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Conserved domains on  [gi|93279635]
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Chain I, ribulose-phosphate 3-epimerase

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]; ...
 5-219 3.61e-131

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: 367.86  E-value: 3.61e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:COG0036   2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:COG0036  82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 93279635 165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTALN 219
Cdd:COG0036 162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAA 216
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-219 3.61e-131

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: 367.86  E-value: 3.61e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:COG0036   2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:COG0036  82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 93279635 165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTALN 219
Cdd:COG0036 162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAA 216
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-218 1.17e-125

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 354.10  E-value: 1.17e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAF 80
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   81 AQAGADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATV 160
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 93279635  161 AKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTAL 218
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-215 1.91e-125

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: 352.94  E-value: 1.91e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:cd00429  81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 93279635 165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLR 215
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-215 5.86e-100

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: 288.79  E-value: 5.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635     6 IAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAGA 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    86 DIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWRD 165
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 93279635   166 EKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLR 215
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 5-202 3.24e-91

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: 266.12  E-value: 3.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635     5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 93279635   165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLF 202
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-219 3.61e-131

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: 367.86  E-value: 3.61e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:COG0036   2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:COG0036  82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 93279635 165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTALN 219
Cdd:COG0036 162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAA 216
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-218 1.17e-125

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 354.10  E-value: 1.17e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAF 80
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   81 AQAGADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATV 160
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 93279635  161 AKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTAL 218
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-215 1.91e-125

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: 352.94  E-value: 1.91e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:cd00429   1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:cd00429  81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 93279635 165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLR 215
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-215 5.86e-100

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: 288.79  E-value: 5.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635     6 IAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAGA 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    86 DIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWRD 165
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 93279635   166 EKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLR 215
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-218 7.19e-99

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 286.51  E-value: 7.19e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAF 80
Cdd:PLN02334   5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   81 AQAGADIMTIHTE--STRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLD--LVDQVLIMTVNPGFGGQAFIPECLEK 156
Cdd:PLN02334  85 AKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMDK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93279635  157 VATVAKWRDEKglsfDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTAL 218
Cdd:PLN02334 165 VRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASV 222
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 5-202 3.24e-91

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: 266.12  E-value: 3.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635     5 KIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAG 84
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    85 ADIMTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAKWR 164
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 93279635   165 DEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLF 202
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 1-219 7.98e-87

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 256.07  E-value: 7.98e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLK--IAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVF-DCHLMVVDPERYV 77
Cdd:PTZ00170   2 KQPLKaiIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFlDCHLMVSNPEKWV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   78 EAFAQAGADIMTIHTESTRHIHGAL-QKIKAAGMKAGVVINPGTPATALEPLLD--LVDQVLIMTVNPGFGGQAFIPECL 154
Cdd:PTZ00170  82 DDFAKAGASQFTFHIEATEDDPKAVaRKIREAGMKVGVAIKPKTPVEVLFPLIDtdLVDMVLVMTVEPGFGGQSFMHDMM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 93279635  155 EKVATV-AKWRDekglsFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTALN 219
Cdd:PTZ00170 162 PKVRELrKRYPH-----LNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQ 222
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-210 2.49e-72

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 219.10  E-value: 2.49e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    2 STLKIAPSILAADYANFASELARIEeTDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFA 81
Cdd:PRK09722   1 MRMKISPSLMCMDLLKFKEQIEFLN-SKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   82 QAGADIMTIHTES-TRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATV 160
Cdd:PRK09722  80 DAGADFITLHPETiNGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAEL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 93279635  161 AKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAG-SYLFKASDLVSQ 210
Cdd:PRK09722 160 KALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDEDIDE 210
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
8-214 6.05e-33

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 118.22  E-value: 6.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    8 PSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHSKLVFDCHLMVVDPERYVEAFAQAGADI 87
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   88 MTIHTESTRHIHGALQKIKAAGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVATVAkwrdEK 167
Cdd:PRK08005  85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSR----EH 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 93279635  168 GLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDL---VSQVQTL 214
Cdd:PRK08005 161 FPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYdvtLSQFTAL 210
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 1-218 4.57e-26

