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Conserved domains on  [gi|1333674270|ref|XP_023498020|]
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ribulose-phosphate 3-epimerase isoform X5 [Equus caballus]

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 1.33e-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: 346.39  E-value: 1.33e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 166 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 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 1.33e-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: 346.39  E-value: 1.33e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 166 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 214
Cdd:cd00429   159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-216 2.29e-111

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 318.47  E-value: 2.29e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQWVKPMAVA 86
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  87 GANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PTZ00170   88 GASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 164 RTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSV 216
Cdd:PTZ00170  168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-220 3.03e-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: 305.08  E-value: 3.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPMA 84
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  85 VAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR 164
Cdd:COG0036    79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270 165 TQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSVCSEA 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 2.20e-82

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: 244.16  E-value: 2.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1333674270 166 QFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 200
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-214 3.15e-80

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: 239.10  E-value: 3.15e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  87 GANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333674270 166 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 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 1.33e-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: 346.39  E-value: 1.33e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 166 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 214
Cdd:cd00429   159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-216 2.29e-111

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 318.47  E-value: 2.29e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQWVKPMAVA 86
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  87 GANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PTZ00170   88 GASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 164 RTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSV 216
Cdd:PTZ00170  168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-220 3.03e-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: 305.08  E-value: 3.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPMA 84
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  85 VAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR 164
Cdd:COG0036    79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270 165 TQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSVCSEA 220
Cdd:COG0036   159 ELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-223 7.77e-106

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 304.62  E-value: 7.77e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWV 80
Cdd:PLN02334    4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPEDYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  81 KPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPW--ANQIDMALVMTVEPGFGGQKFMEDM 156
Cdd:PLN02334   82 PDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFGGQSFIPSM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333674270 157 MPKVHWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSVCSEAAQK 223
Cdd:PLN02334  162 MDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 6-214 1.00e-96

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 281.30  E-value: 1.00e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPEQWVKPMAV 85
Cdd:PRK05581    5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPDRYVPDFAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR- 164
Cdd:PRK05581   83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRk 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333674270 165 ---TQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 214
Cdd:PRK05581  163 lidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLR 215
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-200 2.20e-82

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: 244.16  E-value: 2.20e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1333674270 166 QFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 200
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-214 3.15e-80

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: 239.10  E-value: 3.15e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  87 GANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333674270 166 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLR 214
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 6-198 1.31e-47

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 156.69  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPEQWVKPMAV 85
Cdd:PRK09722    4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQDYIDQLAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEaTENPGA--LIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKV--- 160
Cdd:PRK09722   81 AGADFITLHPE-TINGQAfrLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIael 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1333674270 161 -HWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGS 198
Cdd:PRK09722  160 kALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-211 1.12e-35

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 125.53  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   9 PSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSRPEQWVKPMAVAGA 88
Cdd:PRK08005    5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  89 NQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEylaPW---ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT 165
Cdd:PRK08005   83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLL---PYrylALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSRE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1333674270 166 QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVIS 211
Cdd:PRK08005  160 HFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLS 205
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 6-215 1.96e-16

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 75.30  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSRPEQWVKPMAV 85
Cdd:PRK08091   14 PISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFEVAKACVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  86 AGANQYTFHLEATENPGALIKDIRENGMKV--GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 163
Cdd:PRK08091   90 AGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQV 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333674270 164 RTQFPSLD----IEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRS 215
Cdd:PRK08091  170 ENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKS 225
PRK14057 PRK14057
epimerase; Provisional
 34-204 1.90e-11

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 62.01  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270  34 LHLDVMDGHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSrpEQWVKPMAV--AGANQYTFHLEATENPGALIKDIREN 111
Cdd:PRK14057   49 LHLDLMDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWLGQQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333674270 112 GMKV---------GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGV 178
Cdd:PRK14057  123 TVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSL 202

                         170       180
                  ....*....|....*....|....*.
gi 1333674270 179 GPDTIHKCAEAGANMIVSGSAIMRSE 204
Cdd:PRK14057  203 TQDQLPSLIAQGIDRVVSGSALFRDD 228
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 176-220 6.67e-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: 6.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1333674270 176 GGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSVCSEA 220
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 172-210 4.55e-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: 4.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1333674270 172 IEVDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVI 210
Cdd:cd04726   161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 176-215 4.57e-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: 4.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1333674270 176 GGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRS 215
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
174-210 6.55e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 40.00  E-value: 6.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1333674270 174 VDGGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVI 210
Cdd:PRK13307  335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
176-221 8.90e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 39.01  E-value: 8.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1333674270 176 GGVGPDTIHKCAEAGANMIVSGSAIMRSEDPRSVISLLRSVCSEAA 221
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
 
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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