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Conserved domains on  [gi|32527422|gb|AAP86172|]
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ribulose-5-phosphate 3-epimerase (plasmid) [Cupriavidus necator H16]

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]; ...
16-238 3.30e-130

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: 366.32  E-value: 3.30e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  16 IRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  96 GANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARAR 175
Cdd:COG0036  81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32527422 176 IDrqvaAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAA 215
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
16-238 3.30e-130

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: 366.32  E-value: 3.30e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  16 IRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  96 GANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARAR 175
Cdd:COG0036  81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32527422 176 IDrqvaAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAA 215
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
13-238 2.56e-122

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 346.40  E-value: 2.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   13 QRAIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMF 92
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   93 AKAGANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQA 172
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32527422  173 RARIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PRK05581 161 RKLIDE----RGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAEL 218
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
18-222 4.54e-117

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: 332.70  E-value: 4.54e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32527422   178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
17-218 3.60e-116

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: 330.06  E-value: 3.60e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    17 RLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAG 96
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    97 ANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARI 176
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 32527422   177 DRQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
18-235 4.36e-115

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: 327.90  E-value: 4.36e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:cd00429   2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:cd00429  82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32527422 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLR 235
Cdd:cd00429 162 EN----NLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
16-238 3.30e-130

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: 366.32  E-value: 3.30e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  16 IRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:COG0036   1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  96 GANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARAR 175
Cdd:COG0036  81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32527422 176 IDrqvaAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAA 215
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
13-238 2.56e-122

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 346.40  E-value: 2.56e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   13 QRAIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMF 92
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   93 AKAGANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQA 172
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32527422  173 RARIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PRK05581 161 RKLIDE----RGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAEL 218
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
18-222 4.54e-117

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: 332.70  E-value: 4.54e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32527422   178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
17-218 3.60e-116

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: 330.06  E-value: 3.60e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    17 RLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAG 96
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422    97 ANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARI 176
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 32527422   177 DRQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
18-235 4.36e-115

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: 327.90  E-value: 4.36e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:cd00429   2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:cd00429  82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32527422 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLR 235
Cdd:cd00429 162 EN----NLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
15-237 2.10e-99

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 288.82  E-value: 2.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   15 AIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAK 94
Cdd:PLN02334   7 DAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   95 AGANLISFHPEASR--HVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDK--LDLVLLMSVNPGFGGQAFIPGVLDKVR 170
Cdd:PLN02334  87 AGASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMDKVR 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32527422  171 QARARIDRqvaaggrpVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREA 237
Cdd:PLN02334 167 ALRKKYPE--------LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPD----YAEVISGLRAS 221
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
16-222 1.08e-66

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 205.61  E-value: 1.08e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   16 IRLAPSILSADFARLGEEVCAIEAGgADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNSK-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   96 GANLISFHPE-ASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARA 174
Cdd:PRK09722  82 GADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 32527422  175 RIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAG-SAVFGAPD 222
Cdd:PRK09722 162 LRER----NGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDE 206
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
11-238 8.48e-64

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 198.29  E-value: 8.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   11 GSQRAIrLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRP-LVSIPIDVHLMVEPVDALI 89
Cdd:PTZ00170   3 QPLKAI-IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKhLPNTFLDCHLMVSNPEKWV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   90 PMFAKAGANLISFHPEA-SRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDK--LDLVLLMSVNPGFGGQAFIPGVL 166
Cdd:PTZ00170  82 DDFAKAGASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMM 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32527422  167 DKVRQARAR---IDRQVaaggrpvwleiDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PTZ00170 162 PKVRELRKRyphLNIQV-----------DGGINLETIDIAADAGANVIVAGSSIFKAKD----RKQAIELLRESV 221
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
18-224 5.30e-28

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 105.89  E-value: 5.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:PRK08005   3 LHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:PRK08005  83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 32527422  178 RQvaaggrPVWleIDGGVKADNITEIARAGADTFVAGSAVFGAPDAD 224
Cdd:PRK08005 163 AA------ECW--ADGGITLRAARLLAAAGAQHLVIGRALFTTANYD 201
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
22-224 1.26e-19

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 84.16  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   22 ILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLvceAIRPLVSIPI-DVHLMVEPVDALIPMFAKAGANLI 100
Cdd:PRK08091  19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAI---AIKQFPTHCFkDVHLMVRDQFEVAKACVAAGADIV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  101 SFHPEASRHVDRTIGLIRDHGCKA--GLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQararIDR 178
Cdd:PRK08091  96 TLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQ----VEN 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 32527422  179 QVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDAD 224
Cdd:PRK08091 172 RLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELK 217
PRK14057 PRK14057
epimerase; Provisional
18-218 2.24e-13

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 67.40  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIrPLVSIPiDVHLMVEPVDALIPMFAKAGA 97
Cdd:PRK14057  22 LSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQACVKAGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422   98 NLISFHPEASRHVDRTIGLIRDHGCKA---------GLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDK 168
Cdd:PRK14057 100 HCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHER 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 32527422  169 VRQARARIDRQVAAGgrpvWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:PRK14057 180 VAQLLCLLGDKREGK----IIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
36-215 3.59e-05

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: 43.34  E-value: 3.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  36 AIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAK----AGANLISFHPEASRHVD 111
Cdd:cd04722  20 AAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGADGVEIHGAVGYLAR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422 112 RTIGLIRDH-----GCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARIDRQVAAGGrp 186
Cdd:cd04722 100 EDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG-- 177
                       170       180
                ....*....|....*....|....*....
gi 32527422 187 vwleidGGVKADNITEIARAGADTFVAGS 215
Cdd:cd04722 178 ------GINDPEDAAEALALGADGVIVGS 200
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
166-237 1.86e-04

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: 41.32  E-value: 1.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32527422 166 LDKVRQARARIDRQVAAggrpvwleIdGGVKADNITEIARAGADTFVAGSAVFGAPDADGGYRGILHRLREA 237
Cdd:COG0352 144 LEGLAWWAELVEIPVVA--------I-GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
166-222 1.47e-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: 38.65  E-value: 1.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32527422 166 LDKVRQARARIDRQVAAggrpvwleIdGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:cd00564 139 LELLREIAELVEIPVVA--------I-GGITPENAAEVLAAGADGVAVISAITGADD 186
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
166-224 3.40e-03

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


Pssm-ID: 238807 [Multi-domain]  Cd Length: 272  Bit Score: 37.66  E-value: 3.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422 166 LDKVR-QARARIDRQVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAgSAVFGAPDAD 224
Cdd:cd01573 209 LDKFSpEELAELVPKLRSLAPPVLLAAAGGINIENAAAYAAAGADILVT-SAPYYAKPAD 267
thiE PRK00043
thiamine phosphate synthase;
163-222 4.21e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 37.08  E-value: 4.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32527422  163 PGVLDKVRQARARIdrqvaaGGRPvWLEIdGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:PRK00043 145 PQGLEGLREIRAAV------GDIP-IVAI-GGITPENAPEVLEAGADGVAVVSAITGAED 196
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
161-228 9.34e-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: 36.45  E-value: 9.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32527422 161 FIPGVLDKVRQARARIDRQVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDADGGYR 228
Cdd:cd00516 214 GSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
 
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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