|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
4-229 |
2.34e-145 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 404.77 E-value: 2.34e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 4 DKFSKSDIIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQR 83
Cdd:PLN02334 1 DKFSKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 84 VPDFIKAGADIVSVHCEQSSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDA--VDLVLIMSVNPGFGGQSFIES 161
Cdd:PLN02334 81 VPDFAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4930130 162 QVKKISDLRKICAERglnpWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIKTSKRP 229
Cdd:PLN02334 161 MMDKVRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEK 224
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
11-224 |
3.63e-137 |
|
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: 383.27 E-value: 3.63e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 11 IIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKA 90
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 4930130 171 KICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALR 212
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
12-224 |
8.17e-130 |
|
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: 364.49 E-value: 8.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 12 IVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAG 91
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 92 ADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 171
Cdd:cd00429 81 ADIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4930130 172 ICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:cd00429 159 LIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
12-211 |
9.68e-119 |
|
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: 336.23 E-value: 9.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 12 IVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAG 91
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 92 ADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 171
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4930130 172 ICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVF 211
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
13-224 |
8.92e-116 |
|
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: 329.24 E-value: 8.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 13 VSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAGA 92
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 93 DIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRKI 172
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4930130 173 CAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
4-229 |
2.34e-145 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 404.77 E-value: 2.34e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 4 DKFSKSDIIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQR 83
Cdd:PLN02334 1 DKFSKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 84 VPDFIKAGADIVSVHCEQSSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDA--VDLVLIMSVNPGFGGQSFIES 161
Cdd:PLN02334 81 VPDFAKAGASIFTFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4930130 162 QVKKISDLRKICAERglnpWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIKTSKRP 229
Cdd:PLN02334 161 MMDKVRALRKKYPEL----DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEK 224
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
11-224 |
3.63e-137 |
|
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: 383.27 E-value: 3.63e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 11 IIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKA 90
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:COG0036 81 GADIITVHAE--ATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 4930130 171 KICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:COG0036 159 ELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALR 212
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
11-229 |
3.73e-132 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 371.05 E-value: 3.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 11 IIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKA 90
Cdd:PRK05581 4 VLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:PRK05581 84 GADIITFHVE--ASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 4930130 171 KICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIKTSKRP 229
Cdd:PRK05581 162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
12-224 |
8.17e-130 |
|
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: 364.49 E-value: 8.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 12 IVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAG 91
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 92 ADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 171
Cdd:cd00429 81 ADIITFHAE--ATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 4930130 172 ICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:cd00429 159 LIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
12-211 |
9.68e-119 |
|
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: 336.23 E-value: 9.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 12 IVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAG 91
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 92 ADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRK 171
Cdd:pfam00834 81 ADIISFHAE--ATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 4930130 172 ICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVF 211
Cdd:pfam00834 159 MIDERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
13-224 |
8.92e-116 |
|
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: 329.24 E-value: 8.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 13 VSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKAGA 92
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 93 DIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLRKI 172
Cdd:TIGR01163 81 DIITVHPE--ASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4930130 173 CAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIK 224
Cdd:TIGR01163 159 IDELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
12-226 |
3.18e-75 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 227.18 E-value: 3.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 12 IVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLP-LDVHLMIVEPDQRVPDFIKA 90
