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Conserved domains on  [gi|504427033|ref|WP_014614135|]
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ribulose-phosphate 3-epimerase [Staphylococcus pseudintermedius]

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

CATH:  3.20.20.70
Gene Ontology:  GO:0006098|GO:0016857|GO:0004750|GO:0046872|GO:0005975
PubMed:  12206759|11257493
SCOP:  4003059

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]; ...
 2-216 9.35e-121

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: 341.29  E-value: 9.35e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   2 TKVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEK 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  82 GVNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDI 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427033 162 RKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAA 215
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-216 9.35e-121

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: 341.29  E-value: 9.35e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   2 TKVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEK 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  82 GVNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDI 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427033 162 RKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAA 215
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-213 1.70e-113

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 322.89  E-value: 1.70e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   3 KVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  83 VNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIR 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504427033 163 KNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLK 213
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-216 1.23e-111

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 318.28  E-value: 1.23e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   1 MTKVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAE 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  81 KGVNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDD 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427033 161 IRKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:PRK05581 163 LIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-213 2.59e-99

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: 286.86  E-value: 2.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033    6 PSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKGVNK 85
Cdd:TIGR01163   3 PSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGADI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   86 ISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIRKNR 165
Cdd:TIGR01163  83 ITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMIDEL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 504427033  166 QLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLK 213
Cdd:TIGR01163 163 GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 3-200 1.30e-88

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: 259.19  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033    3 KVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   83 VNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIR 162
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 504427033  163 KNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-216 9.35e-121

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: 341.29  E-value: 9.35e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   2 TKVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEK 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  82 GVNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDI 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427033 162 RKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAA 215
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-213 1.70e-113

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 322.89  E-value: 1.70e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   3 KVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  83 VNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIR 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504427033 163 KNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLK 213
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-216 1.23e-111

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 318.28  E-value: 1.23e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   1 MTKVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAE 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  81 KGVNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDD 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427033 161 IRKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:PRK05581 163 LIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-213 2.59e-99

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: 286.86  E-value: 2.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033    6 PSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKGVNK 85
Cdd:TIGR01163   3 PSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGADI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   86 ISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIRKNR 165
Cdd:TIGR01163  83 ITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMIDEL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 504427033  166 QLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLK 213
Cdd:TIGR01163 163 GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 3-200 1.30e-88

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: 259.19  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033    3 KVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   83 VNKISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDIR 162
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 504427033  163 KNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 3-216 3.53e-86

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 254.16  E-value: 3.53e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   3 KVFPSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:PLN02334   9 IIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  83 VNKISVHMEGNP--HIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIE--EVDFVLVMSVNPGFGGQAFLPAAVDKIKQL 158
Cdd:PLN02334  89 ASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMDKVRAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427033 159 DdiRKNRQLDfkIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLKGEL 216
Cdd:PLN02334 169 R--KKYPELD--IEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASV 222
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 6-213 1.55e-65

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 201.75  E-value: 1.55e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   6 PSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLP-IDAHLMIETPNDYVEAFAEKGVN 84
Cdd:PTZ00170  11 PSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKAGAS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  85 KISVHMEG-NPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIE--EVDFVLVMSVNPGFGGQAFLPAAVDKIKQLddi 161
Cdd:PTZ00170  91 QFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDtdLVDMVLVMTVEPGFGGQSFMHDMMPKVREL--- 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504427033 162 RKNRQlDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEANQRLK 213
Cdd:PTZ00170 168 RKRYP-HLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLR 218
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 3-197 9.63e-64

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 197.14  E-value: 9.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   3 KVFPSLLSADFLNLKQELTKLEeSGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKG 82
Cdd:PRK09722   4 KISPSLMCMDLLKFKEQIEFLN-SKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  83 VNKISVHMEG-NPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLDDI 161
Cdd:PRK09722  83 ADFITLHPETiNGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKAL 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504427033 162 RKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGS 197
Cdd:PRK09722 163 RERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
6-206 1.68e-35

