|
Name |
Accession |
Description |
Interval |
E-value |
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
1-231 |
0e+00 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 498.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK08193 160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
|
|
| araD |
TIGR00760 |
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ... |
1-231 |
8.35e-169 |
|
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]
Pssm-ID: 129843 Cd Length: 231 Bit Score: 463.91 E-value: 8.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVVESHKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
1.95e-96 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 280.02 E-value: 1.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 3 EDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVEShKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 83 LYQAFPTIGGIVHTHSRHATIWAQAGQ-PIPATGTTHADYFYGTIPCTRKMTEaeingeyewETGNVIVETFEKQGIdaA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340763429 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
4.62e-69 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 210.46 E-value: 4.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEIngeyewETGNVIVETFEKqgida 160
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTE------ELAEAIAEALGD----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340763429 161 aqMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQSLLDKHYlRKHG 224
Cdd:COG0235 149 --RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
1.15e-62 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 193.15 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 7 RQVLEANLALPKHNLVTLTWGNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 87 FPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEIngeyewETGNVIVETFEKqgidaaQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGG------DRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 340763429 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
5.53e-62 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 191.70 E-value: 5.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 9 VLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVV-ESHKKPSSDTPTHRLLYQAF 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEgGGGPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 88 PTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYG-TIPCTRKMTEAEINGEYEWETGNVIVETFEKqgidaaqMPGV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPD-------RPAV 153
|
170 180 190
....*....|....*....|....*....|
gi 340763429 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
1-231 |
0e+00 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 498.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK08193 160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
|
|
| araD |
TIGR00760 |
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ... |
1-231 |
8.35e-169 |
|
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very close homologs of araD, the established L-ribulose-5-phosphate 4-epimerase of E. coli. SgbE, part of an operon for L-xylulose metabolism, also has L-ribulose-5-phosphate 4-epimerase activity; L-xylulose-5-phosphate may be converted into L-ribulose-5-phosphate by another product of that operon. The homolog to this family from Mycobacterium smegmatis is flanked by putative araB and araA genes, consistent with it also being araD. [Energy metabolism, Sugars]
Pssm-ID: 129843 Cd Length: 231 Bit Score: 463.91 E-value: 8.35e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVVESHKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
4.59e-160 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 441.95 E-value: 4.59e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVVESHKKPSSDTPTH 80
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
1.53e-131 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 369.83 E-value: 1.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVVESHKKPSSDTPTH 80
Cdd:PRK13213 1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK13213 81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
2-231 |
9.32e-127 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 357.57 E-value: 9.32e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 2 LEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTHR 81
Cdd:PRK12348 1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMS-GKVVEGEYRPSSDTATHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 82 LLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKqgIDAA 161
Cdd:PRK12348 80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGN--AEPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
1-231 |
1.06e-116 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 332.57 E-value: 1.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:PRK13145 2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLD-GNVVEGDLNPSSDLPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK13145 81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
1.95e-96 |
|
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.
Pssm-ID: 238232 [Multi-domain] Cd Length: 209 Bit Score: 280.02 E-value: 1.95e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 3 EDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVEShKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 83 LYQAFPTIGGIVHTHSRHATIWAQAGQ-PIPATGTTHADYFYGTIPCTRKMTEaeingeyewETGNVIVETFEKQGIdaA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340763429 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQSLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-231 |
7.24e-70 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 213.33 E-value: 7.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:PRK06557 7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLD-GNVVEGDLKPSSDTASH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTrkmTEAEINGEyewETGNVIVETfekqgIDA 160
Cdd:PRK06557 86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVG---PFALIGDE---AIGKGIVET-----LKG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763429 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQSLLDKHYLRKHGAkayYGQ 231
Cdd:PRK06557 155 GRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIP-IPQEEIDRLYDRYQNV---YGQ 221
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
4.62e-69 |
|
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440005 [Multi-domain] Cd Length: 208 Bit Score: 210.46 E-value: 4.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEIngeyewETGNVIVETFEKqgida 160
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPGTE------ELAEAIAEALGD----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340763429 161 aqMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQSLLDKHYlRKHG 224
Cdd:COG0235 149 --RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
1.15e-62 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 459862 [Multi-domain] Cd Length: 178 Bit Score: 193.15 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 7 RQVLEANLALPKHNLVTLTWGNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 87 FPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCTRKMTEAEIngeyewETGNVIVETFEKqgidaaQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGG------DRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 340763429 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
5.53e-62 |
|
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.
