|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
7-237 |
2.87e-143 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 399.76 E-value: 2.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 7 DKFSKSDIIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQR 86
Cdd:PLN02334 1 DKFSKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 87 VPDFIKAGADIVSVHCELASTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDV--VDLVLIMSVNPGFGGQSFIES 164
Cdd:PLN02334 81 VPDFAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3264792 165 QVKKISDLRKMCVEKgvnpWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRPEPVAV 237
Cdd:PLN02334 161 MMDKVRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVAV 229
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
14-229 |
1.02e-135 |
|
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: 380.19 E-value: 1.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 14 IIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKA 93
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLR 173
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3264792 174 KMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKAS 229
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
15-227 |
1.01e-126 |
|
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: 357.17 E-value: 1.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 15 IVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAG 94
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 95 ADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 174
Cdd:cd00429 81 ADIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3264792 175 MCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIK 227
Cdd:cd00429 159 LIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
15-214 |
4.57e-115 |
|
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: 326.98 E-value: 4.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 15 IVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAG 94
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 95 ADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 174
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3264792 175 MCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVF 214
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
16-227 |
1.14e-114 |
|
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: 326.54 E-value: 1.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 16 VSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAGA 95
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 96 DIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRKM 175
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3264792 176 CVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIK 227
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
7-237 |
2.87e-143 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 399.76 E-value: 2.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 7 DKFSKSDIIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQR 86
Cdd:PLN02334 1 DKFSKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 87 VPDFIKAGADIVSVHCELASTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDV--VDLVLIMSVNPGFGGQSFIES 164
Cdd:PLN02334 81 VPDFAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3264792 165 QVKKISDLRKMCVEKgvnpWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRPEPVAV 237
Cdd:PLN02334 161 MMDKVRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVAV 229
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
14-229 |
1.02e-135 |
|
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: 380.19 E-value: 1.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 14 IIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKA 93
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLR 173
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3264792 174 KMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKAS 229
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
14-232 |
7.37e-129 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 362.96 E-value: 7.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 14 IIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKA 93
Cdd:PRK05581 4 VLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLR 173
Cdd:PRK05581 84 GADIITFHVE--ASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3264792 174 KMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRP 232
Cdd:PRK05581 162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
15-227 |
1.01e-126 |
|
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: 357.17 E-value: 1.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 15 IVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAG 94
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 95 ADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 174
Cdd:cd00429 81 ADIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3264792 175 MCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIK 227
Cdd:cd00429 159 LIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
15-214 |
4.57e-115 |
|
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: 326.98 E-value: 4.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 15 IVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAG 94
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 95 ADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 174
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3264792 175 MCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVF 214
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
16-227 |
1.14e-114 |
|
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: 326.54 E-value: 1.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 16 VSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAGA 95
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 96 DIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLRKM 175
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3264792 176 CVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIK 227
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
15-229 |
7.47e-74 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 223.71 E-value: 7.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 15 IVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLP-LDVHLMIVEPEQRVPDFIKA 93
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCElASTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLD--VVDLVLIMSVNPGFGGQSFIESQVKKISD 171
