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Conserved domains on  [gi|6322341|ref|NP_012414|]
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ribulose-phosphate 3-epimerase RPE1 [Saccharomyces cerevisiae S288C]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10794312)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 3-234 1.02e-121

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


:

Pssm-ID: 240303  Cd Length: 228  Bit Score: 345.05  E-value: 1.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     3 KPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRpgdasntekkptAFFDCHMM 82
Cdd:PTZ00170   6 KAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPN------------TFLDCHLM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    83 VENPEKWVDDFAKCGADQFTFHYEATQD-PLHLVKLIKSKGIKAACAIKPGTSVDVLFEL--APHLDMALVMTVEPGFGG 159
Cdd:PTZ00170  74 VSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPLidTDLVDMVLVMTVEPGFGG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322341   160 QKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSR 234
Cdd:PTZ00170 154 QSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKHLSKR 228
 
Name Accession Description Interval E-value
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 3-234 1.02e-121

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 345.05  E-value: 1.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     3 KPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRpgdasntekkptAFFDCHMM 82
Cdd:PTZ00170   6 KAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPN------------TFLDCHLM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    83 VENPEKWVDDFAKCGADQFTFHYEATQD-PLHLVKLIKSKGIKAACAIKPGTSVDVLFEL--APHLDMALVMTVEPGFGG 159
Cdd:PTZ00170  74 VSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPLidTDLVDMVLVMTVEPGFGG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322341   160 QKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSR 234
Cdd:PTZ00170 154 QSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKHLSKR 228
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-224 1.23e-116

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: 331.75  E-value: 1.23e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    5 IIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVprpgdasntekkpTAFFDCHMMVE 84
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-------------DLPLDVHLMVE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFME 164
Cdd:cd00429  68 NPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIP 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322341  165 DMMPKVETLRAKFP----HLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMK 224
Cdd:cd00429 148 EVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 4-229 1.65e-109

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: 313.94  E-value: 1.65e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    4 PIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRrsvprpgdasnteKKPTAFFDCHMMV 83
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALR-------------KHTDLPLDVHLMI 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   84 ENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFM 163
Cdd:COG0036  68 ENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFI 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341  164 EDMMPKVETLRAKFPHLN----IQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSK 229
Cdd:COG0036 148 PSVLEKIRRLRELIDERGldilIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAA 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-224 3.55e-87

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: 256.82  E-value: 3.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341      6 IAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVprpgdasntekkpTAFFDCHMMVEN 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT-------------DLPIDVHLMVEN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     86 PEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMED 165
Cdd:TIGR01163  68 PDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322341    166 MMPKVETLRA----KFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMK 224
Cdd:TIGR01163 148 TLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 5-211 2.50e-84

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: 249.17  E-value: 2.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341      5 IIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPgdasntekkptafFDCHMMVE 84
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLP-------------LDVHLMVE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFME 164
Cdd:pfam00834  68 EPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIP 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6322341    165 DMMPKVETLRAKFP----HLNIQVDGGLGKETIPKAAKAGANVIVAGTSVF 211
Cdd:pfam00834 148 SVLEKIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 3-234 1.02e-121

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 345.05  E-value: 1.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     3 KPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRpgdasntekkptAFFDCHMM 82
Cdd:PTZ00170   6 KAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPN------------TFLDCHLM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    83 VENPEKWVDDFAKCGADQFTFHYEATQD-PLHLVKLIKSKGIKAACAIKPGTSVDVLFEL--APHLDMALVMTVEPGFGG 159
Cdd:PTZ00170  74 VSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPLidTDLVDMVLVMTVEPGFGG 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322341   160 QKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSR 234
Cdd:PTZ00170 154 QSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKHLSKR 228
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-224 1.23e-116

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: 331.75  E-value: 1.23e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    5 IIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVprpgdasntekkpTAFFDCHMMVE 84
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-------------DLPLDVHLMVE 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFME 164
Cdd:cd00429  68 NPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIP 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322341  165 DMMPKVETLRAKFP----HLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMK 224
Cdd:cd00429 148 EVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 4-229 1.65e-109

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: 313.94  E-value: 1.65e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    4 PIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRrsvprpgdasnteKKPTAFFDCHMMV 83
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALR-------------KHTDLPLDVHLMI 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   84 ENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFM 163
Cdd:COG0036  68 ENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFI 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341  164 EDMMPKVETLRAKFPHLN----IQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSK 229
Cdd:COG0036 148 PSVLEKIRRLRELIDERGldilIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAA 217
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-229 2.64e-106