Pssm-ID: 214970 [Multi-domain] Cd Length: 185 Bit Score: 191.70 E-value: 5.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 9 VLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLETGEVV-ESHKKPSSDTPTHRLLYQAF 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEgGGGPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 88 PTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYG-TIPCTRKMTEAEINGEYEWETGNVIVETFEKqgidaaqMPGV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPD-------RPAV 153
|
170 180 190
....*....|....*....|....*....|
gi 340763429 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
1-201 |
5.51e-24 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 95.20 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTH 80
Cdd:PRK06833 2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLD-GKVVEGERKPSSELDMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 81 RLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHAdyFYGT-IPCTRKMTeaeingeyeWETGNVIVETFEKQGID 159
Cdd:PRK06833 81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA--VAGPnVRCAEYAT---------FGTKELAENAFEAMEDR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 340763429 160 AAqmpgVLVHSHGPFAWGKNAEDAVHnaiVLEEVAYMG-IFCR 201
Cdd:PRK06833 150 RA----VLLANHGLLAGANNLKNAFN---IAEEIEFCAeIYYQ 185
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
2-208 |
3.13e-22 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 90.47 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 2 LEDLKRQVLEANLALPKHNLVTLTWGNVSAvDRERGVLVIKPSGVDYSVMTADDMVVVSlETGEVVESH--KKPSSDTPT 79
Cdd:PRK05874 4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVD-AGGAVLHAKdgRSPSTELNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 80 HRLLYQAFPTIGGIVHTHSRHATIWAQAGQPIPATGTTHADYFYGTIPCtrkmteAEINGEYEWETGNVIVETFEKQGid 159
Cdd:PRK05874 82 HLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGRNAVRALEGRA-- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 340763429 160 aaqmpGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLP 208
Cdd:PRK05874 154 -----AALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVP 197
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
5-208 |
2.11e-14 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 69.38 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 5 LKRQVLEANLALPKHNLVTLTWGNVSAvdRERGVLVIKPSGVDYSVMTADDMVVVSLETGEvvESHKKPSSDTPTHRLLY 84
Cdd:PRK08087 6 LARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKH--EEGKLPSSEWRFHMAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 85 QAFPTIGGIVHTHSRHATIWAQAGQPIPA-------TGTTHadyfygtIPC-------TRKMTEaeingeyewetgnviv 150
Cdd:PRK08087 82 QTRPDANAVVHNHAVHCTAVSILNRPIPAihymiaaAGGNS-------IPCapyatfgTRELSE---------------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 340763429 151 etFEKQGIdaAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLP 208
Cdd:PRK08087 139 --HVALAL--KNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLKTLAITDPVP 192
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
25-183 |
7.80e-12 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 62.26 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 25 TWGNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIw 104
Cdd:PRK09220 26 TSGNMSVRLDEQHCA-ITVSGKDKGSLTAEDFLQVDIA-GNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTHSVNATV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 105 aqAGQPIPATGTTHADYfygtipctrKMTEAeINGEYEWETgNVIVETFEK-QGIDA---------AQMP---GVLVHSH 171
Cdd:PRK09220 103 --LSRVEKSDALVLEGY---------ELQKA-FAGQTTHET-AVVVPIFDNdQDIARlaarvapylDAQPlryGYLIRGH 169
|
170
....*....|..
gi 340763429 172 GPFAWGKNAEDA 183
Cdd:PRK09220 170 GLYCWGRDMAEA 181
|
|
| PRK08660 |
PRK08660 |
aldolase; |
19-192 |
1.91e-11 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 60.74 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 19 HNLVTLTWGNVSaVDRERGvLVIKPSGVDYSVMTADDMVVVSLE-TGEVvesHKKPSSDTPTHRLLYQAFPTiGGIVHTH 97
Cdd:PRK08660 15 HGLVSSHFGNIS-VRTGDG-LLITRTGSMLDEITEGDVIEVGIDdDGSV---DPLASSETPVHRAIYRRTSA-KAIVHAH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 98 SRHATIWA-QAGQPIPATGTTHadYFYGTIPctrkMTEAEINGEyewETGNVIVETFEKQGIdaaqmpgVLVHSHGPFAW 176
Cdd:PRK08660 89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIP----VVGGDIGSG---ELAENVARALSEHKG-------VVVRGHGTFAI 152
|
170
....*....|....*.
