|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
3-223 |
5.29e-146 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 405.72 E-value: 5.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 3 KNIVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFA 82
Cdd:PRK05581 2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 83 KAGADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRA 162
Cdd:PRK05581 82 KAGADIITFHVE--ASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1TQJ_E 163 LRQMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNSKRP 223
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
5-220 |
1.24e-139 |
|
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: 389.82 E-value: 1.24e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 5 IVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKA 84
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 85 GADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALR 164
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1TQJ_E 165 QMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNS 220
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
7-218 |
5.96e-130 |
|
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: 365.06 E-value: 5.96e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 7 VAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAGA 86
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 87 DIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQM 166
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1TQJ_E 167 CDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVR 218
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
7-218 |
4.28e-129 |
|
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: 362.95 E-value: 4.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 7 VAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAGA 86
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 87 DIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQM 166
Cdd:cd00429 82 DIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1TQJ_E 167 CDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVR 218
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
6-205 |
3.21e-122 |
|
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: 345.08 E-value: 3.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 6 VVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAG 85
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 86 ADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQ 165
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
1TQJ_E 166 MCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVF 205
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
3-223 |
5.29e-146 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 405.72 E-value: 5.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 3 KNIVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFA 82
Cdd:PRK05581 2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 83 KAGADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRA 162
Cdd:PRK05581 82 KAGADIITFHVE--ASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1TQJ_E 163 LRQMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNSKRP 223
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
5-220 |
1.24e-139 |
|
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: 389.82 E-value: 1.24e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 5 IVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKA 84
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 85 GADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALR 164
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1TQJ_E 165 QMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNS 220
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
7-218 |
5.96e-130 |
|
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: 365.06 E-value: 5.96e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 7 VAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAGA 86
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 87 DIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQM 166
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1TQJ_E 167 CDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVR 218
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
7-218 |
4.28e-129 |
|
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: 362.95 E-value: 4.28e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 7 VAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAGA 86
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 87 DIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQM 166
Cdd:cd00429 82 DIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1TQJ_E 167 CDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVR 218
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-223 |
8.57e-128 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 360.09 E-value: 8.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 1 MSKNIVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVED 80
Cdd:PLN02334 4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 81 FAKAGADIISVHVEHNASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVC--DLILIMSVNPGFGGQSFIPEVLP 158
Cdd:PLN02334 84 FAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKGlvDMVLVMSVEPGFGGQSFIPSMMD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1TQJ_E 159 KIRALRQMCDERgldpWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNSKRP 223
Cdd:PLN02334 164 KVRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEK 224
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
6-205 |
3.21e-122 |
|
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: 345.08 E-value: 3.21e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 6 VVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKAG 85
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 86 ADIISVHVEhnASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQ 165
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
1TQJ_E 166 MCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVF 205
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
6-220 |
1.30e-79 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 237.96 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 6 VVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKT-LDVHLMIVEPEKYVEDFAKA 84
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 85 GADIISVHVEhNASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVC--DLILIMSVNPGFGGQSFIPEVLPKIRA 162
Cdd:PTZ00170 88 GASQFTFHIE-ATEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTDlvDMVLVMTVEPGFGGQSFMHDMMPKVRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1TQJ_E 163 LRQmcdeRGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAGVRNS 220
Cdd:PTZ00170 167 LRK----RYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
3-213 |
8.68e-69 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 210.62 E-value: 8.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 3 KNIVVAPSILSADFSRLGEEIKAVDEAgADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFA 82
Cdd:PRK09722 1 MRMKISPSLMCMDLLKFKEQIEFLNSK-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 83 KAGADIISVHVEhNASPHLHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRA 162
Cdd:PRK09722 80 DAGADFITLHPE-TINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1TQJ_E 163 LRQMCDERGLDPWIEVDGGLKPNNTWQVLEAGANA-IVAGSAVFN-APNYAEA 213
Cdd:PRK09722 159 LKALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVfIVGTSGLFNlDEDIDEA 211
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
5-215 |
1.05e-34 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 122.84 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 5 IVVAPSILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAKA 84
Cdd:PRK08005 1 MILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 85 GADIISVHVEHNASPhlHRTLCQIRELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALR 164
Cdd:PRK08005 81 RPGWIFIHAESVQNP--SEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
1TQJ_E 165 QMCDERglDPWieVDGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIA 215
Cdd:PRK08005 159 EHFPAA--ECW--ADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLS 205
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
11-206 |
7.97e-22 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 89.55 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 11 ILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLivdAIRPLTKKTL-DVHLMIVEPEKYVEDFAKAGADII 89
Cdd:PRK08091 19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAI---AIKQFPTHCFkDVHLMVRDQFEVAKACVAAGADIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 90 SVHVEHNASphLHRTLCQIRELGKKA--GAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRQMC 167
Cdd:PRK08091 96 TLQVEQTHD--LALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVENRL 173
|
170 180 190
....*....|....*....|....*....|....*....
