|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-222 |
5.54e-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: 385.20 E-value: 5.54e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 4 YLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 84 AGASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRR 163
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489113708 164 RIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAKV 222
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-221 |
3.34e-133 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 373.36 E-value: 3.34e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 1 MKQYLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGiTAPIDVHLMVKPVDRIVPD 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVT-KLPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 161 VRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAK 221
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-216 |
6.08e-127 |
|
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: 356.97 E-value: 6.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 6 IAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAAAG 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 86 ASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRI 165
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489113708 166 DESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMR 216
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-216 |
6.90e-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: 349.47 E-value: 6.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 5 LIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGiTAPIDVHLMVKPVDRIVPDFAAA 84
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 85 GASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRR 164
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489113708 165 IDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMR 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 |
2.94e-120 |
|
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: 339.69 E-value: 2.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 6 IAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAAAG 85
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 86 ASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRI 165
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489113708 166 DESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIF 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 |
5.54e-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: 385.20 E-value: 5.54e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 4 YLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 84 AGASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRR 163
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489113708 164 RIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAKV 222
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-221 |
3.34e-133 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 373.36 E-value: 3.34e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 1 MKQYLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGiTAPIDVHLMVKPVDRIVPD 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVT-KLPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 161 VRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAK 221
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-216 |
6.08e-127 |
|
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: 356.97 E-value: 6.08e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 6 IAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAAAG 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 86 ASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRI 165
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489113708 166 DESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMR 216
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-216 |
6.90e-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: 349.47 E-value: 6.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 5 LIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGiTAPIDVHLMVKPVDRIVPDFAAA 84
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 85 GASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRR 164
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489113708 165 IDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMR 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 |
2.94e-120 |
|
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: 339.69 E-value: 2.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 6 IAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPDFAAAG 85
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 86 ASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRI 165
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489113708 166 DESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIF 203
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-223 |
6.27e-113 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 322.34 E-value: 6.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 1 MKQYLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPD 80
Cdd:PLN02334 5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKH-TDAPLDCHLMVTNPEDYVPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEAS--EHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDK--LDVILLMSVNPGFGGQSFIPQTLD 156
Cdd:PLN02334 84 FAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489113708 157 KLREVRRRIDEsgydIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAKVS 223
Cdd:PLN02334 164 KVRALRKKYPE----LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAA 226
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
5-221 |
5.38e-76 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 228.72 E-value: 5.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 5 LIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGITAPIDVHLMVKPVDRIVPDFAAA 84
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 85 GASIITFHPEA-SEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDK--LDVILLMSVNPGFGGQSFIPQTLDKLREV 161
Cdd:PTZ00170 88 GASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 162 RRRidesgY-DIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAK 221
Cdd:PTZ00170 168 RKR-----YpHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQK 223
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
2-221 |
3.23e-64 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 198.68 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 2 KQYLIAPSILSADFARLGEDTaRALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGiTAPIDVHLMVKPVDRIVPDF 81
