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Conserved domains on  [gi|2043882023|ref|XP_002196985|]
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ribulose-phosphate 3-epimerase isoform X2 [Taeniopygia guttata]

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 ...
 7-214 2.91e-118

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: 335.22  E-value: 2.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgqEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAKA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRTQ 166
Cdd:cd00429    80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2043882023 167 FP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 214
Cdd:cd00429   160 IPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 7-214 2.91e-118

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: 335.22  E-value: 2.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgqEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAKA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRTQ 166
Cdd:cd00429    80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2043882023 167 FP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 214
Cdd:cd00429   160 IPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-216 3.14e-110

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 315.77  E-value: 3.14e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgQEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEA-ADNPGALIKDIRENGMKVGLAIKPGTTVEHLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVQWL 163
Cdd:PTZ00170   88 GASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2043882023 164 RTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNV 216
Cdd:PTZ00170  168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-220 1.19e-101

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: 293.52  E-value: 1.19e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   5 CRIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRlgQEPFFDMHMMVAAPEQWVKPMA 84
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  85 VAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLR 164
Cdd:COG0036    79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023 165 TQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 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 1.08e-79

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: 237.23  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   6 RIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRlgQEPFFDMHMMVAAPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  86 AGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2043882023 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 2.90e-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: 2.90e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgqEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2043882023 166 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 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 ...
 7-214 2.91e-118

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: 335.22  E-value: 2.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgqEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAKA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRTQ 166
Cdd:cd00429    80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2043882023 167 FP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 214
Cdd:cd00429   160 IPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-216 3.14e-110

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 315.77  E-value: 3.14e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgQEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDFAKA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEA-ADNPGALIKDIRENGMKVGLAIKPGTTVEHLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKVQWL 163
Cdd:PTZ00170   88 GASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2043882023 164 RTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNV 216
Cdd:PTZ00170  168 RKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-223 2.27e-102

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 295.76  E-value: 2.27e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   1 MASGCRIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLGQepFFDMHMMVAAPEQWV 80
Cdd:PLN02334    4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDA--PLDCHLMVTNPEDYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  81 KPMAVAGANQYTFHLEAA--DNPGALIKDIRENGMKVGLAIKPGTTVEHLAPW--ANQIDMALVMTVEPGFGGQKFMEDM 156
Cdd:PLN02334   82 PDFAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFGGQSFIPSM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043882023 157 MPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEAAQK 223
Cdd:PLN02334  162 MDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-220 1.19e-101

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: 293.52  E-value: 1.19e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   5 CRIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRlgQEPFFDMHMMVAAPEQWVKPMA 84
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIEAFA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  85 VAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLR 164
Cdd:COG0036    79 EAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023 165 TQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 220
Cdd:COG0036   159 ELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 6-215 2.34e-95

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 277.84  E-value: 2.34e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   6 RIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKrLGQEPFfDMHMMVAAPEQWVKPMAV 85
Cdd:PRK05581    5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPDRYVPDFAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  86 AGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLR- 164
Cdd:PRK05581   83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRk 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2043882023 165 ---TQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRN 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 1.08e-79

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: 237.23  E-value: 1.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   6 RIGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRlgQEPFFDMHMMVAAPEQWVKPMAV 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  86 AGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRT 165
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2043882023 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 2.90e-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: 2.90e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLgqEPFFDMHMMVAAPEQWVKPMAVA 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRT- 165
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2043882023 166 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 214
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 7-198 5.95e-45

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 149.76  E-value: 5.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSrMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKrLGQEPFfDMHMMVAAPEQWVKPMAVA 86
Cdd:PRK09722    5 ISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQDYIDQLADA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  87 GANQYTFHLEAADNPG-ALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKV----Q 161
Cdd:PRK09722   82 GADFITLHPETINGQAfRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIaelkA 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2043882023 162 WLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGS 198
Cdd:PRK09722  162 LRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-210 2.27e-35

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 124.76  E-value: 2.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   9 PSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLRKRLGQEPFFdmHMMVAAPEQWVKPMAVAGA 88
Cdd:PRK08005    5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  89 NQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRTQFP 168
Cdd:PRK08005   83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2043882023 169 SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 210
Cdd:PRK08005  163 AAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 7-205 2.10e-15

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 72.22  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023   7 IGPSILNSDLAALGAECSRMLDCGADYLHLDVMDGHFVPNITFGHPVVESLrkrlgQEPFF-DMHMMVAAPEQWVKPMAV 85
Cdd:PRK08091   15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQF-----PTHCFkDVHLMVRDQFEVAKACVA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  86 AGANQYTFHLEAADNPGALIKDIRENGMKV--GLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWL 163
Cdd:PRK08091   90 AGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQV 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2043882023 164 RTQFPSLD----IEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSAD 205
Cdd:PRK08091  170 ENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 34-211 1.85e-10

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 58.93  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023  34 LHLDVMDGHFVPNITFGHPVVeslrKRLGQEPFFDMHMMVAapEQWVKPMAVAGANQYTFHLEAADNP---------GAL 104
Cdd:PRK14057   49 LHLDLMDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACVKAGAHCITLQAEGDIhlhhtlswlGQQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882023 105 IKDIRENGMKV--GLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVQWLRTQFPSLD----IEVDGGV 178
Cdd:PRK14057  123 TVPVIGGEMPVirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSL 202

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2043882023 179 GPDTIHKCAEAGANMIVSGSAIMKsaDPRSVIN 211
Cdd:PRK14057  203 TQDQLPSLIAQGIDRVVSGSALFR--DDRLVEN 233
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 172-210 3.11e-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: 43.34  E-value: 3.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2043882023 172 IEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 210
Cdd:cd04726   161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 176-220 3.58e-05

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: 43.25  E-value: 3.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2043882023 176 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 220
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 176-214 6.81e-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: 42.12  E-value: 6.81e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2043882023 176 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 214
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
174-210 5.98e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 40.38  E-value: 5.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2043882023 174 VDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 210
Cdd:PRK13307  335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
176-221 2.57e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 37.85  E-value: 2.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2043882023 176 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEAA 221
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 154-200 3.42e-03

Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold.


Pssm-ID: 396337  Cd Length: 169  Bit Score: 36.91  E-value: 3.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2043882023 154 EDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 200
Cdd:pfam01729 112 EEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 154-198 4.77e-03

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 37.07  E-value: 4.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2043882023 154 EDMMPKVQWLRtQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGS 198
Cdd:cd01568   213 EELKEAVKLLK-GLPRVLLEASGGITLENIRAYAETGVDVISTGA 256
 
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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