|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
5-223 |
2.07e-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: 378.65 E-value: 2.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 5 FLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAK 84
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 85 AGASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRR 164
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2530922974 165 LIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAELSHV 223
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
2-220 |
7.10e-131 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 367.59 E-value: 7.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 2 MKDFLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGIeAPIDVHLMVKPVDRIIPD 81
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTK-LPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 82 FAKAGASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQ 161
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2530922974 162 VRRLIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAEL 220
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
7-217 |
3.19e-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: 357.74 E-value: 3.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 7 IAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAKAG 86
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 87 ASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRLI 166
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2530922974 167 DESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMR 217
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-217 |
9.55e-120 |
|
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: 339.07 E-value: 9.55e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 6 LIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGiEAPIDVHLMVKPVDRIIPDFAKA 85
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 86 GASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRL 165
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2530922974 166 IDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMR 217
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
7-204 |
6.97e-118 |
|
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: 333.91 E-value: 6.97e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 7 IAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAKAG 86
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 87 ASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRLI 166
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2530922974 167 DESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIF 204
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
5-223 |
2.07e-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: 378.65 E-value: 2.07e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 5 FLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAK 84
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKH-TDLPLDVHLMIENPDRYIEAFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 85 AGASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRR 164
Cdd:COG0036 80 AGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2530922974 165 LIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAELSHV 223
Cdd:COG0036 160 LIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
2-220 |
7.10e-131 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 367.59 E-value: 7.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 2 MKDFLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGIeAPIDVHLMVKPVDRIIPD 81
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTK-LPLDVHLMVENPDRYVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 82 FAKAGASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQ 161
Cdd:PRK05581 80 FAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2530922974 162 VRRLIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAEL 220
Cdd:PRK05581 160 LRKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAEL 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
7-217 |
3.19e-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: 357.74 E-value: 3.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 7 IAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAKAG 86
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKY-TDLPIDVHLMVENPDRYIEDFAEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 87 ASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRLI 166
Cdd:TIGR01163 80 ADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2530922974 167 DESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMR 217
Cdd:TIGR01163 160 DELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-217 |
9.55e-120 |
|
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: 339.07 E-value: 9.55e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 6 LIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGiEAPIDVHLMVKPVDRIIPDFAKA 85
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHT-DLPLDVHLMVENPERYIEAFAKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 86 GASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRL 165
Cdd:cd00429 80 GADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLREL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2530922974 166 IDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMR 217
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
7-204 |
6.97e-118 |
|
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: 333.91 E-value: 6.97e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 7 IAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAKAG 86
Cdd:pfam00834 2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPL-TDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 87 ASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRLI 166
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 2530922974 167 DESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIF 204
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-220 |
6.71e-110 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 314.63 E-value: 6.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 1 MMKDFLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIP 80
Cdd:PLN02334 4 SKNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKH-TDAPLDCHLMVTNPEDYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 81 DFAKAGASLITFHPEAS--DHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDK--LDVILLMSVNPGFGGQSFIPGTL 156
Cdd:PLN02334 83 DFAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2530922974 157 DKLRQVRRLIDEsgrdIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAEL 220
Cdd:PLN02334 163 DKVRALRKKYPE----LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASV 222
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
6-218 |
2.59e-73 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 221.78 E-value: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 6 LIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGIEAPIDVHLMVKPVDRIIPDFAKA 85
Cdd:PTZ00170 8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTFLDCHLMVSNPEKWVDDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 86 GASLITFHPEA-SDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDK--LDVILLMSVNPGFGGQSFIPGTLDKLRQV 162
Cdd:PTZ00170 88 GASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2530922974 163 RRLIdesgRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRA 218
Cdd:PTZ00170 168 RKRY----PHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRE 219
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
6-205 |