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 100.72  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKHskLVFDCHLMVVDPERYVEAF 80
Cdd:PRK08091  10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTH--CFKDVHLMVRDQFEVAKAC 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   81 AQAGADIMTIHTESTRHIHGALQKIKA--AGMKAGVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIPECLEKVA 158
Cdd:PRK08091  88 VAAGADIVTLQVEQTHDLALTIEWLAKqkTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVI 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  159 TVAKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTAL 218
Cdd:PRK08091 168 QVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSL 227
PRK14057 PRK14057
epimerase; Provisional
 1-220 3.05e-23

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 93.98  E-value: 3.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    1 MSTLKIAPSILAADYANFASELARIEETDAEYVHIDIMDGQFVPNISFGADVVASMRKhsKLVFDCHLMVVDPERYVEAF 80
Cdd:PRK14057  17 LASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQ--TFIKDVHLMVADQWTAAQAC 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   81 AQAGADIMTIHTESTRHIHGAL-----QKIKAAGMKA----GVVINPGTPATALEPLLDLVDQVLIMTVNPGFGGQAFIP 151
Cdd:PRK14057  95 VKAGAHCITLQAEGDIHLHHTLswlgqQTVPVIGGEMpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSS 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 93279635  152 ECLEKVATVAKWRDEKGLSFDIEVDGGVDNKTIRACYEAGANVFVAGSYLFKASDLVSQVQTLRTALNV 220
Cdd:PRK14057 175 DLHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDDRLVENTRSWRAMFKV 243
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 10-208 1.02e-06

Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.


Pssm-ID: 395160  Cd Length: 215  Bit Score: 47.64  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    10 ILAADYANFASELARIEETDAEY----VHIDIMdgqfvpnISFGADVVASMRKHSKLVFdCHLMVVD----PERYVEAFA 81
Cdd:pfam00215   4 CVALDVPTLEEALELADELGPYVdilkVGTPLF-------EAFGLKLVAELRKHGFLIF-LDLKFADigntVAKQAKYKA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635    82 QAGADIMTIHT---ESTrhIHGALQKIKAAGMKAGVVI---NPGtPATALEPLLDLVDQVLIMT------VNPGF--GGQ 147
Cdd:pfam00215  76 KLGADIVTVHAyagEGT--LKAAKEAAEEYGRGLLLVAelsSKG-SLDLQEEGDLGYTQEIVHRaadlaaGVDGVvaSAT 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 93279635   148 AFIPECLEKVATVAkwrdeKGLSFDIEVDGGVDNKTIRAC-YEAGANVFVAGSYLFKASDLV 208
Cdd:pfam00215 153 EALREILPDFLILT-----PGIGLQGGDAGGQQRVTTPAVaKEAGADIIIVGRGITGAGDPV 209
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 46-208 3.25e-05

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: 43.34  E-value: 3.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635  46 ISFGADVVASMRK---HSKLVFDchLMVVDPERY-VEAFAQAGADIMTI---HTESTrhIHGALQKIKAAGMKAGV-VIN 117
Cdd:cd04726  37 KSEGMEAVRALREafpDKIIVAD--LKTADAGALeAEMAFKAGADIVTVlgaAPLST--IKKAVKAAKKYGKEVQVdLIG 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635 118 PGTPATALEpLLDL-VDQVLIMTvnpGFGGQA-FIPECLEKVATVakwrdEKGLSFDIEVDGGVDNKTIRACYEAGANVF 195
Cdd:cd04726 113 VEDPEKRAK-LLKLgVDIVILHR---GIDAQAaGGWWPEDDLKKV-----KKLLGVKVAVAGGITPDTLPEFKKAGADIV 183

                       170
                ....*....|...
gi 93279635 196 VAGSYLFKASDLV 208
Cdd:cd04726 184 IVGRAITGAADPA 196
PLN02417 PLN02417
dihydrodipicolinate synthase
 65-158 6.32e-04

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 39.63  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 93279635   65 DCHLMVVDpeRYVEAFAQAGADIMTIHTESTRH-IHGALQKIkAAGMKAGVVINPGTPATALEPLLDLVDQVLIM--TV- 140
Cdd:PLN02417  54 DEHIMLIG--HTVNCFGGKIKVIGNTGSNSTREaIHATEQGF-AVGMHAALHINPYYGKTSQEGLIKHFETVLDMgpTIi 130

                         90       100
                 ....*....|....*....|
gi 93279635  141 -N-PGFGGQAFIPECLEKVA 158
Cdd:PLN02417 131 yNvPGRTGQDIPPEVIFKIA 150
 
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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