gi 340763429 177 GKNAEDAVHNAIVLEE 192
Cdd:PRK08660 153 GKTLEEAYIYTSQLEH 168
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
27-194 |
1.57e-10 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 58.73 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 27 GNVSAVDRERGVLvIKPSGVDYSVMTADDMVVVSLEtGEVVeSHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIWAQ 106
Cdd:PRK08130 28 GNISARLDDGGWL-VTPTGSCLGRLDPARLSKVDAD-GNWL-SGDKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 107 AGqpipatGTTHADyfygtipCTRKMTEAeingeYEWETGNVIVETFEKQGiD----------AAQMPGVLVHSHGPFAW 176
Cdd:PRK08130 105 LG------GLDPTN-------VLPPFTPY-----YVMRVGHVPLIPYYRPG-DpaiaealaglAARYRAVLLANHGPVVW 165
|
170
....*....|....*...
gi 340763429 177 GKNAEDAVHNAIVLEEVA 194
Cdd:PRK08130 166 GSSLEAAVNATEELEETA 183
|
|
| PRK06357 |
PRK06357 |
hypothetical protein; Provisional |
27-128 |
7.29e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 180541 [Multi-domain] Cd Length: 216 Bit Score: 48.23 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 27 GNVSavdrergVLVIKPSGVDYSVMT-------------ADDMVVVSLETGEVVESHKKPSSDTPTHRLLYQAFPTIGGI 93
Cdd:PRK06357 28 GNIS-------VRMTAEKNKEYIIMTptlmseaklcdlsPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCV 100
|
90 100 110
....*....|....*....|....*....|....*
gi 340763429 94 VHTHSRHATIWAQAGQPIPatGTTHADYFYGTIPC 128
Cdd:PRK06357 101 YHSHAKESMFWATLGLEMP--NLTEATQKLGKIPT 133
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
27-191 |
1.44e-05 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 44.98 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 27 GNVSAVDRERGVLV-IKPSGVDYSVMTADDMVVVSLEtGEVVE-SHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIW 104
Cdd:PRK06208 65 GHITARDPELPDHFwVNPLGVHFSQIKVSDLLLVDHD-GEVVEgDRPLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAW 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 105 AQAGQPI-PATGTTHAdyFYgtipctrkmteaEINGEYEWETGnVIVETFEKQGIDAAQMP--GVLVHSHGPFAWGKNAE 181
Cdd:PRK06208 144 STLGRPLdPITQDACA--FY------------EDHALFDDFTG-VVVDTSEGRRIAAALGThkAVILQNHGLLTVGPSVD 208
|
170
....*....|
gi 340763429 182 DAVHNAIVLE 191
Cdd:PRK06208 209 AAAWWFIALE 218
|
|
| PRK08333 |
PRK08333 |
aldolase; |
27-194 |
1.18e-03 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 38.65 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 27 GNVSAvdRERGVLVIKPSGVDYSVMTADDMVVVSLEtGEVVeSHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIWAQ 106
Cdd:PRK08333 26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLN-GNQL-SSVRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 107 AGQPIPATGTTHADYFYGTIPCtrkmteAEINGEYEWETGNVIVETFEkqGIDAaqmpgVLVHSHGPFAWGKNAEDAVHN 186
Cdd:PRK08333 102 LLEEELPIITPEAELYLKKIPI------LPFRPAGSVELAEQVAEAMK--EYDA-----VIMERHGIVTVGRSLREAFYK 168
|
....*...
gi 340763429 187 AIVLEEVA 194
Cdd:PRK08333 169 AELVEESA 176
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
27-111 |
1.69e-03 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 38.46 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 27 GNVSAVDRERGVLVIKPSGVDYSVMTADDMVVVSlETGEVVESHKKPSSDTPTHRLLYQAFPTIGGIVHTHSRHATIWAQ 106
Cdd:PRK07090 53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVD-EDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSM 131
|
....*
gi 340763429 107 AGQPI 111
Cdd:PRK07090 132 LEVPL 136
|
|
| PRK06486 |
PRK06486 |
aldolase; |
37-139 |
2.56e-03 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 38.15 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763429 37 GVLVIKPSGVDYSVMTADDMVVVSLEtGEVVESHKKPSsdtPT----HRLLYQAFPTIGGIVHTHSRHATIWAQ-AGQPI 111
Cdd:PRK06486 60 DLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLtEGRPL 135
|
90 100
....*....|....*....|....*...
gi 340763429 112 PATGTThADYFYGtipctRKMTEAEING 139
Cdd:PRK06486 136 TTLGQT-ALKFYG-----RTAVDEDYNG 157
|
|
| |