1.27e-57 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 182.12 E-value: 1.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 6 LIAPSILSADFARLGDDVAkVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGiEAPIDVHLMVKPVDRIIPDFAKA 85
Cdd:PRK09722 4 KISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLA-SKPLDVHLMVTDPQDYIDQLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 86 GASLITFHPE-ASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRR 164
Cdd:PRK09722 82 GADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2530922974 165 LIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAG-SAIFS 205
Cdd:PRK09722 162 LRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFN 203
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
6-218 |
2.18e-33 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 119.37 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 6 LIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMVKPVDRIIPDFAKA 85
Cdd:PRK08005 2 ILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQ-TRHPLSFHLMVSSPQRWLPWLAAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 86 GASLITFHPEASDHVDRSLGLIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRL 165
Cdd:PRK08005 81 RPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2530922974 166 IDESgrdiRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRA 218
Cdd:PRK08005 161 FPAA----ECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQFTA 209
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
7-221 |
5.58e-28 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 105.73 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 7 IAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGIEapiDVHLMVKPVDRIIPDFAKAG 86
Cdd:PRK08091 15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK---DVHLMVRDQFEVAKACVAAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 87 ASLITFHPEASDHVDRSLGLIKEQGCQA--GLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRR 164
Cdd:PRK08091 92 ADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVEN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2530922974 165 LIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAELS 221
Cdd:PRK08091 172 RLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSLM 228
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
1-204 |
6.95e-18 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 79.73 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 1 MMKDFLIAPSILSADFARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYGIEapiDVHLMVKPVDRIIP 80
Cdd:PRK14057 16 LLASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK---DVHLMVADQWTAAQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 81 DFAKAGASLITFHPEASDHVDRSLGLIKEQGCQA---------GLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSF 151
Cdd:PRK14057 93 ACVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2530922974 152 IPGTLDKLRQVRRLIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIF 204
Cdd:PRK14057 173 SSDLHERVAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
179-221 |
2.80e-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: 2.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2530922974 179 GGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAELS 221
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALE 204
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
179-218 |
8.71e-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: 41.74 E-value: 8.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2530922974 179 GGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRA 218
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
127-207 |
1.09e-04 |
|
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: 42.08 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 127 LEYVMDKLDVILL--MSvnpgfggqsfipgtLDKLRQVRRLIDESGRdIRLEIDGGVKVENIREIAQAGADMFVAGSAIF 204
Cdd:cd01568 195 EEALEAGADIIMLdnMS--------------PEELKEAVKLLKGLPR-VLLEASGGITLENIRAYAETGVDVISTGALTH 259
|
...
gi 2530922974 205 SRP 207
Cdd:cd01568 260 SAP 262
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
17-201 |
1.14e-04 |
|
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: 41.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 17 ARLGDDVAKVLAAGADVVHFDVMDNHYVPNLTIGPMVCQALRDYgIEAPIDVHLMV----KPVDRIIPDFAKAGASLITF 92
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAE-TDLPLGVQLAIndaaAAVDIAAAAARAAGADGVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 93 HPEASDHVDRSLGLIKE-----QGCQAGLVLNPATPLTCLEYVMDKLDVILLMSVNPGFGGQSFIPGTLDKLRQVRRlid 167
Cdd:cd04722 91 HGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKR--- 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2530922974 168 esGRDIRLEIDGGVKV-ENIREIAQAGADMFVAGS 201
Cdd:cd04722 168 --GSKVPVIAGGGINDpEDAAEALALGADGVIVGS 200
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
94-213 |
2.00e-04 |
|
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: 41.52 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530922974 94 PEASDHVDRslglIKEQGCQAGLVLNPATPLTCLEYVMDKLDVILLmsvnpgfggQSFIPGTLDKLRQvrrLIDESGRDI 173
Cdd:cd01573 168 PEPLKALAR----LRATAPEKKIVVEVDSLEEALAAAEAGADILQL---------DKFSPEELAELVP---KLRSLAPPV 231
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2530922974 174 RLEIDGGVKVENIREIAQAGADMFVAGSAIFSRP-DYKAVI 213
Cdd:cd01573 232 LLAAAGGINIENAAAYAAAGADILVTSAPYYAKPaDIKVKI 272
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
153-224 |
2.28e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 40.94 E-value: 2.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2530922974 153 PGTLDKLRQVRRLIdesgRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAELSHVK 224
Cdd:PRK00043 145 PQGLEGLREIRAAV----GDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
155-207 |
2.38e-04 |
|
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: 40.37 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2530922974 155 TLDKLRQVRRLIDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRP 207
Cdd:pfam01729 110 SPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVP 162
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
155-205 |
3.32e-04 |
|
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: 40.77 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2530922974 155 TLDKLRQVRRLIDesGRdIRLEIDGGVKVENIREIAQAGADMFVAGSAIFS 205
Cdd:COG0157 213 SPEELREAVALLR--GR-ALLEASGGITLENIRAYAETGVDYISVGALTHS 260
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
149-216 |
6.02e-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: 39.49 E-value: 6.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2530922974 149 QSFIPGTLDKLRQVRRLIDesgrdIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEM 216
Cdd:cd04726 140 AAGGWWPEDDLKKVKKLLG-----VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
150-207 |
2.33e-03 |
|
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase 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, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.
Pssm-ID: 238286 [Multi-domain] Cd Length: 281 Bit Score: 37.99 E-value: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2530922974 150 SFIPGTLDKLRQVRRLIDESGR----DIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRP 207
Cdd:cd00516 213 SGSPEELDPAVLILKARAHLDGkglpRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAP 274
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
166-220 |
3.51e-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: 3.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2530922974 166 IDESGRDIRLEIDGGVKVENIREIAQAGADMFVAGSAIFSRPDYKAVIDEMRAEL 220
Cdd:PRK13307 324 IKKAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKL 378
|
|
| |