Cdd:PRK09722 1 MRMKISPSLMCMDLLKFKEQI-EFLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLA-SKPLDVHLMVTDPQDYIDQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 82 AAAGASIITFHPE-ASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK09722 79 ADAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489113708 161 VRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAG-SAIFD-QPDYKKVIDEMRNELAK 221
Cdd:PRK09722 159 LKALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNlDEDIDEAWDIMTAQIEA 221
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
5-209 |
1.12e-31 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 114.75 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 5 LIAPSILSADFARLGedtaRALTAGADV----VHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMVKPVDRIVPD 80
Cdd:PRK08005 2 ILHPSLASADPLRYA----EALTALHDAplgsLHLDIEDTSFINNITFGMKTIQAVAQQ-TRHPLSFHLMVSSPQRWLPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEASEHVDRTLQLIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLRE 160
Cdd:PRK08005 77 LAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489113708 161 VRRRIDESgydiRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYK 209
Cdd:PRK08005 157 SREHFPAA----ECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYD 201
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
1-219 |
5.24e-28 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 105.73 E-value: 5.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 1 MKQYLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGITapiDVHLMVKPVDRIVPD 80
Cdd:PRK08091 10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK---DVHLMVRDQFEVAKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEASEHVDRTLQLIKEHGCKA--GLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKL 158
Cdd:PRK08091 87 CVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 159 REVRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNEL 219
Cdd:PRK08091 167 IQVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSL 227
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
1-203 |
1.53e-15 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 73.18 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 1 MKQYLIAPSILSADFARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYGITapiDVHLMVKPVDRIVPD 80
Cdd:PRK14057 17 LASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK---DVHLMVADQWTAAQA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 81 FAAAGASIITFHPEASEHVDRTLQLIKEHGCKA---------GLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFI 151
Cdd:PRK14057 94 CVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489113708 152 PQTLDKLREVRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIF 203
Cdd:PRK14057 174 SDLHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
16-200 |
3.13e-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: 46.04 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 16 ARLGEDTARALTAGADVVHFDVMDNHYVPNLTIGPMVLKSLRKYgITAPIDVHLMV----KPVDRIVPDFAAAGASIITF 91
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAE-TDLPLGVQLAIndaaAAVDIAAAAARAAGADGVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 92 HPEASEHVDRTLQLIKEH-----GCKAGLVFNPATPLSYLDYVMDKLDVILLMSVNPGFGGQSFIPQTLDKLREVRRRid 166
Cdd:cd04722 91 HGAVGYLAREDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRG-- 168
|
170 180 190
....*....|....*....|....*....|....*
gi 489113708 167 esgYDIRLEVDGGVKV-NNIGEIAAAGADMFVAGS 200
Cdd:cd04722 169 ---SKVPVIAGGGINDpEDAAEALALGADGVIVGS 200
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
152-216 |
1.91e-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: 43.66 E-value: 1.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489113708 152 PQTLDKLREVRRRIDesgydIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMR 216
Cdd:cd00564 136 PLGLELLREIAELVE-----IPVVAIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
152-222 |
2.74e-05 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 43.64 E-value: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 152 PQTLDKLREVRRRIDESGYDIrlevdGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAKV 222
Cdd:COG0352 141 PLGLEGLAWWAELVEIPVVAI-----GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
152-222 |
8.33e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.09 E-value: 8.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489113708 152 PQTLDKLREVRRRIDesgyDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNELAKV 222
Cdd:PRK00043 145 PQGLEGLREIRAAVG----DIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAA 211
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
165-219 |
8.04e-04 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 39.61 E-value: 8.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489113708 165 IDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEMRNEL 219
Cdd:PRK13307 324 IKKAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKL 378
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
154-202 |
1.22e-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: 1.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489113708 154 TLDKLREVRRRIDESGYDIRLEVDGGVKVNNIGEIAAAGADMFVAGSAI 202
Cdd:pfam01729 110 SPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
154-206 |
1.43e-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: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 489113708 154 TLDKLREVRRRIDESgydIRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQP 206
Cdd:COG0157 213 SPEELREAVALLRGR---ALLEASGGITLENIRAYAETGVDYISVGALTHSAP 262
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
93-212 |
1.87e-03 |
|
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: 38.43 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113708 93 PEASEHVDRtlqlIKEHGCKAGLVFNPATPLSYLDYVMDKLDVILLmsvnpgfggQSFIPQTLDKLREVRRRIDEsgyDI 172
Cdd:cd01573 168 PEPLKALAR----LRATAPEKKIVVEVDSLEEALAAAEAGADILQL---------DKFSPEELAELVPKLRSLAP---PV 231
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489113708 173 RLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQP-DYKKVI 212
Cdd:cd01573 232 LLAAAGGINIENAAAYAAAGADILVTSAPYYAKPaDIKVKI 272
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
154-200 |
4.19e-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: 37.45 E-value: 4.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489113708 154 TLDKLREVRRRIDESGyDIRLEVDGGVKVNNIGEIAAAGADMFVAGS 200
Cdd:cd01568 211 SPEELKEAVKLLKGLP-RVLLEASGGITLENIRAYAETGVDVISTGA 256
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
172-215 |
7.77e-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: 36.40 E-value: 7.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489113708 172 IRLEVDGGVKVNNIGEIAAAGADMFVAGSAIFDQPDYKKVIDEM 215
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| |
