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Conserved domains on  [gi|1958803699|ref|XP_038940025|]
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ribulose-phosphate 3-epimerase isoform X7 [Rattus norvegicus]

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 ...
 12-166 1.55e-80

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: 237.76  E-value: 1.55e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:cd00429    58 LPLDVHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK-----AGVALNPGTPVEVLEPYLDEVDLVL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:cd00429   133 VMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 12-166 1.55e-80

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: 237.76  E-value: 1.55e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:cd00429    58 LPLDVHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK-----AGVALNPGTPVEVLEPYLDEVDLVL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:cd00429   133 VMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 14-168 1.04e-72

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 218.70  E-value: 1.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAP--WANQIDMA 90
Cdd:PTZ00170   68 LDCHLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMK-----VGVAIKPKTPVEVLFPliDTDLVDMV 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958803699  91 LVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 168
Cdd:PTZ00170  143 LVMTVEPGFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 14-172 3.38e-67

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: 204.15  E-value: 3.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMALVM 93
Cdd:COG0036    61 LDVHLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAK-----AGVALNPATPLEALEYVLDDVDLVLVM 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  94 TVEPGFGGQKFMEDMMPKVHWLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVC 169
Cdd:COG0036   136 SVNPGFGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAA 215


                  ...
gi 1958803699 170 SEA 172
Cdd:COG0036   216 AAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 14-152 7.05e-50

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: 159.42  E-value: 7.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMALVM 93
Cdd:pfam00834  60 LDVHLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAK-----AGLVLNPATPLDAIEYLLDKLDLVLLM 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958803699  94 TVEPGFGGQKFMEDMMPKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 152
Cdd:pfam00834 135 SVNPGFGGQSFIPSVLEKIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 12-166 9.09e-50

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: 159.75  E-value: 9.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:TIGR01163  57 LPIDVHLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAK-----AGIVLNPATPLEFLEYVLPDVDLVL 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLRT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:TIGR01163 132 LMSVNPGFGGQKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 12-166 1.55e-80

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: 237.76  E-value: 1.55e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:cd00429    58 LPLDVHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMK-----AGVALNPGTPVEVLEPYLDEVDLVL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:cd00429   133 VMSVNPGFGGQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 14-168 1.04e-72

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 218.70  E-value: 1.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAP--WANQIDMA 90
Cdd:PTZ00170   68 LDCHLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMK-----VGVAIKPKTPVEVLFPliDTDLVDMV 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958803699  91 LVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 168
Cdd:PTZ00170  143 LVMTVEPGFGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 14-175 4.79e-68

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 206.78  E-value: 4.79e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPW--ANQIDM 89
Cdd:PLN02334   68 LDCHLMVTNPEDYVPDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMK-----AGVVLNPGTPVEAVEPVveKGLVDM 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  90 ALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVC 169
Cdd:PLN02334  143 VLVMSVEPGFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASV 222


                  ....*.
gi 1958803699 170 SEAAQK 175
Cdd:PLN02334  223 EKAAVA 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 14-172 3.38e-67

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: 204.15  E-value: 3.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMALVM 93
Cdd:COG0036    61 LDVHLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAK-----AGVALNPATPLEALEYVLDDVDLVLVM 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  94 TVEPGFGGQKFMEDMMPKVHWLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVC 169
Cdd:COG0036   136 SVNPGFGGQKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAA 215


                  ...
gi 1958803699 170 SEA 172
Cdd:COG0036   216 AAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 12-167 4.10e-62

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 191.17  E-value: 4.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:PRK05581   62 LPLDVHLMVENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIK-----AGLVLNPATPLEPLEDVLDLLDLVL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLR----TQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRN 167
Cdd:PRK05581  137 LMSVNPGFGGQKFIPEVLEKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 14-152 7.05e-50

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: 159.42  E-value: 7.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMALVM 93
Cdd:pfam00834  60 LDVHLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAK-----AGLVLNPATPLDAIEYLLDKLDLVLLM 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958803699  94 TVEPGFGGQKFMEDMMPKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 152
Cdd:pfam00834 135 SVNPGFGGQSFIPSVLEKIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 12-166 9.09e-50

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: 159.75  E-value: 9.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  12 LDLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:TIGR01163  57 LPIDVHLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAK-----AGIVLNPATPLEFLEYVLPDVDLVL 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKVHWLRT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:TIGR01163 132 LMSVNPGFGGQKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 14-150 1.38e-27

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 103.15  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEaTENPGA--LIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMAL 91
Cdd:PRK09722   62 LDVHLMVTDPQDYIDQLADAGADFITLHPE-TINGQAfrLIDEIRRAGMK-----VGLVLNPETPVESIKYYIHLLDKIT 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958803699  92 VMTVEPGFGGQKFMEDMMPKV----HWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGS 150
Cdd:PRK09722  136 VMTVDPGFAGQPFIPEMLDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
14-162 1.85e-24

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 94.72  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  14 LDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKhcllqVGLAIKPGTTVEYLAPWANQIDMALVM 93
Cdd:PRK08005   61 LSFHLMVSSPQRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAK-----AGLALNPATPLLPYRYLALQLDALMIM 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958803699  94 TVEPGFGGQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 162
Cdd:PRK08005  136 TSEPDGRGQQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 5-157 9.38e-13

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 64.13  E-value: 9.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699   5 YPTHFFfldLDMHMMVSRPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENgmKHCLLqVGLAIKPGTTVEYLAPWA 84
Cdd:PRK08091   65 FPTHCF---KDVHLMVRDQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQ--KTTVL-IGLCLCPETPISLLEPYL 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803699  85 NQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLD----IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDD 157
Cdd:PRK08091  139 DQIDLIQILTLDPRTGTKAPSDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 128-172 1.41e-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: 46.33  E-value: 1.41e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958803699 128 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 172
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 128-166 2.04e-06

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: 45.97  E-value: 2.04e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958803699 128 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 166
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 124-162 1.13e-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: 43.72  E-value: 1.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1958803699 124 IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 162
Cdd:cd04726   161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
thiE PRK00043
thiamine phosphate synthase;
128-173 6.07e-05

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 41.71  E-value: 6.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958803699 128 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAA 173
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
126-162 1.09e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 41.54  E-value: 1.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958803699 126 VDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 162
Cdd:PRK13307  335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
PRK14057 PRK14057
epimerase; Provisional
 15-156 1.12e-04

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 41.21  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803699  15 DMHMMVSrpEQWVKPMAVAGANQYTFHLEAtENPGALIKDIRENGMK-------HCLLQVGLAIKPGTTVEYLAPWANQI 87
Cdd:PRK14057   79 DVHLMVA--DQWTAAQACVKAGAHCITLQA-EGDIHLHHTLSWLGQQtvpviggEMPVIRGISLCPATPLDVIIPILSDV 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958803699  88 DMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLD----IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSD 156
Cdd:PRK14057  156 EVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
132-162 9.70e-04

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 38.43  E-value: 9.70e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958803699 132 PDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 162
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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