Cdd:PTZ00170 88 GASQFTFHIE-ATEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDtdLVDMVLVMTVEPGFGGQSFMHDMMPKVRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3264792 172 LRKmcveKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKAS 229
Cdd:PTZ00170 167 LRK----RYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
14-218 |
8.98e-67 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 206.00 E-value: 8.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 14 IIVSPSILSANFAKLGEQVKAVElAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKA 93
Cdd:PRK09722 3 MKISPSLMCMDLLKFKEQIEFLN-SKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCELASTiHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLR 173
Cdd:PRK09722 82 GADFITLHPETING-QAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3264792 174 KMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAG-SAVFGAKD 218
Cdd:PRK09722 161 ALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDE 206
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
14-219 |
1.93e-33 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 119.76 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 14 IIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKA 93
Cdd:PRK08005 1 MILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 94 GADIVSVHCElaSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISDLR 173
Cdd:PRK08005 81 RPGWIFIHAE--SVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3264792 174 KMCvekgvnPWIE--VDGGVTPANAYKVIEAGANALVAGSAVFGAKDY 219
Cdd:PRK08005 159 EHF------PAAEcwADGGITLRAARLLAAAGAQHLVIGRALFTTANY 200
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
16-229 |
5.80e-23 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 93.02 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 16 VSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALrPVTDLPlDVHLMIVEPEQRVPDFIKAGA 95
Cdd:PRK08091 15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQF-PTHCFK-DVHLMVRDQFEVAKACVAAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 96 DIVSVHCE----LASTIHLHRTvnqiKSLGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQVKKISD 171
Cdd:PRK08091 93 DIVTLQVEqthdLALTIEWLAK----QKTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3264792 172 LRKMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKAS 229
Cdd:PRK08091 169 VENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSS 226
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
16-228 |
5.94e-22 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 90.90 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 16 VSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALrPVTDLPlDVHLMIVEPEQRVPDFIKAGA 95
Cdd:PRK14057 22 LSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQACVKAGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 96 DIVSVHCElaSTIHLHRTVN-----QIKSLGAKA----GVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIESQV 166
Cdd:PRK14057 100 HCITLQAE--GDIHLHHTLSwlgqqTVPVIGGEMpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLH 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3264792 167 KKISDLRKMCVEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKA 228
Cdd:PRK14057 178 ERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDDRLVENTRSWRA 239
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
16-211 |
1.39e-16 |
|
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: 75.32 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 16 VSPSILSANFAK-LGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPD----F 90
Cdd:cd04722 1 VILALLAGGPSGdPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIaaaaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 91 IKAGADIVSVHCELASTI-HLHRTVNQIKS--LGAKAGVVLNPGTPLSTIEYVLDVVDLVLIMSVNPGFGGQSFIEsqvk 167
Cdd:cd04722 81 RAAGADGVEIHGAVGYLArEDLELIRELREavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVP---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 3264792 168 kISDLRKMCVEKGVNPWIEVDGGV-TPANAYKVIEAGANALVAGS 211
Cdd:cd04722 157 -IADLLLILAKRGSKVPVIAGGGInDPEDAAEALALGADGVIVGS 200
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
189-228 |
4.91e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.86 E-value: 4.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 3264792 189 GGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKA 228
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
189-228 |
5.66e-05 |
|
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: 42.51 E-value: 5.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 3264792 189 GGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKA 228
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
189-228 |
2.11e-04 |
|
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: 40.94 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 3264792 189 GGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKA 228
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRA 201
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
171-226 |
2.49e-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: 40.64 E-value: 2.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 3264792 171 DLRKMCVEKGVNpwIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGI 226
Cdd:cd04726 149 DLKKVKKLLGVK--VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
81-218 |
2.90e-04 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 41.18 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3264792 81 VEPEQRVPDFIKAGADIV---SVHCELASTIHLHRTV-NQIKSLGAKAGVVLnpgtplsTIEYVLDVVDL---VLIMSVN 153
Cdd:PRK06843 152 IDTIERVEELVKAHVDILvidSAHGHSTRIIELVKKIkTKYPNLDLIAGNIV-------TKEAALDLISVgadCLKVGIG 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3264792 154 PGFGGQSFIES-----QVKKISDLRKMCveKGVNPWIEVDGGVT-PANAYKVIEAGANALVAGSAVFGAKD 218
Cdd:PRK06843 225 PGSICTTRIVAgvgvpQITAICDVYEVC--KNTNICIIADGGIRfSGDVVKAIAAGADSVMIGNLFAGTKE 293
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
172-226 |
5.73e-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: 36.84 E-value: 5.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 3264792 172 LRKMCVEKGVNPWIEVdGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGI 226
Cdd:TIGR00693 143 LREIAATLIDIPIVAI-GGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
178-234 |
6.90e-03 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 36.91 E-value: 6.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 3264792 178 EKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRPEP 234
Cdd:PRK13307 326 KAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLKPDI 382
|
|
| |