1TQJ_E 168 DERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVFN 206
Cdd:PRK08091 174 GNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFS 212
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
11-205 |
2.46e-19 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 83.58 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 11 ILSADFSRLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKtlDVHLMIVEPEKYVEDFAKAGADIIS 90
Cdd:PRK14057 26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK--DVHLMVADQWTAAQACVKAGAHCIT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 91 VHVEHNAspHLHRTLCQI---------RELGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIR 161
Cdd:PRK14057 104 LQAEGDI--HLHHTLSWLgqqtvpvigGEMPVIRGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1TQJ_E 162 ALRQMCDERGLDPWIEVDGGLKPNNTWQVLEAGANAIVAGSAVF 205
Cdd:PRK14057 182 QLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
18-202 |
4.76e-12 |
|
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: 62.60 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 18 RLGEEIKAVDEAGADWIHVDVMDGRFVPNITIGPLIVDAIRPLTKKTLDVHLMIVEPEKYVEDFAK----AGADIISVHV 93
Cdd:cd04722 13 DPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGADGVEIHG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 94 EHNASPHLHRTLC-QIRE--LGKKAGAVLNPSTPLDFLEYVLPVCDLILIMSVNPGFGGQSFIPEVLPKIRALRqmcdeR 170
Cdd:cd04722 93 AVGYLAREDLELIrELREavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK-----R 167
|
170 180 190
....*....|....*....|....*....|...
1TQJ_E 171 GLDPWIEVDGGLKPNNT-WQVLEAGANAIVAGS 202
Cdd:cd04722 168 GSKVPVIAGGGINDPEDaAEALALGADGVIVGS 200
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
11-213 |
4.49e-05 |
|
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: 43.02 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 11 ILSADFSRLGEEIKAVDEAGAdwiHVDVmdgrFVPNITI----GPLIVDAIRPLTK------KTLDV-HLMivepEKYVE 79
Cdd:pfam00215 4 CVALDVPTLEEALELADELGP---YVDI----LKVGTPLfeafGLKLVAELRKHGFlifldlKFADIgNTV----AKQAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 80 DFAKAGADIISVHvehnASPHLhRTLCQIRELGKKAG------AVLNPSTPLDFL-EYVLPVCDLILIMSV-----NPGF 147
Cdd:pfam00215 73 YKAKLGADIVTVH----AYAGE-GTLKAAKEAAEEYGrglllvAELSSKGSLDLQeEGDLGYTQEIVHRAAdlaagVDGV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1TQJ_E 148 --GGQSFIPEVLPKIRALRqmcdeRGLDPWIEVDGGLKPNNTWQV-LEAGANAIVAGSAVFNAPNYAEA 213
Cdd:pfam00215 148 vaSATEALREILPDFLILT-----PGIGLQGGDAGGQQRVTTPAVaKEAGADIIIVGRGITGAGDPVAA 211
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
180-215 |
6.66e-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: 39.42 E-value: 6.66e-04
10 20 30
....*....|....*....|....*....|....*.
1TQJ_E 180 GGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIA 215
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAAR 192
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
180-215 |
1.93e-03 |
|
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: 38.24 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|....*.
1TQJ_E 180 GGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIA 215
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAAR 197
|
|
| PRAI |
cd00405 |
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ... |
21-193 |
4.34e-03 |
|
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.
Pssm-ID: 238237 Cd Length: 203 Bit Score: 37.17 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 21 EEIKAVDEAGADWIHVDVMDG--RFVPNITIgPLIVDAIRPLTKKtldVHLMIVEPEKYVEDFAKA-GADIIsvhvehna 97
Cdd:cd00405 10 EDALAAAEAGADAIGFIFAPKspRYVSPEQA-REIVAALPPFVKR---VGVFVNEDLEEILEIAEElGLDVV-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TQJ_E 98 spHLHRTLCQ--IRELGKKAGA----VLNPSTPLDFLEYVL--PVCDLILIMSVNPGFG---GQSFIPEVLPKIRALRqm 166
Cdd:cd00405 78 --QLHGDESPeyCAQLRARLGLpvikAIRVKDEEDLEKAAAyaGEVDAILLDSKSGGGGggtGKTFDWSLLRGLASRK-- 153
|
170 180
....*....|....*....|....*..
1TQJ_E 167 cdergldPWIeVDGGLKPNNtwqVLEA 193
Cdd:cd00405 154 -------PVI-LAGGLTPDN---VAEA 169
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
162-216 |
9.42e-03 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 36.07 E-value: 9.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
1TQJ_E 162 ALRQMCDERGLDPWIEVdGGLKPNNTWQVLEAGANAIVAGSAVFNAPNYAEAIAG 216
Cdd:TIGR00693 142 LLREIAATLIDIPIVAI-GGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKR 195
|
|
| |
