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Conserved domains on  [gi|1570587047|ref|XP_027879776|]
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ribulose-phosphate 3-epimerase isoform X1 [Xiphophorus couchianus]

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 ...
 30-238 3.97e-123

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: 348.70  E-value: 3.97e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1570587047 190 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:cd00429   159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 30-238 3.97e-123

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: 348.70  E-value: 3.97e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1570587047 190 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:cd00429   159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 24-248 1.05e-112

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 323.09  E-value: 1.05e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  24 SMAYSAKIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgQDPFFDMHMMVSRPEQW 103
Cdd:PTZ00170    2 KQPLKAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 104 VKPMAAAGASQYTFHVEATTN-PGNLIKEIRESGMKVGLAIKPGTTVEELAP--WANQVDMALVMTVEPGFGGQKFMEDM 180
Cdd:PTZ00170   81 VDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDM 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570587047 181 MPKVSWLRSQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEAIQKR 248
Cdd:PTZ00170  161 MPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKHLSKR 228
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 30-244 3.60e-107

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: 308.54  E-value: 3.60e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:COG0036     2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMIENPDRYIEAFAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:COG0036    80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1570587047 190 QF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEA 244
Cdd:COG0036   160 LIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 30-225 1.20e-79

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 238.00  E-value: 1.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTvgQDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1570587047 190 QFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAVI 225
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 31-238 5.01e-79

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: 236.79  E-value: 5.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  31 IGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAAA 110
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 111 GASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS- 189
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1570587047 190 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 30-238 3.97e-123

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: 348.70  E-value: 3.97e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:cd00429     1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMVENPERYIEAFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:cd00429    79 AGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1570587047 190 QFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:cd00429   159 LIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 24-248 1.05e-112

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 323.09  E-value: 1.05e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  24 SMAYSAKIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgQDPFFDMHMMVSRPEQW 103
Cdd:PTZ00170    2 KQPLKAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHL-PNTFLDCHLMVSNPEKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 104 VKPMAAAGASQYTFHVEATTN-PGNLIKEIRESGMKVGLAIKPGTTVEELAP--WANQVDMALVMTVEPGFGGQKFMEDM 180
Cdd:PTZ00170   81 VDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPGFGGQSFMHDM 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570587047 181 MPKVSWLRSQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEAIQKR 248
Cdd:PTZ00170  161 MPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKHLSKR 228
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 25-244 2.46e-110

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 316.94  E-value: 2.46e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  25 MAYSAKIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWV 104
Cdd:PLN02334    4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHT--DAPLDCHLMVTNPEDYV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 105 KPMAAAGASQYTFHVE--ATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPW--ANQVDMALVMTVEPGFGGQKFMEDM 180
Cdd:PLN02334   82 PDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPGFGGQSFIPSM 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1570587047 181 MPKVSWLRSQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEA 244
Cdd:PLN02334  162 MDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKA 225
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 30-244 3.60e-107

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: 308.54  E-value: 3.60e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:COG0036     2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT--DLPLDVHLMIENPDRYIEAFAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:COG0036    80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1570587047 190 QF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEA 244
Cdd:COG0036   160 LIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 30-242 1.73e-96

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 281.69  E-value: 1.73e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKtVGQDPFfDMHMMVSRPEQWVKPMAA 109
Cdd:PRK05581    5 LIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRK-VTKLPL-DVHLMVENPDRYVPDFAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLR- 188
Cdd:PRK05581   83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRk 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1570587047 189 ---SQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVA 242
Cdd:PRK05581  163 lidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELA 219
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 30-225 1.20e-79

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 238.00  E-value: 1.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  30 KIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTvgQDPFFDMHMMVSRPEQWVKPMAA 109
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL--TDLPLDVHLMVEEPDRIIPDFAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 110 AGASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS 189
Cdd:pfam00834  79 AGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1570587047 190 QFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAVI 225
Cdd:pfam00834 159 MIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 31-238 5.01e-79

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: 236.79  E-value: 5.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  31 IGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVgqDPFFDMHMMVSRPEQWVKPMAAA 110
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT--DLPIDVHLMVENPDRYIEDFAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 111 GASQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRS- 189
Cdd:TIGR01163  79 GADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKm 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1570587047 190 ---QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:TIGR01163 159 ideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 28-222 3.05e-47

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 156.31  E-value: 3.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  28 SAKIGPSILSSDLSCLGsECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKtVGQDPFfDMHMMVSRPEQWVKPM 107
Cdd:PRK09722    2 RMKISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKK-LASKPL-DVHLMVTDPQDYIDQL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 108 AAAGASQYTFHVEATTNPG-NLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSW 186
Cdd:PRK09722   79 ADAGADFITLHPETINGQAfRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1570587047 187 LRS--QFPSLD--IEVDGGVGPDTIHKCAEAGANMIVSGS 222
Cdd:PRK09722  159 LKAlrERNGLEylIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
33-235 5.82e-34

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 121.68  E-value: 5.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  33 PSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLRKTVGQDPFFdmHMMVSRPEQWVKPMAAAGA 112
Cdd:PRK08005    5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSF--HLMVSSPQRWLPWLAAIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 113 SQYTFHVEATTNPGNLIKEIRESGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVSWLRSQFP 192
Cdd:PRK08005   83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1570587047 193 SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIA 235
Cdd:PRK08005  163 AAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLS 205
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 28-229 2.81e-18

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 80.69  E-value: 2.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  28 SAKIGPSILSSDLSCLGSECVRMMECGADYLHLDVMDGHFVPNITFGHPMVECLrktvgQDPFF-DMHMMVSRPEQWVKP 106
Cdd:PRK08091   12 QQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQF-----PTHCFkDVHLMVRDQFEVAKA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 107 MAAAGASQYTFHVEATTNPGNLIKEIRE--SGMKVGLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKV 184
Cdd:PRK08091   87 CVAAGADIVTLQVEQTHDLALTIEWLAKqkTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRV 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1570587047 185 SWLRSQFPSLD----IEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDD 229
Cdd:PRK08091  167 IQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 58-240 1.91e-11

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 62.39  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047  58 LHLDVMDGHFVPNITFGHPMVECLRKTVGQdpffDMHMMVSrpEQWVKPMAA--AGASQYTFHVEATTNPGNLIKEIRES 135
Cdd:PRK14057   49 LHLDLMDGQFCPQFTVGPWAVGQLPQTFIK----DVHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWLGQQ 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570587047 136 GMKV---------GLAIKPGTTVEELAPWANQVDMALVMTVEPGFGGQKFMEDMMPKVS----WLRSQFPSLDIEVDGGV 202
Cdd:PRK14057  123 TVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAqllcLLGDKREGKIIVIDGSL 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1570587047 203 GPDTIHKCAEAGANMIVSGSAVIGSD----DPRSVIALLRTA 240
Cdd:PRK14057  203 TQDQLPSLIAQGIDRVVSGSALFRDDrlveNTRSWRAMFKVA 244
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 200-244 3.65e-05

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 43.25  E-value: 3.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1570587047 200 GGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEA 244
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 196-234 4.49e-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: 42.95  E-value: 4.49e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1570587047 196 IEVDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVI 234
Cdd:cd04726   161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 200-238 2.81e-04

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: 40.58  E-value: 2.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1570587047 200 GGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLR 238
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
198-234 1.39e-03

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 39.23  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1570587047 198 VDGGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVI 234
Cdd:PRK13307  335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
200-245 1.86e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 38.24  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1570587047 200 GGVGPDTIHKCAEAGANMIVSGSAVIGSDDPRSVIALLRTAVAEAI 245
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
 
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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