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Conserved domains on  [gi|568906784|ref|XP_006496251|]
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ribulose-phosphate 3-epimerase isoform X1 [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 ...
6-217 1.96e-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: 323.28  E-value: 1.96e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKP 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDV--MDG-HFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:cd00429   76 FAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906784 166 LRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:cd00429  156 LRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
6-217 1.96e-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: 323.28  E-value: 1.96e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKP 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDV--MDG-HFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:cd00429   76 FAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906784 166 LRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:cd00429  156 LRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
7-219 2.48e-104

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 300.75  E-value: 2.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQWVKPM 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDV--MDG-HFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  87 AVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKV 163
Cdd:PTZ00170  85 AKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906784 164 HWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 219
Cdd:PTZ00170 165 RELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
5-223 2.81e-97

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: 282.74  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVK 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDV--MDG-HFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  85 PMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVH 164
Cdd:COG0036   76 AFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568906784 165 WLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 223
Cdd:COG0036  156 RLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
6-203 2.11e-74

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: 223.75  E-value: 2.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDAPCSsgrHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKP 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDG---HFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:pfam00834  76 FAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568906784  166 LRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 203
Cdd:pfam00834 156 VRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
7-217 1.33e-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: 219.84  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcsSGRHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPM 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDV---MDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   87 AVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 166
Cdd:TIGR01163  76 AEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568906784  167 RT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:TIGR01163 156 RKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
6-217 1.96e-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: 323.28  E-value: 1.96e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPEQWVKP 85
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDV--MDG-HFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:cd00429   76 FAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906784 166 LRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:cd00429  156 LRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
7-219 2.48e-104

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 300.75  E-value: 2.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQLgQDPFFDMHMMVSRPEQWVKPM 86
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDV--MDG-HFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKWVDDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  87 AVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTTVEYLAP--WANQIDMALVMTVEPGFGGQKFMEDMMPKV 163
Cdd:PTZ00170  85 AKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDMMPKV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568906784 164 HWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNV 219
Cdd:PTZ00170 165 RELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
1-226 5.73e-98

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 284.97  E-value: 5.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   1 MASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDApcsSGRHFVPNITFGHPVVESLRKQLgqDPFFDMHMMVSRPE 80
Cdd:PLN02334   4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDV---MDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  81 QWVKPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPW--ANQIDMALVMTVEPGFGGQKFM 156
Cdd:PLN02334  79 DYVPDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFGGQSFI 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784 157 EDMMPKVHWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAAQK 226
Cdd:PLN02334 159 PSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
5-223 2.81e-97

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: 282.74  E-value: 2.81e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   5 CKIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVK 84
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDV--MDG-HFVPNLTFGPPVVKALRKH--TDLPLDVHLMIENPDRYIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  85 PMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVH 164
Cdd:COG0036   76 AFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIR 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568906784 165 WLRTQF----PTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 223
Cdd:COG0036  156 RLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
6-218 4.25e-87

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 257.03  E-value: 4.25e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDApcSSGrHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPEQWVKP 85
Cdd:PRK05581   5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDV--MDG-HFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPDRYVPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:PRK05581  80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568906784 166 LR----TQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRN 218
Cdd:PRK05581 160 LRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
6-203 2.11e-74

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: 223.75  E-value: 2.11e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784    6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDAPCSsgrHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKP 85
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDG---HFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   86 MAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:pfam00834  76 FAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568906784  166 LRTQFP----TLDIEVDGGVGPDTVQKCAEAGANMIVSGSAI 203
Cdd:pfam00834 156 VRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
7-217 1.33e-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: 219.84  E-value: 1.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784    7 IGPSILNSDLANLGAECLRMLDSGADYLHLDApcsSGRHFVPNITFGHPVVESLRKQlgQDPFFDMHMMVSRPEQWVKPM 86
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDV---MDGHFVPNLTFGPPVLEALRKY--TDLPIDVHLMVENPDRYIEDF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   87 AVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWL 166
Cdd:TIGR01163  76 AEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568906784  167 RT----QFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:TIGR01163 156 RKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
6-201 1.74e-40

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 138.20  E-value: 1.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGaECLRMLDSGADYLHLDapCSSGrHFVPNITFGHPVVESLRKqLGQDPFfDMHMMVSRPEQWVKP 85
Cdd:PRK09722   4 KISPSLMCMDLLKFK-EQIEFLNSKADYFHID--IMDG-HFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQDYIDQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEaTENPGA--LIKDIRENGMKVGLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKV 163
Cdd:PRK09722  78 LADAGADFITLHPE-TINGQAfrLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKI 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 568906784 164 ----HWLRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGS 201
Cdd:PRK09722 157 aelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
9-213 1.30e-33

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 120.14  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   9 PSILNSDLANLGAECLRMLDSGADYLHLDAPCSSgrhFVPNITFGHPVVESLRKQLGQDPFFdmHMMVSRPEQWVKPMAV 88
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTS---FINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  89 AGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTTVEylaPW---ANQIDMALVMTVEPGFGGQKFMEDMMPKVHW 165
Cdd:PRK08005  80 IRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLL---PYrylALQLDALMIMTSEPDGRGQQFIAAMCEKVSQ 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568906784 166 LRTQFPTLDIEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 213
Cdd:PRK08005 157 SREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
6-208 1.70e-12

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 64.51  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784   6 KIGPSILNSDLANLGAECLRMLDSGADYLHLDapCSSGRhFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSRPEQWVKP 85
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFD--IADGQ-FSPFFTVGAIAI----KQFPTHCFKDVHLMVRDQFEVAKA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  86 MAVAGANQYTFHLEATENPGALIKDIRENGMKV--GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKV 163
Cdd:PRK08091  87 CVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRV 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568906784 164 HWLRTQFPTLD----IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDD 208
Cdd:PRK08091 167 IQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
34-207 1.13e-06

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 48.14  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784  34 LHLDApcsSGRHFVPNITFGHPVVeslrKQLGQDPFFDMHMMVSrpEQWVKPMAV--AGANQYTFHLEATENPGALIKDI 111
Cdd:PRK14057  49 LHLDL---MDGQFCPQFTVGPWAV----GQLPQTFIKDVHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906784 112 RENGMKV---------GLAIKPGTTVEYLAPWANQIDMALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPTLD----IEVD 178
Cdd:PRK14057 120 GQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVID 199
                        170       180
                 ....*....|....*....|....*....
gi 568906784 179 GGVGPDTVQKCAEAGANMIVSGSAIMRSD 207
Cdd:PRK14057 200 GSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
179-223 3.60e-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: 45.95  E-value: 3.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568906784 179 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEA 223
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
179-217 3.95e-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: 3.95e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568906784 179 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLR 217
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
175-213 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 568906784 175 IEVDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 213
Cdd:cd04726  161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
thiE PRK00043
thiamine phosphate synthase;
179-224 1.46e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 41.32  E-value: 1.46e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568906784 179 GGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVINLLRNVCSEAA 224
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
177-213 1.92e-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: 1.92e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 568906784 177 VDGGVGPDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 213
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
183-213 1.72e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 38.43  E-value: 1.72e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568906784  183 PDTVQKCAEAGANMIVSGSAIMRSDDPRAVI 213
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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