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Conserved domains on  [gi|763412636|ref|WP_044268984|]
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MULTISPECIES: ribulose-phosphate 3-epimerase [Enterobacteriaceae]

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]; ...
 3-214 6.37e-98

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: 283.51  E-value: 6.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   3 QILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTG 82
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  83 AEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV 162
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763412636 163 --TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFN-DAPRESYQALRAAIQ 214
Cdd:COG0036  162 deRGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGaEDYAAAIAALREAAA 216
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 3-214 6.37e-98

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: 283.51  E-value: 6.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   3 QILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTG 82
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  83 AEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV 162
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763412636 163 --TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFN-DAPRESYQALRAAIQ 214
Cdd:COG0036  162 deRGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGaEDYAAAIAALREAAA 216
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-205 4.92e-89

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: 260.87  E-value: 4.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   3 QILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  83 AEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 763412636 163 --TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDAPRES 205
Cdd:cd00429  161 peNNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAE 205
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-212 3.38e-82

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 243.55  E-value: 3.38e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   1 MAQILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIK 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  81 TGAEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKK 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763412636 161 MV--TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDA-PRESYQALRAA 212
Cdd:PRK05581 163 LIdeRGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPdYKEAIDSLRAE 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 4-199 1.32e-76

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: 229.08  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636    4 ILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGA 83
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   84 EMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMVT 163
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 763412636  164 GRN--IQIEVDGGVNTEIAKKVKEAGADLIVVGGALFN 199
Cdd:TIGR01163 161 ELGlsILIEVDGGVNDDNARELAEAGADILVAGSAIFG 198
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 4-198 1.72e-70

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: 213.35  E-value: 1.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636    4 ILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGA 83
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   84 EMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV- 162
Cdd:pfam00834  82 DIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMId 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 763412636  163 -TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALF 198
Cdd:pfam00834 162 eRGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 3-214 6.37e-98

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: 283.51  E-value: 6.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   3 QILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTG 82
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  83 AEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV 162
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763412636 163 --TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFN-DAPRESYQALRAAIQ 214
Cdd:COG0036  162 deRGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGaEDYAAAIAALREAAA 216
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-205 4.92e-89

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: 260.87  E-value: 4.92e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   3 QILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  83 AEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 763412636 163 --TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDAPRES 205
Cdd:cd00429  161 peNNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAE 205
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-212 3.38e-82

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 243.55  E-value: 3.38e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   1 MAQILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIK 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  81 TGAEMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKK 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763412636 161 MV--TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDA-PRESYQALRAA 212
Cdd:PRK05581 163 LIdeRGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPdYKEAIDSLRAE 217
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 4-199 1.32e-76

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: 229.08  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636    4 ILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGA 83
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   84 EMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMVT 163
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 763412636  164 GRN--IQIEVDGGVNTEIAKKVKEAGADLIVVGGALFN 199
Cdd:TIGR01163 161 ELGlsILIEVDGGVNDDNARELAEAGADILVAGSAIFG 198
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-214 1.56e-70

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 214.48  E-value: 1.56e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   2 AQILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKT 81
Cdd:PLN02334   8 AIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  82 GAEMMSVHYE--STPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLD--DIDYILIMTINPGQPGQTFIEKSLEKIRN 157
Cdd:PLN02334  88 GASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMDKVRA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 763412636 158 TKKMVTGRNiqIEVDGGVNTEIAKKVKEAGADLIVVGGALFN-DAPRESYQALRAAIQ 214
Cdd:PLN02334 168 LRKKYPELD--IEVDGGVGPSTIDKAAEAGANVIVAGSAVFGaPDYAEVISGLRASVE 223
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 4-198 1.72e-70

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: 213.35  E-value: 1.72e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636    4 ILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGA 83
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   84 EMMSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMV- 162
Cdd:pfam00834  82 DIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMId 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 763412636  163 -TGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALF 198
Cdd:pfam00834 162 eRGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-199 1.67e-52

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 168.63  E-value: 1.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   2 AQILPSVFGANILRLQEEIQFLETeKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKT 81
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNS-KADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  82 GAEMMSVHYES-TPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKK 160
Cdd:PRK09722  82 GADFITLHPETiNGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 763412636 161 MVT--GRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGA-LFN 199
Cdd:PRK09722 162 LRErnGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSgLFN 203
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 1-214 4.37e-52