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEQSSTIHLhRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDA--VDLVLIMSVNPGFGGQSFIESQVKKISD 168
Cdd:PTZ00170 88 GASQFTFHIEATEDDPK-AVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 4930130 169 LRKicAERGLNpwIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIKTS 226
Cdd:PTZ00170 167 LRK--RYPHLN--IQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
11-219 |
2.19e-68 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 209.47 E-value: 2.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 11 IIVSPSILSANFSKLGEQVKAIEQAGcDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKA 90
Cdd:PRK09722 3 MKISPSLMCMDLLKFKEQIEFLNSKA-DYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEQSSTiHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:PRK09722 82 GADFITLHPETING-QAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 4930130 171 KICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAG-SAVFG-APDYAEA 219
Cdd:PRK09722 161 ALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNlDEDIDEA 211
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
11-216 |
1.51e-32 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 117.45 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 11 IIVSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPDFIKA 90
Cdd:PRK08005 1 MILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 91 GADIVSVHCEqsSTIHLHRTINQIKSLGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:PRK08005 81 RPGWIFIHAE--SVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4930130 171 KicAERGLNPWieVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDY 216
Cdd:PRK08005 159 E--HFPAAECW--ADGGITLRAARLLAAAGAQHLVIGRALFTTANY 200
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
13-226 |
1.84e-23 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 94.17 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 13 VSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLrPITDLPlDVHLMIVEPDQRVPDFIKAGA 92
Cdd:PRK08091 15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQF-PTHCFK-DVHLMVRDQFEVAKACVAAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 93 DIVSVHCEQssTIHLHRTINQIKSLGAKA--GVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQVKKISDLR 170
Cdd:PRK08091 93 DIVTLQVEQ--THDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 4930130 171 KICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGIKTS 226
Cdd:PRK08091 171 NRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSS 226
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
13-208 |
4.05e-23 |
|
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: 92.26 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 13 VSPSILSANFSK-LGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLRPITDLPLDVHLMIVEPDQRVPD----F 87
Cdd:cd04722 1 VILALLAGGPSGdPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIaaaaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 88 IKAGADIVSVHCEQSSTI-HLHRTINQIKS--LGAKAGVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIEsqvk 164
Cdd:cd04722 81 RAAGADGVEIHGAVGYLArEDLELIRELREavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVP---- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 4930130 165 kISDLRKICAERGLNPWIEVDGGVG-PKNAYKVIEAGANALVAGS 208
Cdd:cd04722 157 -IADLLLILAKRGSKVPVIAGGGINdPEDAAEALALGADGVIVGS 200
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
13-211 |
1.91e-21 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 89.36 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 13 VSPSILSANFSKLGEQVKAIEQAGCDWIHVDVMDGRFVPNITIGPLVVDSLrPITDLPlDVHLMIVEPDQRVPDFIKAGA 92
Cdd:PRK14057 22 LSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQACVKAGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 93 DIVSVHCEqsSTIHLHRTIN-----QIKSLGAKA----GVVLNPGTPLTAIEYVLDAVDLVLIMSVNPGFGGQSFIESQV 163
Cdd:PRK14057 100 HCITLQAE--GDIHLHHTLSwlgqqTVPVIGGEMpvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLH 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4930130 164 KKISDLRKICAERGLNPWIEVDGGVGPKNAYKVIEAGANALVAGSAVF 211
Cdd:PRK14057 178 ERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
166-221 |
3.89e-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: 42.89 E-value: 3.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 4930130 166 ISDLRKICAERGLnPWIeVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIK 221
Cdd:cd00564 139 LELLREIAELVEI-PVV-AIGGITPENAAEVLAAGADGVAVISAITGADDPAAAAR 192
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
169-221 |
6.22e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.48 E-value: 6.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 4930130 169 LRKICAERGLNPWIEVdGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIK 221
Cdd:PRK00043 151 LREIRAAVGDIPIVAI-GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAAR 202
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
169-223 |
4.07e-04 |
|
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: 39.92 E-value: 4.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 4930130 169 LRKICAERGLNPWIEVdGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGI 223
Cdd:TIGR00693 143 LREIAATLIDIPIVAI-GGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
186-221 |
8.98e-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: 39.01 E-value: 8.98e-04
10 20 30
....*....|....*....|....*....|....*.
gi 4930130 186 GGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIK 221
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAAR 197
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
168-223 |
3.13e-03 |
|
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: 37.56 E-value: 3.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 4930130 168 DLRKICAERGLNpwIEVDGGVGPKNAYKVIEAGANALVAGSAVFGAPDYAEAIKGI 223
Cdd:cd04726 149 DLKKVKKLLGVK--VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
3-97 |
5.60e-03 |
|
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. The specific function of this group is unknown.
Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 36.92 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4930130 3 VDKFSKSDIIVSPSIlSANFSKLGEQV-KAIEQAGCDWIHVDVMDgrfvpnitigPLVVDSLRPITDLPLDVHLMI---V 78
Cdd:cd02911 132 IKALKETGVPVSVKI-RAGVDVDDEELaRLIEKAGADIIHVDAMD----------PGNHADLKKIRDISTELFIIGnnsV 200
|
90
....*....|....*....
gi 4930130 79 EPDQRVPDFIKAGADIVSV 97
Cdd:cd02911 201 TTIESAKEMFSYGADMVSV 219
|
|
| |
