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Conserved domains on  [gi|506949360|ref|NP_001265211|]
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ribulose-phosphate 3-epimerase isoform 2 [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 ...
 1-164 6.94e-78

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: 230.83  E-value: 6.94e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  81 WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDP 156
Cdd:cd00429  124 YLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDY 203


                 ....*...
gi 506949360 157 RSVINLLR 164
Cdd:cd00429  204 AEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 1-164 6.94e-78

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: 230.83  E-value: 6.94e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  81 WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDP 156
Cdd:cd00429  124 YLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDY 203


                 ....*...
gi 506949360 157 RSVINLLR 164
Cdd:cd00429  204 AEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-166 3.69e-69

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 209.46  E-value: 3.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP 80
Cdd:PTZ00170  71 HLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTPVEVLFP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  81 --WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRS 158
Cdd:PTZ00170 133 liDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQ 212


                 ....*...
gi 506949360 159 VINLLRNV 166
Cdd:PTZ00170 213 AIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-170 7.50e-65

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: 197.99  E-value: 7.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW 81
Cdd:COG0036   64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEYV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:COG0036  126 LDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYA 205

                        170
                 ....*....|...
gi 506949360 158 SVINLLRNVCSEA 170
Cdd:COG0036  206 AAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-150 2.63e-47

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: 152.87  E-value: 2.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYL 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506949360   82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 150
Cdd:pfam00834 125 LDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-164 1.56e-46

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: 151.27  E-value: 1.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEYLAPW 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLEFLEYV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:TIGR01163 124 LPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYK 203


                  ....*..
gi 506949360  158 SVINLLR 164
Cdd:TIGR01163 204 EVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 1-164 6.94e-78

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: 230.83  E-value: 6.94e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK------------------AGVALNPGTPVEVLEP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  81 WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDP 156
Cdd:cd00429  124 YLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDY 203


                 ....*...
gi 506949360 157 RSVINLLR 164
Cdd:cd00429  204 AEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-166 3.69e-69

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 209.46  E-value: 3.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAP 80
Cdd:PTZ00170  71 HLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMK------------------VGVAIKPKTPVEVLFP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  81 --WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRS 158
Cdd:PTZ00170 133 liDTDLVDMVLVMTVEPGFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQ 212


                 ....*...
gi 506949360 159 VINLLRNV 166
Cdd:PTZ00170 213 AIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-170 7.50e-65

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: 197.99  E-value: 7.50e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW 81
Cdd:COG0036   64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAK------------------AGVALNPATPLEALEYV 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:COG0036  126 LDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYA 205

                        170
                 ....*....|...
gi 506949360 158 SVINLLRNVCSEA 170
Cdd:COG0036  206 AAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-173 4.94e-64

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 196.38  E-value: 4.94e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLA 79
Cdd:PLN02334  71 HLMVTNPEDYVPDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMK------------------AGVVLNPGTPVEAVE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  80 PW--ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:PLN02334 133 PVveKGLVDMVLVMSVEPGFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYA 212

                        170
                 ....*....|....*.
gi 506949360 158 SVINLLRNVCSEAAQK 173
Cdd:PLN02334 213 EVISGLRASVEKAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 2-165 4.22e-60

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 186.16  E-value: 4.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW 81
Cdd:PRK05581  67 HLMVENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIK------------------AGLVLNPATPLEPLEDV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360  82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLR----TQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:PRK05581 129 LDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYK 208


                 ....*...
gi 506949360 158 SVINLLRN 165
Cdd:PRK05581 209 EAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-150 2.63e-47

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: 152.87  E-value: 2.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLAPW 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAK------------------AGLVLNPATPLDAIEYL 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506949360   82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 150
Cdd:pfam00834 125 LDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-164 1.56e-46

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: 151.27  E-value: 1.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEYLAPW 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKA------------------GIVLNPATPLEFLEYV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPR 157
Cdd:TIGR01163 124 LPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYK 203


                  ....*..
gi 506949360  158 SVINLLR 164
Cdd:TIGR01163 204 EVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-148 5.81e-24

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 93.52  E-value: 5.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEaTENPGA--LIKDIRENGMKscsvtqaevqwhsqgplqVGLAIKPGTSVEYLA 79
Cdd:PRK09722  65 HLMVTDPQDYIDQLADAGADFITLHPE-TINGQAfrLIDEIRRAGMK------------------VGLVLNPETPVESIK 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506949360  80 PWANQIDMALVMTVEPGFGGQKFMEDMMPKV----HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGS 148
Cdd:PRK09722 126 YYIHLLDKITVMTVDPGFAGQPFIPEMLDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
2-160 5.90e-21

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 85.47  E-value: 5.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKScsvtqaevqwhsqgplqvGLAIKPGTSVEYLAPW 81
Cdd:PRK08005  64 HLMVSSPQRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAKA------------------GLALNPATPLLPYRYL 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506949360  82 ANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 160
Cdd:PRK08005 126 ALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 1-155 9.91e-08

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 49.87  E-value: 9.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENgmkscsvtqaevqwhsQGPLQVGLAIKPGTSVEYLAP 80
Cdd:PRK08091  73 VHLMVRDQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQ----------------KTTVLIGLCLCPETPISLLEP 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506949360  81 WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSED 155
Cdd:PRK08091 137 YLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 126-170 2.76e-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: 2.76e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 506949360 126 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 170
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
PRK14057 PRK14057
epimerase; Provisional
 1-154 6.97e-06

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 44.67  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506949360   1 MHMMVSkpEQWVKPMAVAGANQYTFHLEAtENPGALIKDIRENGMKSCSVTQAEVqwhsqgPLQVGLAIKPGTSVEYLAP 80
Cdd:PRK14057  80 VHLMVA--DQWTAAQACVKAGAHCITLQA-EGDIHLHHTLSWLGQQTVPVIGGEM------PVIRGISLCPATPLDVIIP 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506949360  81 WANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSE 154
Cdd:PRK14057 151 ILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 126-164 2.48e-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: 2.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 506949360 126 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 164
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 122-160 3.28e-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: 42.57  E-value: 3.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 506949360 122 IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 160
Cdd:cd04726  161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
124-160 1.49e-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: 1.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 506949360 124 VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 160
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
126-171 2.15e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 40.17  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 506949360 126 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAA 171
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
130-160 4.27e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 36.51  E-value: 4.27e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 506949360  130 PDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 160
Cdd:pfam00218 220 PADVRELKEHGANAFLVGESLMRQEDVRAAI 250
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 104-150 5.92e-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: 35.75  E-value: 5.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 506949360  104 EDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 150
Cdd:pfam01729 112 EEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
 
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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