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Conserved domains on  [gi|40385883|ref|NP_954699|]
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ribulose-phosphate 3-epimerase isoform 1 [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 ...
6-214 3.60e-122

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: 345.23  E-value: 3.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429  79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 40385883 166 QFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:cd00429 159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
6-214 3.60e-122

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: 345.23  E-value: 3.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429  79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 40385883 166 QFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:cd00429 159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
7-216 1.70e-111

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 318.85  E-value: 1.70e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   87 GANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTSVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40385883  164 RTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 216
Cdd:PTZ00170 168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
5-220 5.54e-106

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: 304.31  E-value: 5.54e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  85 VAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR 164
Cdd:COG0036  79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883 165 TQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 220
Cdd:COG0036 159 ELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
6-200 3.43e-81

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: 241.08  E-value: 3.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883     6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 40385883   166 QFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 200
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
7-214 3.88e-79

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: 236.02  E-value: 3.88e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883     7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    87 GANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 40385883   166 ---QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
6-214 3.60e-122

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: 345.23  E-value: 3.60e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429  79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 40385883 166 QFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:cd00429 159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
7-216 1.70e-111

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 318.85  E-value: 1.70e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   87 GANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTSVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PTZ00170  88 GASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 40385883  164 RTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 216
Cdd:PTZ00170 168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
5-220 5.54e-106

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: 304.31  E-value: 5.54e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMA 84
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  85 VAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR 164
Cdd:COG0036  79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883 165 TQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 220
Cdd:COG0036 159 ELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
1-223 7.82e-105

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 301.92  E-value: 7.82e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWV 80
Cdd:PLN02334   4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPEDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   81 KPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPW--ANQIDMALVMTVEPGFGGQKFMEDM 156
Cdd:PLN02334  82 PDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFGGQSFIPSM 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40385883  157 MPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQK 223
Cdd:PLN02334 162 MDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
6-215 1.48e-96

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 280.53  E-value: 1.48e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSKPEQWVKPMAV 85
Cdd:PRK05581   5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPDRYVPDFAK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR- 164
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRk 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 40385883  165 ---TQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRN 215
Cdd:PRK05581 163 lidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
6-200 3.43e-81

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: 241.08  E-value: 3.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883     6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 40385883   166 QFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 200
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
7-214 3.88e-79

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: 236.02  E-value: 3.88e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883     7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSKPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    87 GANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 40385883   166 ---QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
6-198 1.40e-46

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 154.00  E-value: 1.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSKPEQWVKPMAV 85
Cdd:PRK09722   4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQDYIDQLAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   86 AGANQYTFHLEaTENPGA--LIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKV--- 160
Cdd:PRK09722  81 AGADFITLHPE-TINGQAfrLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIael 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 40385883  161 -HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGS 198
Cdd:PRK09722 160 kALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-210 7.32e-35

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 123.22  E-value: 7.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    9 PSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSKPEQWVKPMAVAGA 88
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   89 NQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEylaPW---ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:PRK08005  83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLL---PYrylALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSRE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 40385883  166 QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 210
Cdd:PRK08005 160 HFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
6-205 9.56e-17

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 76.07  E-value: 9.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSKPEQWVKPMAV 85
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFEVAKACVA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   86 AGANQYTFHLEATENPGALIKDIRENGMKV--GLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PRK08091  90 AGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQV 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 40385883  164 RTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSED 205
Cdd:PRK08091 170 ENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
34-211 1.58e-11

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 62.01  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883   34 LHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSkpEQWVKPMAV--AGANQYTFHLEATENPGALIKDIREN 111
Cdd:PRK14057  49 LHLDLMDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWLGQQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40385883  112 GMKV---------GLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGV 178
Cdd:PRK14057 123 TVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSL 202
                        170       180       190
                 ....*....|....*....|....*....|...
gi 40385883  179 GPDTVHKCAEAGANMIVSGSAIMRseDPRSVIN 211
Cdd:PRK14057 203 TQDQLPSLIAQGIDRVVSGSALFR--DDRLVEN 233
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
176-220 7.07e-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: 45.18  E-value: 7.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 40385883 176 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 220
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
176-214 4.53e-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: 4.53e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 40385883 176 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 214
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
172-210 6.64e-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: 42.18  E-value: 6.64e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 40385883 172 IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 210
Cdd:cd04726 161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
174-210 3.86e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 40.77  E-value: 3.86e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 40385883  174 VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 210
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
176-221 4.63e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 39.78  E-value: 4.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 40385883  176 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAA 221
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
180-210 7.35e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 36.51  E-value: 7.35e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 40385883   180 PDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 210
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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