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 124.38  E-value: 1.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   6 PSLLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKGVNK 85
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  86 ISVHMEGNPHIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLddirknR 165
Cdd:PRK08005  85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQS------R 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504427033 166 QLDFKIE--VDGGINDQTAKQVIEAGADWLVAGSYFFSRADYK 206
Cdd:PRK08005 159 EHFPAAEcwADGGITLRAARLLAAAGAQHLVIGRALFTTANYD 201
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 8-206 1.36e-28

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 106.88  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   8 LLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIG------FPvleairaaTDLPIDAHLMIETPNDYVEAFAEK 81
Cdd:PRK08091  19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGaiaikqFP--------THCFKDVHLMVRDQFEVAKACVAA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  82 GVNKISVHMEGNPHIHRVVQNIKKH--GVEAGVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDKIKQLD 159
Cdd:PRK08091  91 GADIVTLQVEQTHDLALTIEWLAKQktTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVE 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504427033 160 DIRKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYK 206
Cdd:PRK08091 171 NRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELK 217
PRK14057 PRK14057
epimerase; Provisional
 8-211 9.85e-18

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 78.96  E-value: 9.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033   8 LLSADFLNLKQELTKLEESGIDALHFDVMDGQFVPNISIGfpvleaIRAATDLP----IDAHLMIETPNDYVEAFAEKGV 83
Cdd:PRK14057  26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVG------PWAVGQLPqtfiKDVHLMVADQWTAAQACVKAGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  84 NKISVHMEGNPHIHRVVQNIKKHGVEA---------GVVINPGTPVHALDAIIEEVDFVLVMSVNPGFGGQAFLPAAVDK 154
Cdd:PRK14057 100 HCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHER 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427033 155 IKQLDDIRKNRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFsRADYKEANQR 211
Cdd:PRK14057 180 VAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF-RDDRLVENTR 235
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 20-197 1.25e-11

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: 61.45  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  20 LTKLEESGIDALHFDVMDGQFVPNISIGFPVLEAIRAATDLPIDAHLMI----ETPNDYVEAFAEKGVNKISVHMEGNP- 94
Cdd:cd04722   18 AKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAIndaaAAVDIAAAAARAAGADGVEIHGAVGYl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  95 --HIHRVVQNIKKHGVEAGVVINPGTPVHALDAIIEE--VDFVLVMSVNPGFGGQAFLPAAVDKIkqlddIRKNRQLDFK 170
Cdd:cd04722   98 arEDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEagVDEVGLGNGGGGGGGRDAVPIADLLL-----ILAKRGSKVP 172

                        170       180
                 ....*....|....*....|....*...
gi 504427033 171 IEVDGGIND-QTAKQVIEAGADWLVAGS 197
Cdd:cd04722  173 VIAGGGINDpEDAAEALALGADGVIVGS 200
kbaY PRK12738
tagatose-bisphosphate aldolase subunit KbaY;
13-91 8.44e-04

tagatose-bisphosphate aldolase subunit KbaY;


Pssm-ID: 183711  Cd Length: 286  Bit Score: 39.25  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427033  13 FLNLKQELTKLEE-SGIDALHFDV--MDGQFVPNISIGFPVLEAIRAATDLPIDAHLMIETPNDYVEAFAEKGVNKISVH 89
Cdd:PRK12738 153 FLTDPQEAKRFVElTGVDSLAVAIgtAHGLYSKTPKIDFQRLAEIREVVDVPLVLHGASDVPDEFVRRTIELGVTKVNVA 232


                 ..
gi 504427033  90 ME 91
Cdd:PRK12738 233 TE 234
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 171-213 6.79e-03

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 36.61  E-value: 6.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 504427033 171 IEVDGGINDQTAKQVIEAGADWLVAGSYFFSraDYKEANQRLK 213
Cdd:PLN02446  86 LQVGGGVNSENAMSYLDAGASHVIVTSYVFR--DGQIDLERLK 126
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 158-208 8.52e-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: 36.02  E-value: 8.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504427033 158 LDDIRK-NRQLDFKIEVDGGINDQTAKQVIEAGADWLVAGSYFFSRADYKEA 208
Cdd:cd04726  147 EDDLKKvKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEA 198
 
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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