|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-222 |
3.70e-138 |
|
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: 385.58 E-value: 3.70e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 4 YLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAE 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 84 AGASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQ 163
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490307108 164 RIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAKV 222
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-221 |
1.91e-132 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 371.44 E-value: 1.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 1 MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGiTAPIDVHLMVKPVDRIIPD 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVT-KLPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 81 FAEAGASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 161 VRQRIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAK 221
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-216 |
1.92e-128 |
|
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: 360.82 E-value: 1.92e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 6 IAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAEAG 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 86 ASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQRI 165
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490307108 166 DASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMR 216
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-216 |
5.02e-124 |
|
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: 349.86 E-value: 5.02e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 5 LIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGiTAPIDVHLMVKPVDRIIPDFAEA 84
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 85 GASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQR 164
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490307108 165 IDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMR 216
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
6-203 |
2.13e-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: 337.77 E-value: 2.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 6 IAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAEAG 85
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 86 ASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQRI 165
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 490307108 166 DASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIF 203
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-222 |
3.70e-138 |
|
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: 385.58 E-value: 3.70e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 4 YLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAE 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 84 AGASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQ 163
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490307108 164 RIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAKV 222
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-221 |
1.91e-132 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 371.44 E-value: 1.91e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 1 MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGiTAPIDVHLMVKPVDRIIPD 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVT-KLPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 81 FAEAGASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 161 VRQRIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAK 221
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-216 |
1.92e-128 |
|
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: 360.82 E-value: 1.92e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 6 IAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAEAG 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 86 ASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQRI 165
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490307108 166 DASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMR 216
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-216 |
5.02e-124 |
|
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: 349.86 E-value: 5.02e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 5 LIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGiTAPIDVHLMVKPVDRIIPDFAEA 84
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 85 GASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQR 164
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490307108 165 IDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMR 216
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
6-203 |
2.13e-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: 337.77 E-value: 2.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 6 IAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAEAG 85
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 86 ASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQRI 165
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 490307108 166 DASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIF 203
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-223 |
1.68e-112 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 321.18 E-value: 1.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 1 MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPD 80
Cdd:PLN02334 5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKH-TDAPLDCHLMVTNPEDYVPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 81 FAEAGASIITFHPEAS--EHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDK--LDVILLMSVNPGFGGQSFIPQTLD 156
Cdd:PLN02334 84 FAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490307108 157 KLREVRQRIDasgyDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAKVS 223
Cdd:PLN02334 164 KVRALRKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAA 226
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
5-221 |
3.22e-75 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 226.79 E-value: 3.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 5 LIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITAPIDVHLMVKPVDRIIPDFAEA 84
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 85 GASIITFHPEA-SEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDK--LDVILLMSVNPGFGGQSFIPQTLDKLREV 161
Cdd:PTZ00170 88 GASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 162 RQRidasgY-DIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAK 221
Cdd:PTZ00170 168 RKR-----YpHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQK 223
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
2-221 |
4.17e-63 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 195.98 E-value: 4.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 2 KQYLIAPSILSADFARLGEDTAkALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGiTAPIDVHLMVKPVDRIIPDF 81
