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Conserved domains on  [gi|1285902373|gb|ATZ76205|]
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ribulose-5-phosphate 3-epimerase [uncultured euryarchaeote]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10784968)

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
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
34-250 8.14e-104

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: 300.07  E-value: 8.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:COG0036     2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERL 193
Cdd:COG0036    82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1285902373 194 DRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEG 250
Cdd:COG0036   162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
34-250 8.14e-104

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: 300.07  E-value: 8.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:COG0036     2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERL 193
Cdd:COG0036    82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1285902373 194 DRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEG 250
Cdd:COG0036   162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
35-244 4.05e-95

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: 277.82  E-value: 4.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAGG 114
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 115 DSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLD 194
Cdd:cd00429    82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1285902373 195 RIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLR 244
Cdd:cd00429   162 ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
31-246 2.72e-87

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 258.19  E-value: 2.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  31 RKLRLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFR 110
Cdd:PRK05581    2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 111 KAGGDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSAR 190
Cdd:PRK05581   82 KAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1285902373 191 ERLDRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRAS 246
Cdd:PRK05581  162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAE 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
35-244 1.43e-82

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: 246.03  E-value: 1.43e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAGG 114
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 115 DSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLD 194
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1285902373 195 RIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLR 244
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
34-231 1.55e-77

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: 232.99  E-value: 1.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERL 193
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1285902373 194 DRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVF 231
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
34-250 8.14e-104

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: 300.07  E-value: 8.14e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:COG0036     2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERL 193
Cdd:COG0036    82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1285902373 194 DRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEG 250
Cdd:COG0036   162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
35-244 4.05e-95

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: 277.82  E-value: 4.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAGG 114
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 115 DSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLD 194
Cdd:cd00429    82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1285902373 195 RIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLR 244
Cdd:cd00429   162 ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
31-246 2.72e-87

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 258.19  E-value: 2.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  31 RKLRLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFR 110
Cdd:PRK05581    2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 111 KAGGDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSAR 190
Cdd:PRK05581   82 KAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1285902373 191 ERLDRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRAS 246
Cdd:PRK05581  162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAE 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
35-244 1.43e-82

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: 246.03  E-value: 1.43e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAGG 114
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 115 DSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLD 194
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1285902373 195 RIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLR 244
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
34-231 1.55e-77

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: 232.99  E-value: 1.55e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERL 193
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1285902373 194 DRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVF 231
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
34-251 2.50e-74

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 225.65  E-value: 2.50e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  34 RLAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAG 113
Cdd:PLN02334    9 IIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSDPAA--VIREGHRLGATVGAALRPDTPIEAVDRWIEK--LDQVLVMGVHPGFSGQKFIPETVPKIRSA 189
Cdd:PLN02334   89 ASIFTFHIEQASTIHLhrLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMDKVRAL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1285902373 190 RERLDrigsSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEGA 251
Cdd:PLN02334  169 RKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAA 226
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
35-250 9.20e-73

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 221.78  E-value: 9.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLP-LDIHLMIDDPLRYLDAFRKAG 113
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 114 GDSLVFHLECRSD-PAAVIREGHRLGATVGAALRPDTPIEAVDRWIEK--LDQVLVMGVHPGFSGQKFIPETVPKIRSAR 190
Cdd:PTZ00170   89 ASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRELR 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 191 ERLDRIgssaDLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEG 250
Cdd:PTZ00170  169 KRYPHL----NIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQKH 224
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
32-229 5.55e-51

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 166.32  E-value: 5.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  32 KLRLAPSLLSADFGAIGDAVQTAERGgADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRK 111
Cdd:PRK09722    2 RMKISPSLMCMDLLKFKEQIEFLNSK-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 112 AGGDSLVFHLECRSDPA-AVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSAR 190
Cdd:PRK09722   81 AGADFITLHPETINGQAfRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELK 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1285902373 191 ERLDRIGSSADLSVDGGITPETAILAAEAGATFFVCGNS 229
Cdd:PRK09722  161 ALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTS 199
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
35-245 1.01e-32

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 118.60  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLDAFRKAGG 114
Cdd:PRK08005    3 LHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 115 DSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLd 194
Cdd:PRK08005   83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHF- 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1285902373 195 rigSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRA 245
Cdd:PRK08005  162 ---PAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQFTA 209
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
39-247 8.29e-16

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 74.14  E-value: 8.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  39 LLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRavRARTRLPLDIHLMIDDPLRYLDAFRKAGGDSLV 118
Cdd:PRK08091   19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIK--QFPTHCFKDVHLMVRDQFEVAKACVAAGADIVT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 119 FHLECRSDPAAVIR--EGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGfSGQKFIPETVpkIRSARERLDRI 196
Cdd:PRK08091   97 LQVEQTHDLALTIEwlAKQKTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPR-TGTKAPSDLI--LDRVIQVENRL 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1285902373 197 GSSAD---LSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASV 247
Cdd:PRK08091  174 GNRRVeklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSL 227
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
49-227 1.24e-07

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 50.66  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  49 DAVQTAERGGADAFHLDVMDGHFVPNISFGPALIRAVRARTRLPLDIHLMIDDPLRYLD----AFRKAGGDSLVFHLECR 124
Cdd:cd04722    16 ELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDiaaaAARAAGADGVEIHGAVG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 125 ---SDPAAVIREGHR--LGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPETVPKIRSARERLDRIgss 199
Cdd:cd04722    96 ylaREDLELIRELREavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVP--- 172
                         170       180
                  ....*....|....*....|....*....
gi 1285902373 200 adLSVDGGI-TPETAILAAEAGATFFVCG 227
Cdd:cd04722   173 --VIAGGGInDPEDAAEALALGADGVIVG 199
PRK14057 PRK14057
epimerase; Provisional
35-245 1.72e-07

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 50.84  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373  35 LAPSLLSADFGAIGDAVQTAERGGADAFHLDVMDGHFVPNISFGPAliravrARTRLPL----DIHLMIDDPLRYLDAFR 110
Cdd:PRK14057   22 LSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPW------AVGQLPQtfikDVHLMVADQWTAAQACV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 111 KAG---------GDSLVFHLECRSDPAAVIREGHRLGATVGAALRPDTPIEAVDRWIEKLDQVLVMGVHPGFSGQKFIPE 181
Cdd:PRK14057   96 KAGahcitlqaeGDIHLHHTLSWLGQQTVPVIGGEMPVIRGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSD 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1285902373 182 TVPKIRSARERLDRIGSSADLSVDGGITPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRA 245
Cdd:PRK14057  176 LHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDDRLVENTRSWRA 239
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
131-251 7.31e-04

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 40.39  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1285902373 131 IREGHRLGATVGAAL--RPDTPIEAVDrwIEKLDqVLVMGVHPGFSGQKFIPETVPKIRSARERLdrigsSADLSVDGGI 208
Cdd:PRK07028  100 VRAARKYGVRLMADLinVPDPVKRAVE--LEELG-VDYINVHVGIDQQMLGKDPLELLKEVSEEV-----SIPIAVAGGL 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1285902373 209 TPETAILAAEAGATFFVCGNSVFAGGSVDDNLRRLRASVEEGA 251
Cdd:PRK07028  172 DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGK 214
 
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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