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 306.16  E-value: 2.64e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     1 MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRrsvprpgdasnteKKPTAFFDCH 80
Cdd:PLN02334   5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALR-------------KHTDAPLDCH 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    81 MMVENPEKWVDDFAKCGADQFTFHYEATQDP-LH-LVKLIKSKGIKAACAIKPGTSVDVLFEL--APHLDMALVMTVEPG 156
Cdd:PLN02334  72 LMVTNPEDYVPDFAKAGASIFTFHIEQASTIhLHrLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEPG 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322341   157 FGGQKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSK 229
Cdd:PLN02334 152 FGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEK 224
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-226 2.71e-103

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 298.25  E-value: 2.71e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     1 MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPgdasntekkptafFDCH 80
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLP-------------LDVH 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    81 MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ 160
Cdd:PRK05581  68 LMVENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   161 KFMEDMMPKVETLR----AKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEE 226
Cdd:PRK05581 148 KFIPEVLEKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAE 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-224 3.55e-87

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: 256.82  E-value: 3.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341      6 IAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVprpgdasntekkpTAFFDCHMMVEN 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYT-------------DLPIDVHLMVEN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     86 PEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMED 165
Cdd:TIGR01163  68 PDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322341    166 MMPKVETLRA----KFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMK 224
Cdd:TIGR01163 148 TLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 5-211 2.50e-84

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: 249.17  E-value: 2.50e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341      5 IIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPgdasntekkptafFDCHMMVE 84
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLP-------------LDVHLMVE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFME 164
Cdd:pfam00834  68 EPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIP 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6322341    165 DMMPKVETLRAKFP----HLNIQVDGGLGKETIPKAAKAGANVIVAGTSVF 211
Cdd:pfam00834 148 SVLEKIRKVRKMIDerglDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 3-216 1.69e-46

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 154.00  E-value: 1.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     3 KPIIAPSILASDFANLGcECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPgdasntekkptafFDCHMM 82
Cdd:PRK09722   2 RMKISPSLMCMDLLKFK-EQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKP-------------LDVHLM 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    83 VENPEKWVDDFAKCGADQFTFHYE-ATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQK 161
Cdd:PRK09722  68 VTDPQDYIDQLADAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   162 FMEDMMPKVETLRA----KFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTS-VFTAADP 216
Cdd:PRK09722 148 FIPEMLDKIAELKAlrerNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSgLFNLDED 207
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
5-215 1.17e-30

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 112.82  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     5 IIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPgdasntekkptafFDCHMMVE 84
Cdd:PRK08005   2 ILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHP-------------LSFHLMVS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFME 164
Cdd:PRK08005  69 SPQRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIA 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6322341   165 DMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAAD 215
Cdd:PRK08005 149 AMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTAN 199
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 6-215 2.41e-10

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 58.73  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341     6 IAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGqpivtslrrsvprpgdASNTEKKPTAFF-DCHMMVE 84
Cdd:PRK08091  15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVG----------------AIAIKQFPTHCFkDVHLMVR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    85 NPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAAC--AIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKF 162
Cdd:PRK08091  79 DQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVLIglCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322341   163 MEDMMPKVETLRAKFPHLN----IQVDGGLGKETIPKAAKAGANVIVAGTSVFTAAD 215
Cdd:PRK08091 159 SDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 33-211 1.42e-09

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 56.62  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341    33 LHIDVMDGHFVPNITLGQPIVTSLrrsvprpgdasntekkPTAFF-DCHMMVENPEKWVDDFAKCGADQFTFHYEATQDP 111
Cdd:PRK14057  49 LHLDLMDGQFCPQFTVGPWAVGQL----------------PQTFIkDVHLMVADQWTAAQACVKAGAHCITLQAEGDIHL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322341   112 LHLVKLIKSKGIKA---------ACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMEDMMPKVETLRA----KFP 178
Cdd:PRK14057 113 HHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCllgdKRE 192

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6322341   179 HLNIQVDGGLGKETIPKAAKAGANVIVAGTSVF 211
Cdd:PRK14057 193 GKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 170-219 1.66e-03

ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide.


Pssm-ID: 238807 [Multi-domain]  Cd Length: 272  Bit Score: 38.82  E-value: 1.66e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6322341  170 VETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVagTSVFTAADPHDV 219
Cdd:cd01573 221 VPKLRSLAPPVLLAAAGGINIENAAAYAAAGADILV--TSAPYYAKPADI 268
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 170-216 2.09e-03

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: 37.95  E-value: 2.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6322341  170 VETLRAKFPHLN--IQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADP 216
Cdd:cd04726 147 EDDLKKVKKLLGvkVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADP 195
 
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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