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Conserved domains on  [gi|197305061]
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Chain D, D-allulose-6-phosphate 3-epimerase

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10793306)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate; also catalyzes with lower efficiency 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
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 1-227 3.37e-168

allulose-6-phosphate 3-epimerase; Provisional


:

Pssm-ID: 236616  Cd Length: 229  Bit Score: 462.54  E-value: 3.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:PRK09722  83 ADFITLHPETINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKAL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197305061 161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPH 227
Cdd:PRK09722 163 RERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSGLFNLDEDIDEAWDIMTAQIEAATGEVQPH 229
 
Name Accession Description Interval E-value
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 1-227 3.37e-168

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 462.54  E-value: 3.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:PRK09722  83 ADFITLHPETINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKAL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197305061 161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPH 227
Cdd:PRK09722 163 RERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSGLFNLDEDIDEAWDIMTAQIEAATGEVQPH 229
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 1-220 1.42e-106

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: 306.23  E-value: 1.42e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFID-SHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARA 79
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  80 GADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKA 159
Cdd:COG0036   81 GADIITVHAEATP-HLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197305061 160 WREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIMTAQILAA 220
Cdd:COG0036  160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAG-SAVFG-AEDYAAAIAALREAAAAA 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 2-213 9.55e-101

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: 290.92  E-value: 9.55e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   2 KISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAgADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:cd00429   81 ADIITFHAEATD-HLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197305061 161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIM 213
Cdd:cd00429  160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAG-SALFG-SDDYAEAIKEL 210
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 3-213 1.14e-72

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: 219.84  E-value: 1.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061    3 ISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAGA 81
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAgADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   82 DFITLHPETiNGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAWR 161
Cdd:TIGR01163  81 DIITVHPEA-SEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 197305061  162 EREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIM 213
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAG-SAIFG-ADDYKEVIRSL 209
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-200 9.45e-66

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: 201.79  E-value: 9.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061    2 KISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAgADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   81 ADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:pfam00834  81 ADIISFHAEATP-HPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKM 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 197305061  161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLF 200
Cdd:pfam00834 160 IDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAG-SAVF 198
 
Name Accession Description Interval E-value
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 1-227 3.37e-168

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 462.54  E-value: 3.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:PRK09722   3 MKISPSLMCMDLLKFKEQIEFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:PRK09722  83 ADFITLHPETINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKAL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 197305061 161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPH 227
Cdd:PRK09722 163 RERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSGLFNLDEDIDEAWDIMTAQIEAATGEVQPH 229
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 1-220 1.42e-106

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: 306.23  E-value: 1.42e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFID-SHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARA 79
Cdd:COG0036    1 IKIAPSILSADFANLGEEVKRVEaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  80 GADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKA 159
Cdd:COG0036   81 GADIITVHAEATP-HLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197305061 160 WREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIMTAQILAA 220
Cdd:COG0036  160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAG-SAVFG-AEDYAAAIAALREAAAAA 218
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 2-213 9.55e-101

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: 290.92  E-value: 9.55e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   2 KISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAgADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:cd00429   81 ADIITFHAEATD-HLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 197305061 161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIM 213
Cdd:cd00429  160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAG-SALFG-SDDYAEAIKEL 210
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-208 1.93e-77

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 232.38  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIE-FIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARA 79
Cdd:PRK05581   4 VLIAPSILSADFARLGEEVKaVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  80 GADFITLHPE---TINgqafRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAE 156
Cdd:PRK05581  84 GADIITFHVEaseHIH----RLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 197305061 157 LKAWREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNH---AENIDE 208
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAG-SAVFGApdyKEAIDS 213
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 3-213 1.14e-72

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: 219.84  E-value: 1.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061    3 ISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAGA 81
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAgADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   82 DFITLHPETiNGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAWR 161
Cdd:TIGR01163  81 DIITVHPEA-SEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 197305061  162 EREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAWRIM 213
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAG-SAIFG-ADDYKEVIRSL 209
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-231 6.09e-68

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 208.70  E-value: 6.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   2 KISPSLMCMDLLKFKEQIEF-IDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:PLN02334   9 IIAPSILSADFANLAEEAKRvLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPE---TINGQafRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKA--DKITVMTVDPGFAGQPFIPEMLDKLA 155
Cdd:PLN02334  89 ASIFTFHIEqasTIHLH--RLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKGlvDMVLVMSVEPGFGGQSFIPSMMDKVR 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 197305061 156 ELKAWREreglEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNhAENIDEAwrimtaqILAAKSEVQPHAKTA 231
Cdd:PLN02334 167 ALRKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAG-SAVFG-APDYAEV-------ISGLRASVEKAAVAV 229
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-200 9.45e-66

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: 201.79  E-value: 9.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061    2 KISPSLMCMDLLKFKEQIEFIDSH-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAG 80
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAgADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   81 ADFITLHPETINgQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW 160
Cdd:pfam00834  81 ADIISFHAEATP-HPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKM 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 197305061  161 REREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLF 200
Cdd:pfam00834 160 IDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAG-SAVF 198
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 3-204 6.88e-56

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 177.87  E-value: 6.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   3 ISPSLMCMDLLKF-KEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKP-LDCHLMVTRPQDYIAQLARAG 80
Cdd:PTZ00170   9 IAPSILAADFSKLaDEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKAG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKA--DKITVMTVDPGFAGQPFIPEMLDKLAELk 158
Cdd:PTZ00170  89 ASQFTFHIEATEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTDlvDMVLVMTVEPGFGGQSFMHDMMPKVREL- 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 197305061 159 awREREGLeYEIEVDGSCNQATYEKLMAAGADVFIVGTSgLFNHAE 204
Cdd:PTZ00170 168 --RKRYPH-LNIQVDGGINLETIDIAADAGANVIVAGSS-IFKAKD 209
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
1-219 7.04e-30

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 110.51  E-value: 7.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   1 MKISPSLMCMDLLKFKEQIEFIDShADY--FHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLAR 78
Cdd:PRK08005   1 MILHPSLASADPLRYAEALTALHD-APLgsLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  79 AGADFITLHPETINGQAfRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELk 158
Cdd:PRK08005  80 IRPGWIFIHAESVQNPS-EILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQS- 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197305061 159 awreREGL-EYEIEVDGSCNQATYEKLMAAGADVFIVGTSgLFNHAEnideaWRIMTAQILA 219
Cdd:PRK08005 158 ----REHFpAAECWADGGITLRAARLLAAAGAQHLVIGRA-LFTTAN-----YDVTLSQFTA 209
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 2-204 4.95e-19

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 82.23  E-value: 4.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   2 KISPSLMCMDLLKFKEQIE-FIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKplDCHLMVTRPQDYIAQLARAG 80
Cdd:PRK08091  14 PISVGILASNWLKFNETLTtLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK--DVHLMVRDQFEVAKACVAAG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  81 ADFITLHPETINGQAfRLIDEIRRH--DMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELK 158
Cdd:PRK08091  92 ADIVTLQVEQTHDLA-LTIEWLAKQktTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVE 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 197305061 159 AWREREGLEYEIEVDGSCNQATYEKLMAAGADvFIVGTSGLFNHAE 204
Cdd:PRK08091 171 NRLGNRRVEKLISIDGSMTLELASYLKQHQID-WVVSGSALFSQGE 215
PRK14057 PRK14057
epimerase; Provisional
 12-213 9.85e-13

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 65.48  E-value: 9.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  12 LLKFKEQIEFIDShaDYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKplDCHLMVTRPQDYIAQLARAGADFITLHPE-- 89
Cdd:PRK14057  34 LHRYLQQLEALNQ--PLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK--DVHLMVADQWTAAQACVKAGAHCITLQAEgd 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  90 -----TINGQAFRLIDEIrRHDMKV--GLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAW-- 160
Cdd:PRK14057 110 ihlhhTLSWLGQQTVPVI-GGEMPVirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQLLCLlg 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 197305061 161 REREGleYEIEVDGSCNQATYEKLMAAGADVFIVGtSGLFNHAENID--EAWRIM 213
Cdd:PRK14057 189 DKREG--KIIVIDGSLTQDQLPSLIAQGIDRVVSG-SALFRDDRLVEntRSWRAM 240
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 3-196 2.91e-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: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061   3 ISPSLMC-MDLLKFKEQIEFI-DSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLAR-- 78
Cdd:cd04722    1 VILALLAgGPSGDPVELAKAAaEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197305061  79 --AGADFITLHpeTINGQAFRLIDEIRR------HDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEM 150
Cdd:cd04722   81 raAGADGVEIH--GAVGYLAREDLELIRelreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 197305061 151 LDKLAELKawrerEGLEYEIEVDGSCN-QATYEKLMAAGADVFIVGT 196
Cdd:cd04722  159 DLLLILAK-----RGSKVPVIAGGGINdPEDAAEALALGADGVIVGS 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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