK------------------VGLVLNPETPVESIKYYIHLLDKITVMTVDP 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 974576755 164 GFGGQKFMEDMMPKV----HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGS 216
Cdd:PRK09722 142 GFAGQPFIPEMLDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-228 1.74e-30

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 112.44  E-value: 1.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   9 PSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSKPEQWVKPMAVAGA 88
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  89 NQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEylaPW---ANQIDMALVMTVEPGF 165
Cdd:PRK08005  83 GWIFIHAESVQNPSEILADIRAIGAKA------------------GLALNPATPLL---PYrylALQLDALMIMTSEPDG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974576755 166 GGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 228
Cdd:PRK08005 142 RGQQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 6-223 1.15e-14

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 70.68  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFEVAKACVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  86 AGANQYTFHLEATENPGALIKDIRENgmkscsvtqaevqwhsQGPLQVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 165
Cdd:PRK08091  90 AGADIVTLQVEQTHDLALTIEWLAKQ----------------KTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRT 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974576755 166 GGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSED 223
Cdd:PRK08091 154 GTKAPSDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 34-222 5.25e-13

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 66.63  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755  34 LHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSkpEQWVKPMAVAGANQYTFHLEAtENPGALIKDIRENGM 113
Cdd:PRK14057  49 LHLDLMDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACVKAGAHCITLQA-EGDIHLHHTLSWLGQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576755 114 KSCSVTQAEVqwhsqgPLQVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD---- 189
Cdd:PRK14057 122 QTVPVIGGEM------PVIRGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegki 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 974576755 190 IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSE 222
Cdd:PRK14057 196 IVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 194-238 6.55e-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: 6.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 974576755 194 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 238
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 194-232 5.29e-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: 5.29e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 974576755 194 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 232
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 190-228 5.47e-05

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: 42.95  E-value: 5.47e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 974576755 190 IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 228
Cdd:cd04726  161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
192-228 3.33e-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: 3.33e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 974576755 192 VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 228
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
194-239 4.42e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 40.17  E-value: 4.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 974576755 194 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAA 239
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
198-228 8.49e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 36.51  E-value: 8.49e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 974576755  198 PDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 228
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH