|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
13-228 |
2.24e-116 |
|
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: 330.88 E-value: 2.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 13 PRLHPSILSADFARLAEELARI--PSADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEA 90
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVeaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 91 GAESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAA 170
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2232071820 171 LDGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAARHA 228
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
17-226 |
1.19e-115 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 329.07 E-value: 1.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 17 PSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGAES 94
Cdd:PRK05581 8 PSILSADFARLGEEVKAVEAAGAdwIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAKAGADI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 95 VTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALDGA 174
Cdd:PRK05581 88 ITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRKLIDER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2232071820 175 ATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAAR 226
Cdd:PRK05581 168 GLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELA 219
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
15-222 |
1.10e-105 |
|
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: 303.63 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 15 LHPSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGA 92
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGAdwIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 93 ESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALD 172
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2232071820 173 GAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALR 222
Cdd:cd00429 162 ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
17-222 |
3.43e-93 |
|
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: 271.84 E-value: 3.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 17 PSILSADFARLAEELARI--PSADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGAES 94
Cdd:TIGR01163 3 PSILSADFARLGEEVKAVeeAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 95 VTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALDGA 174
Cdd:TIGR01163 83 ITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMIDEL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2232071820 175 ATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALR 222
Cdd:TIGR01163 163 GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
14-209 |
3.68e-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: 261.11 E-value: 3.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 14 RLHPSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAG 91
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGAdwLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 92 AESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAAL 171
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2232071820 172 DGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVF 209
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
13-228 |
2.24e-116 |
|
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: 330.88 E-value: 2.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 13 PRLHPSILSADFARLAEELARI--PSADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEA 90
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVeaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 91 GAESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAA 170
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2232071820 171 LDGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAARHA 228
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
17-226 |
1.19e-115 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 329.07 E-value: 1.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 17 PSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGAES 94
Cdd:PRK05581 8 PSILSADFARLGEEVKAVEAAGAdwIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAKAGADI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 95 VTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALDGA 174
Cdd:PRK05581 88 ITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELRKLIDER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2232071820 175 ATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAAR 226
Cdd:PRK05581 168 GLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELA 219
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
15-222 |
1.10e-105 |
|
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: 303.63 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 15 LHPSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGA 92
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGAdwIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 93 ESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALD 172
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2232071820 173 GAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALR 222
Cdd:cd00429 162 ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
17-222 |
3.43e-93 |
|
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: 271.84 E-value: 3.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 17 PSILSADFARLAEELARI--PSADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGAES 94
Cdd:TIGR01163 3 PSILSADFARLGEEVKAVeeAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 95 VTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALDGA 174
Cdd:TIGR01163 83 ITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMIDEL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2232071820 175 ATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALR 222
Cdd:TIGR01163 163 GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
14-209 |
3.68e-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: 261.11 E-value: 3.68e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 14 RLHPSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAG 91
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGAdwLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 92 AESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAAL 171
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2232071820 172 DGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVF 209
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
12-228 |
2.70e-80 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 239.90 E-value: 2.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 12 SPRLHPSILSADFARLAEELARIPS--ADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAE 89
Cdd:PLN02334 7 DAIIAPSILSADFANLAEEAKRVLDagADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 90 AGAESVTFHAEASGAP--VRLARELRARGSRAGMALKPATPVE---PYLDmLPELDKLLLMTVEPGFGGQAFLDVVLPKI 164
Cdd:PLN02334 87 AGASIFTFHIEQASTIhlHRLIQQIKSAGMKAGVVLNPGTPVEavePVVE-KGLVDMVLVMSVEPGFGGQSFIPSMMDKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2232071820 165 RRARAALDgaatPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAARHA 228
Cdd:PLN02334 166 RALRKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKA 225
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
17-226 |
8.97e-80 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 238.73 E-value: 8.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 17 PSILSADFARLAEELARIPS--ADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALP-LDIHLMIADADRWAPDYAEAGAE 93
Cdd:PTZ00170 11 PSILAADFSKLADEAQDVLSggADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKAGAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 94 SVTFHAEA-SGAPVRLARELRARGSRAGMALKPATPVE---PYLDmLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARA 169
Cdd:PTZ00170 91 QFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEvlfPLID-TDLVDMVLVMTVEPGFGGQSFMHDMMPKVRELRK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2232071820 170 ALdgaatP-LALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAAR 226
Cdd:PTZ00170 170 RY-----PhLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQ 222
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
12-214 |
7.68e-57 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 180.19 E-value: 7.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 12 SPRLHPSILSADFARLAEELARIPS-ADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEA 90
Cdd:PRK09722 2 RMKISPSLMCMDLLKFKEQIEFLNSkADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 91 GAESVTFHAE-ASGAPVRLARELRARGSRAGMALKPATPVE---PYLDMlpeLDKLLLMTVEPGFGGQAFLDVVLPKIRR 166
Cdd:PRK09722 82 GADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVEsikYYIHL---LDKITVMTVDPGFAGQPFIPEMLDKIAE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2232071820 167 ARAALDGAATPLALQVDGGVNRDTIERAAEAGADTFVAG-SAVFGADDP 214
Cdd:PRK09722 159 LKALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDED 207
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
15-218 |
1.84e-38 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 132.47 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 15 LHPSILSADFARLAEELARIPSAD--AVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYAEAGA 92
Cdd:PRK08005 3 LHPSLASADPLRYAEALTALHDAPlgSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 93 ESVTFHAEASGAPVRLARELRARGSRAGMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALD 172
Cdd:PRK08005 83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2232071820 173 GAATplalQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAV 218
Cdd:PRK08005 163 AAEC----WADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
10-216 |
2.28e-15 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 72.22 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 10 LHSPRLHPSILSADFARLAEELARIPS--ADAVHVDVMDNHFVPNLTLGLPVVQAIraATALPLDIHLMIADADRWAPDY 87
Cdd:PRK08091 10 LKQQPISVGILASNWLKFNETLTTLSEnqLRLLHFDIADGQFSPFFTVGAIAIKQF--PTHCFKDVHLMVRDQFEVAKAC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 88 AEAGAESVTFHAEASGAPVRLARELRARGSRA--GMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIR 165
Cdd:PRK08091 88 VAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2232071820 166 RARAALDGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDA 216
Cdd:PRK08091 168 QVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKT 218
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
10-212 |
7.52e-12 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 63.16 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 10 LHSPRLHPSILSADFARLAEELARIPSADA--VHVDVMDNHFVPNLTLGLPVVQAIraATALPLDIHLMIADADRWAPDY 87
Cdd:PRK14057 17 LASYPLSVGILAGQWIALHRYLQQLEALNQplLHLDLMDGQFCPQFTVGPWAVGQL--PQTFIKDVHLMVADQWTAAQAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 88 AEAGAESVTFHAEASgapVRLARELRARGSRA------------GMALKPATPVEPYLDMLPELDKLLLMTVEPGFGGQA 155
Cdd:PRK14057 95 VKAGAHCITLQAEGD---IHLHHTLSWLGQQTvpviggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2232071820 156 FLDVVLPKIRRARAALDGAATPLALQVDGGVNRDTIERAAEAGADTFVAGSAVFGAD 212
Cdd:PRK14057 172 RSSDLHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
184-228 |
9.02e-05 |
|
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: 42.09 E-value: 9.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2232071820 184 GGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAARHA 228
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
21-206 |
1.92e-04 |
|
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: 41.03 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 21 SADFARLAEELARIPsADAVHVDVMDNHFVPNLTLGLPVVQAIRAATALPLDIHLMIADADRWAPDYA----EAGAESVT 96
Cdd:cd04722 11 SGDPVELAKAAAEAG-ADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAaaarAAGADGVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2232071820 97 FHAEASGAPvRLARELRARGSRAGMALKP---ATPVEPYLDMLPELDKLLLMTVEPGFGGQAFLDVVLPKIRRARAALdg 173
Cdd:cd04722 90 IHGAVGYLA-REDLELIRELREAVPDVKVvvkLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK-- 166
|
170 180 190
....*....|....*....|....*....|....
gi 2232071820 174 AATPLALQVDGGVN-RDTIERAAEAGADTFVAGS 206
Cdd:cd04722 167 RGSKVPVIAGGGINdPEDAAEALALGADGVIVGS 200
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
184-223 |
2.22e-04 |
|
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: 40.96 E-value: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2232071820 184 GGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRD 223
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
180-218 |
4.52e-04 |
|
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: 39.87 E-value: 4.52e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2232071820 180 LQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAV 218
Cdd:cd04726 161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
184-228 |
2.93e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 37.47 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2232071820 184 GGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRDAARHA 228
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| ulaD |
PRK13306 |
3-dehydro-L-gulonate-6-phosphate decarboxylase; |
178-223 |
8.36e-03 |
|
3-dehydro-L-gulonate-6-phosphate decarboxylase;
Pssm-ID: 237344 Cd Length: 216 Bit Score: 36.44 E-value: 8.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2232071820 178 LALQVDGGVNRDTIERAAEAGADTFVAGSAVFGADDPDAAVVALRD 223
Cdd:PRK13306 164 FKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAFKD 209
|
|
| |