Cdd:PRK09722 1 MRMKISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLA-SKPLDVHLMVTDPQDYIDQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 82 AEAGASIITFHPE-ASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK09722 79 ADAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490307108 161 VRQRIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAG-SAIFG-QPDYKKVIDQMRSELAK 221
Cdd:PRK09722 159 LKALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNlDEDIDEAWDIMTAQIEA 221
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
5-214 |
1.37e-31 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 114.75 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 5 LIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMVKPVDRIIPDFAEA 84
Cdd:PRK08005 2 ILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQ-TRHPLSFHLMVSSPQRWLPWLAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 85 GASIITFHPEASEHVDRSLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQR 164
Cdd:PRK08005 81 RPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490307108 165 IDASgydiRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQ 214
Cdd:PRK08005 161 FPAA----ECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQ 206
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
1-219 |
9.95e-26 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 99.95 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 1 MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITapiDVHLMVKPVDRIIPD 80
Cdd:PRK08091 10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK---DVHLMVRDQFEVAKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 81 FAEAGASIITFHPEASEHVDRSLQLIKEHGCKA--GLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKL 158
Cdd:PRK08091 87 CVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 159 REVRQRIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSEL 219
Cdd:PRK08091 167 IQVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSL 227
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
1-203 |
6.26e-15 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 71.64 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 1 MKQYLIAPSILSADFARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYGITapiDVHLMVKPVDRIIPD 80
Cdd:PRK14057 17 LASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK---DVHLMVADQWTAAQA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 81 FAEAGASIITFHPEASEHVDRSLQLIKEHGCKA---------GLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSfi 151
Cdd:PRK14057 94 CVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKM-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490307108 152 pQTLDKLREVRQRIDASGyDIR----LEVDGGVKASNIGEIAAAGADMFVAGSAIF 203
Cdd:PRK14057 172 -RSSDLHERVAQLLCLLG-DKRegkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
152-222 |
2.14e-06 |
|
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: 46.72 E-value: 2.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 152 PQTLDKLREVRQRIDASGYDIrlevdGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAKV 222
Cdd:COG0352 141 PLGLEGLAWWAELVEIPVVAI-----GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
152-217 |
7.06e-06 |
|
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: 45.20 E-value: 7.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490307108 152 PQTLDKLREVRQRIDASGYDIrlevdGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRS 217
Cdd:cd00564 136 PLGLELLREIAELVEIPVVAI-----GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
16-200 |
9.29e-06 |
|
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: 44.88 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 16 ARLGEDTAKALAAGADVVHFDVMDNHYVPNLTIGPMVLKSLRNYgITAPIDVHLMV----KPVDRIIPDFAEAGASIITF 91
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAE-TDLPLGVQLAIndaaAAVDIAAAAARAAGADGVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 92 HPEASEHVDRSLQLIKEH-----GCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRQRid 166
Cdd:cd04722 91 HGAVGYLAREDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRG-- 168
|
170 180 190
....*....|....*....|....*....|....*
gi 490307108 167 asgYDIRLEVDGGVKASNIG-EIAAAGADMFVAGS 200
Cdd:cd04722 169 ---SKVPVIAGGGINDPEDAaEALALGADGVIVGS 200
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
93-212 |
9.89e-05 |
|
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide.
Pssm-ID: 238807 [Multi-domain] Cd Length: 272 Bit Score: 42.29 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490307108 93 PEASEHVDRslqlIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLmsvnpgfggQSFIPQTLdklREVRQRIDASGYDI 172
Cdd:cd01573 168 PEPLKALAR----LRATAPEKKIVVEVDSLEEALAAAEAGADILQL---------DKFSPEEL---AELVPKLRSLAPPV 231
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490307108 173 RLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQP-DYKKVI 212
Cdd:cd01573 232 LLAAAGGINIENAAAYAAAGADILVTSAPYYAKPaDIKVKI 272
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
152-222 |
1.53e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 41.32 E-value: 1.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490307108 152 PQTLDKLREVRQRIDasgyDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSELAKV 222
Cdd:PRK00043 145 PQGLEGLREIRAAVG----DIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
154-206 |
1.18e-03 |
|
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold.
Pssm-ID: 396337 Cd Length: 169 Bit Score: 38.45 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490307108 154 TLDKLREVRQRIDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQP 206
Cdd:pfam01729 110 SPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVP 162
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
154-200 |
1.47e-03 |
|
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439927 [Multi-domain] Cd Length: 272 Bit Score: 38.85 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490307108 154 TLDKLREVRQRIDASgydIRLEVDGGVKASNIGEIAAAGADMFVAGS 200
Cdd:COG0157 213 SPEELREAVALLRGR---ALLEASGGITLENIRAYAETGVDYISVGA 256
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
154-206 |
2.01e-03 |
|
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
Pssm-ID: 238802 [Multi-domain] Cd Length: 269 Bit Score: 38.22 E-value: 2.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490307108 154 TLDKLREVRQRIDASGyDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQP 206
Cdd:cd01568 211 SPEELKEAVKLLKGLP-RVLLEASGGITLENIRAYAETGVDVISTGALTHSAP 262
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
155-219 |
2.58e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 38.33 E-value: 2.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490307108 155 LDKLREVRQRIDASGYDIrlevdGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKVIDQMRSEL 219
Cdd:PRK02615 283 LEYLKYAAKEAPIPWFAI-----GGIDKSNIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQL 342
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
165-216 |
3.71e-03 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 37.68 E-value: 3.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490307108 165 IDASGYDIRLEVDGGVKASNIGEIAAAGADMFVAGSAIFGQPDYKKV-----------IDQMR 216
Cdd:PRK13307 324 IKKAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAaedflnklkpdIDQFR 386
|
|
| |
