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Conserved domains on  [gi|488376877|ref|WP_002446262|]
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MULTISPECIES: ribulose-phosphate 3-epimerase [Staphylococcus]

Protein Classification

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

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-214 5.40e-124

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: 349.37  E-value: 5.40e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   2 VKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQL 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488376877 162 KHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-214 5.40e-124

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: 349.37  E-value: 5.40e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   2 VKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQL 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488376877 162 KHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-213 3.30e-118

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: 334.45  E-value: 3.30e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   3 KILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  83 ADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLK 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488376877 163 HENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLK 213
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-214 3.55e-109

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 312.12  E-value: 3.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   1 MVKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAE 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  81 HGADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQ 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488376877 161 LKHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:PRK05581 163 LIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 4-213 2.13e-96

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: 279.55  E-value: 2.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877    4 ILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHGA 83
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   84 DMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLKH 163
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488376877  164 ENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLK 213
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 3-200 9.18e-89

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 259.57  E-value: 9.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877    3 KILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHG 82
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   83 ADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLK 162
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 488376877  163 HENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-214 5.40e-124

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: 349.37  E-value: 5.40e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   2 VKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQL 161
Cdd:COG0036   81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488376877 162 KHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:COG0036  161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 3-213 3.30e-118

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: 334.45  E-value: 3.30e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   3 KILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHG 82
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  83 ADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLK 162
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488376877 163 HENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLK 213
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-214 3.55e-109

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 312.12  E-value: 3.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   1 MVKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAE 80
Cdd:PRK05581   3 MVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  81 HGADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQ 160
Cdd:PRK05581  83 AGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488376877 161 LKHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:PRK05581 163 LIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 4-213 2.13e-96

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: 279.55  E-value: 2.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877    4 ILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHGA 83
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   84 DMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLKH 163
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488376877  164 ENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLK 213
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 3-200 9.18e-89

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 259.57  E-value: 9.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877    3 KILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHG 82
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   83 ADMISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQLK 162
Cdd:pfam00834  81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 488376877  163 HENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-214 1.31e-86

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 255.31  E-value: 1.31e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   2 VKILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:PLN02334   8 AIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVE--ATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPIL--SIVDYVLVMTVNPGFGGQTFIEQCVTKIEQ 157
Cdd:PLN02334  88 GASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVekGLVDMVLVMSVEPGFGGQSFIPSMMDKVRA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488376877 158 LNQLKHENhltfDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:PLN02334 168 LRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRA 220
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-197 1.86e-66

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 204.07  E-value: 1.86e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   2 VKILPSLLSIDFLNLKEELQLLEAaKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNS-KADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVE-ATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQ 160
Cdd:PRK09722  82 GADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKA 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 488376877 161 LKHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGS 197
Cdd:PRK09722 162 LRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 4-214 1.02e-64

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 199.83  E-value: 1.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   4 ILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQqsHLP---IDVHLMIEQPENYINLFAE 80
Cdd:PTZ00170   9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRK--HLPntfLDCHLMVSNPEKWVDDFAK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  81 HGADMISVHVEATT-HIHRAIEQIKQLGKKAGVVINPGTSVETILPILS--IVDYVLVMTVNPGFGGQTFIEQCVTKIEQ 157
Cdd:PTZ00170  87 AGASQFTFHIEATEdDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDtdLVDMVLVMTVEPGFGGQSFMHDMMPKVRE 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488376877 158 LNQLKheNHLtfDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLKE 214
Cdd:PTZ00170 167 LRKRY--PHL--NIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRE 219
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
6-205 7.28e-32

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 115.13  E-value: 7.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   6 PSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYINLFAEHGADM 85
Cdd:PRK08005   5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  86 ISVHVEATTHIHRAIEQIKQLGKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLnqlkHEN 165
Cdd:PRK08005  85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQS----REH 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 488376877 166 HLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDY 205
Cdd:PRK08005 161 FPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANY 200
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 3-213 6.72e-21

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 86.85  E-value: 6.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   3 KILPSLLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGIPildAVRQ-QSHLPIDVHLMIEQPENYINLFAEH 81
Cdd:PRK08091  14 PISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAI---AIKQfPTHCFKDVHLMVRDQFEVAKACVAA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  82 GADMISVHVEATTHIHRAIEQIKQLGKKA--GVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLN 159
Cdd:PRK08091  91 GADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVE 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488376877 160 QLKHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQEDYAKVTSLLK 213
Cdd:PRK08091 171 NRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWK 224
PRK14057 PRK14057
epimerase; Provisional
 8-203 1.06e-18

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 81.65  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877   8 LLSIDFLNLKEELQLLEAAKVDGLHFDVMDGKFVPNISIGiPILDAVRQQSHLPiDVHLMIEQPENYINLFAEHGADMIS 87
Cdd:PRK14057  26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVG-PWAVGQLPQTFIK-DVHLMVADQWTAAQACVKAGAHCIT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  88 VHVEATTHIHRAIEQIKQ-----LGKKA----GVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQL 158
Cdd:PRK14057 104 LQAEGDIHLHHTLSWLGQqtvpvIGGEMpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 488376877 159 NQLKHENHLTFDIEVDGGINDQTSKRCVEQGATMLVTGSYFFKQE 203
Cdd:PRK14057 184 LCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 18-197 1.76e-08

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: 52.59  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  18 EELQLLEAAKVDGLHFDVMDGKFVPNISIGIPILDAVRQQSHLPIDVHLMIEQPENYIN----LFAEHGADMISVHVEAT 93
Cdd:cd04722   16 ELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDiaaaAARAAGADGVEIHGAVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488376877  94 THIHRAIEQIKQL-----GKKAGVVINPGTSVETILPILSIVDYVLVMTVNPGFGGQTFIEQCVTKIEQLNQlkhenHLT 168
Cdd:cd04722   96 YLAREDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKR-----GSK 170

                        170       180       190
                 ....*....|....*....|....*....|
gi 488376877 169 FDIEVDGGIND-QTSKRCVEQGATMLVTGS 197
Cdd:cd04722  171 VPVIAGGGINDpEDAAEALALGADGVIVGS 200
 
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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