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 167.47  E-value: 4.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   1 MAQILPSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTF-DVHMMLANPERHIDDVI 79
Cdd:PTZ00170   6 KAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFlDCHLMVSNPEKWVDDFA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  80 KTGAEMMSVHYEST-PHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDD--IDYILIMTINPGQPGQTFIEKSLEKIR 156
Cdd:PTZ00170  86 KAGASQFTFHIEATeDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 763412636 157 NTKKMVTGRNIQieVDGGVNTEIAKKVKEAGADLIVVGGALFN-DAPRESYQALRAAIQ 214
Cdd:PTZ00170 166 ELRKRYPHLNIQ--VDGGINLETIDIAADAGANVIVAGSSIFKaKDRKQAIELLRESVQ 222
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
6-201 3.51e-31

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 113.21  E-value: 3.51e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   6 PSVFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGAEM 85
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  86 MSVHYESTPHVHYIIQKIKKAGRKAGVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMVTgr 165
Cdd:PRK08005  85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP-- 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 763412636 166 NIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDA 201
Cdd:PRK08005 163 AAECWADGGITLRAARLLAAAGAQHLVIGRALFTTA 198
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 8-201 5.82e-20

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 84.16  E-value: 5.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   8 VFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGpnQIAAMKKASSMTFDVHMMLANPERHIDDVIKTGAEMMS 87
Cdd:PRK08091  19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVG--AIAIKQFPTHCFKDVHLMVRDQFEVAKACVAAGADIVT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  88 VHYESTPHVHYIIQKIKKAGRKA--GVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNTKKMVTGR 165
Cdd:PRK08091  97 LQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVENRLGNR 176

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 763412636 166 NIQ--IEVDGGVNTEIAKKVKEAGADLIVVGGALFNDA 201
Cdd:PRK08091 177 RVEklISIDGSMTLELASYLKQHQIDWVVSGSALFSQG 214
PRK14057 PRK14057
epimerase; Provisional
 8-200 2.03e-14

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 69.71  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636   8 VFGANILRLQEEIQFLETEKTEILHVDLMDGTYVSNIAFGPNQIAAMKKasSMTFDVHMMLANPERHIDDVIKTGAEMMS 87
Cdd:PRK14057  26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQ--TFIKDVHLMVADQWTAAQACVKAGAHCIT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  88 VHYESTPHVHYII-----QKIKKAGRKA----GVVLNPGTPEHVIEYLLDDIDYILIMTINPGQPGQTFIEKSLEKIRNT 158
Cdd:PRK14057 104 LQAEGDIHLHHTLswlgqQTVPVIGGEMpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 763412636 159 KKMVTGRNIQ--IEVDGGVNTEIAKKVKEAGADLIVVGGALFND 200
Cdd:PRK14057 184 LCLLGDKREGkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRD 227
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 81-195 2.72e-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: 49.12  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636  81 TGAEMMSVHYESTPHVHYIIQKIKKA--GRKAGVVLNPGTPEHVIEYLLDDIDYILIMTinpGQPGQTFIEKSLEKIRNT 158
Cdd:cd04722   86 DGVEIHGAVGYLAREDLELIRELREAvpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGN---GGGGGGGRDAVPIADLLL 162

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 763412636 159 KKMVTGRNIQIEVDGGVNT-EIAKKVKEAGADLIVVGG 195
Cdd:cd04722  163 ILAKRGSKVPVIAGGGINDpEDAAEALALGADGVIVGS 200
thiE PRK00043
thiamine phosphate synthase;
117-214 5.33e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 39.78  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636 117 GTPEHVIEYLLDDIDYILIMTINP-----GQPGQTFIEKsLEKIRNTkkmvtGRNIQIEVDGGVNTEIAKKVKEAGADLI 191
Cdd:PRK00043 112 HTLEEAAAALAAGADYVGVGPIFPtptkkDAKAPQGLEG-LREIRAA-----VGDIPIVAIGGITPENAPEVLEAGADGV 185

                         90       100
                 ....*....|....*....|....
gi 763412636 192 VVGGALF-NDAPRESYQALRAAIQ 214
Cdd:PRK00043 186 AVVSAITgAEDPEAAARALLAAFR 209
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 151-202 6.59e-04

Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439927 [Multi-domain]  Cd Length: 272  Bit Score: 39.62  E-value: 6.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 763412636 151 SLEKIRNTKKMVTGRnIQIEVDGGVNTEIAKKVKEAGADLIVVgGALFNDAP 202
Cdd:COG0157  213 SPEELREAVALLRGR-ALLEASGGITLENIRAYAETGVDYISV-GALTHSAP 262
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
153-214 8.52e-04

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 39.02  E-value: 8.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763412636 153 EKIRNTKKMVTgrNIQIEVDGGVNT-EIAKKVKEAGADLIVVGGALFNDaPRESYQALRAAIQ 214
Cdd:PRK04169 173 EMVKAVKKALD--ITPLIYGGGIRSpEQARELMAAGADTIVVGNIIEED-PKKTVKAIKKAIK 232
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
153-194 1.03e-03

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 38.99  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 763412636 153 EKIRNTKKMVTgrNIQIEVDGGVNT-EIAKKVKEAGADLIVVG 194
Cdd:COG1646  185 EMVKAVKKALE--DTPLIYGGGIRSpEKAREMAEAGADTIVVG 225
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 159-205 1.04e-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: 38.72  E-value: 1.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 763412636 159 KKMVTGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDA-PRES 205
Cdd:cd04726  151 KKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAAdPAEA 198
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 159-213 1.05e-03

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 39.23  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 763412636 159 KKMVTGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALF-NDAPRESYQALRAAI 213
Cdd:PRK07028 155 KEVSEEVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIkSADVTEAARKIREAI 210
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 153-200 1.10e-03

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 38.76  E-value: 1.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 763412636 153 EKIRNTKKMVTgrNIQIEVDGGV-NTEIAKKVKEAGADLIVVGGALFND 200
Cdd:cd02812  164 EVVRAVKKVLG--DTPLIVGGGIrSGEQAKEMAEAGADTIVVGNIVEED 210
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 118-211 2.08e-03

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: 37.88  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636 118 TPEHVIEYLLDDIDYILIMTI-------NPGQPgqtfieKSLEKIRNTKKMVtgrNIQIEVDGGVNTEIAKKVKEAGADL 190
Cdd:cd00564  104 SLEEALRAEELGADYVGFGPVfptptkpGAGPP------LGLELLREIAELV---EIPVVAIGGITPENAAEVLAAGADG 174

                         90       100
                 ....*....|....*....|..
gi 763412636 191 IVVGGALFNDA-PRESYQALRA 211
Cdd:cd00564  175 VAVISAITGADdPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 173-214 2.14e-03

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: 37.86  E-value: 2.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 763412636 173 GGVNTEIAKKVKEAGADLIVVGGALFNDA-PRESYQALRAAIQ 214
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPdPAAAARELRAALE 204
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 152-202 3.86e-03

Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses 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, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.


Pssm-ID: 238286 [Multi-domain]  Cd Length: 281  Bit Score: 37.22  E-value: 3.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 763412636 152 LEKIRNTKKMVTGRNIQIEVDGGVNTEIAKKVKEAGADLIVVGGALFNDAP 202
Cdd:cd00516  225 ILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPP 275
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 121-194 5.61e-03

universal stress protein At3g01520 and similar proteins; This subfamily includes plant and fungal proteins of unknown function, including Arabidopsis thaliana At3g01520. A. thaliana contains 44 USP domain-containing proteins; the USP domain is found either in a small protein with unknown physiological function or as an N-terminal portion of a multi-domain protein, usually a protein kinase. The gene At3g01520 of Arabidopsis thaliana encodes a 175-residue universal stress protein (USP)-like protein which is widely found in the genomes of bacteria, as well as fungi, protozoa, and plants. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 belongs to the ATP-binding USP subfamily. Universal stress proteins (USPs) are small cytoplasmic bacterial proteins whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467505  Cd Length: 143  Bit Score: 36.06  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763412636 121 HVIEYLLDDIDYILIMTINPGQPGQTFIEKS---LEKIRntKKMVTGRNIQIEVD---GGVNTEIAKKVKEAGADLIVVG 194
Cdd:cd23659   35 HVIEPPSLPAASLGSGSEEWEALEEEAREKAeklLEKYE--KKLKEEKGIKVKVEvvaGDPGEVICKAAEELKADLIVMG 112
 
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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