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Conserved domains on  [gi|890778124|ref|NP_001297571|]
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ribulose-phosphate 3-epimerase isoform 1 [Mus musculus]

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 ...
 6-221 4.05e-113

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: 322.51  E-value: 4.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapcssgrsVF-LHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPE 84
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHID--------VMdGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:cd00429   71 RYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890778124 165 PKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:cd00429  151 EKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-221 4.05e-113

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: 322.51  E-value: 4.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapcssgrsVF-LHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPE 84
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHID--------VMdGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:cd00429   71 RYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890778124 165 PKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:cd00429  151 EKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-223 4.84e-104

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 300.36  E-value: 4.84e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcssgrsVFLHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQW 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDV-------MDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  87 VKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDM 163
Cdd:PTZ00170  81 VDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124 164 MPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 223
Cdd:PTZ00170 161 MPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-227 1.34e-96

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: 280.81  E-value: 1.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrsvflHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPE 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDV--MDG-----HFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:COG0036   72 RYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890778124 165 PKVHWLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 227
Cdd:COG0036  152 EKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-207 1.24e-73

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: 222.21  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDAPCSsgrsvflHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQ 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDG-------HFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   86 WVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMP 165
Cdd:pfam00834  72 IIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 890778124  166 KVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 207
Cdd:pfam00834 152 KIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-221 7.70e-72

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: 217.91  E-value: 7.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrsvflHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQW 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDV--MDG-----HFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   87 VKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPK 166
Cdd:TIGR01163  72 IEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEK 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 890778124  167 VHWLRT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:TIGR01163 152 IREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 6-221 4.05e-113

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: 322.51  E-value: 4.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapcssgrsVF-LHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPE 84
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHID--------VMdGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:cd00429   71 RYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890778124 165 PKVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:cd00429  151 EKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 7-223 4.84e-104

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 300.36  E-value: 4.84e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcssgrsVFLHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQW 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDV-------MDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  87 VKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDM 163
Cdd:PTZ00170  81 VDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124 164 MPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 223
Cdd:PTZ00170 161 MPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-230 1.95e-97

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 283.43  E-value: 1.95e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDapcssgrsVF-LHFVPNITFGHPVVESLRKQLgqDPFFDMHMM 79
Cdd:PLN02334   4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVD--------VMdGHFVPNLTIGPPVVKALRKHT--DAPLDCHLM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  80 VSRPEQWVKPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPW--ANQIDMALVMTVEPGFG 155
Cdd:PLN02334  74 VTNPEDYVPDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 890778124 156 GQKFMEDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAAQK 230
Cdd:PLN02334 154 GQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-227 1.34e-96

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: 280.81  E-value: 1.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrsvflHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPE 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDV--MDG-----HFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:COG0036   72 RYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890778124 165 PKVHWLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 227
Cdd:COG0036  152 EKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 6-222 9.21e-87

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 256.26  E-value: 9.21e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapcssgrsVF-LHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPE 84
Cdd:PRK05581   5 LIAPSILSADFARLGEEVKAVEAAGADWIHVD--------VMdGHFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  85 QWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMM 164
Cdd:PRK05581  75 RYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 890778124 165 PKVHWLR----TQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRN 222
Cdd:PRK05581 155 EKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-207 1.24e-73

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: 222.21  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDAPCSsgrsvflHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQ 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDG-------HFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   86 WVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMP 165
Cdd:pfam00834  72 IIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 890778124  166 KVHWLRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 207
Cdd:pfam00834 152 KIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 7-221 7.70e-72

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: 217.91  E-value: 7.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrsvflHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQW 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDV--MDG-----HFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRY 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   87 VKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPK 166
Cdd:TIGR01163  72 IEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEK 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 890778124  167 VHWLRT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:TIGR01163 152 IREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 6-205 7.87e-40

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 136.66  E-value: 7.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDapCSSGrsvflHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPEQ 85
Cdd:PRK09722   4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHID--IMDG-----HFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  86 WVKPMAVAGANQYTFHLEaTENPGA--LIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDM 163
Cdd:PRK09722  74 YIDQLADAGADFITLHPE-TINGQAfrLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEM 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 890778124 164 MPKV----HWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGS 205
Cdd:PRK09722 153 LDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-217 5.92e-33

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 118.60  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   9 PSILNSDLANLGAECLRMLDSGADYLHLDAPCSSgrsvflhFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSRPEQWVK 88
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTS-------FINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  89 PMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEylaPW---ANQIDMALVMTVEPGFGGQKFMEDMMP 165
Cdd:PRK08005  76 WLAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLL---PYrylALQLDALMIMTSEPDGRGQQFIAAMCE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 890778124 166 KVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 217
Cdd:PRK08005 153 KVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 6-212 6.47e-12

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 62.97  E-value: 6.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapCSSGRsvflhFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSRPEQ 85
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFD--IADGQ-----FSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  86 WVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKV--GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDM 163
Cdd:PRK08091  83 VAKACVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLI 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 890778124 164 MPKVHWLRTQFPTLD----IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDD 212
Cdd:PRK08091 163 LDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 49-211 1.77e-06

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 47.76  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124  49 HFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSrpEQWVKPMAV--AGANQYTFHLEATENPGALIKDIRENGMKV---- 122
Cdd:PRK14057  57 QFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWLGQQTVPVigge 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890778124 123 -----GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLD----IEVDGGVGPDTVQKC 193
Cdd:PRK14057 131 mpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSLTQDQLPSL 210

                        170
                 ....*....|....*...
gi 890778124 194 AEAGANMIVSGSAIMRSD 211
Cdd:PRK14057 211 IAQGIDRVVSGSALFRDD 228
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 183-227 3.57e-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: 3.57e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 890778124 183 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 227
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 183-221 4.11e-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: 4.11e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 890778124 183 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 221
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 179-217 2.34e-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: 2.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 890778124 179 IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 217
Cdd:cd04726  161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
thiE PRK00043
thiamine phosphate synthase;
183-228 1.45e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 41.71  E-value: 1.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 890778124 183 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAA 228
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
181-217 1.97e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 41.92  E-value: 1.97e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 890778124 181 VDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 217
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
187-217 1.78e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 38.43  E-value: 1.78e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 890778124  187 PDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 217
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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