|
Name |
Accession |
Description |
Interval |
E-value |
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
3.17e-180 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 492.80 E-value: 3.17e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTH 80
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
TIGR00760 |
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ... |
1-231 |
2.11e-165 |
|
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: 455.44 E-value: 2.11e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
4-223 |
5.72e-95 |
|
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: 276.55 E-value: 5.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 4 ELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGnKKPSSDTPTHLAL 83
Cdd:cd00398 2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 84 YRRYPEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRLMTSAeiageyeyqTGEVIIKTFeeRDLSPMQ 162
Cdd:cd00398 80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQ--RALGFPN 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 163 IPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKH 223
Cdd:cd00398 149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
6.58e-72 |
|
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: 217.78 E-value: 6.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDREsGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMT--SAEIAgeyeyqtgEVIIKTFEERdl 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEELA--------EAIAEALGDR-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556315303 159 spmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPvMQQELLDKHYlRKHG 224
Cdd:COG0235 150 -----PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
4.44e-61 |
|
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: 189.29 E-value: 4.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 7 AEVLAANLALPAHQLVTFTWGNVSAVDRESGMmIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTHLALYRR 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGF-LITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 87 YPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAgeyeyqTGEVIIKTFEERDlspmqiPAV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGGDR------KAV 146
|
170 180 190
....*....|....*....|....*....|
gi 556315303 167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 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 |
3.15e-60 |
|
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: 187.46 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 9 VLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGN-KKPSSDTPTHLALYRRY 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 88 PEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERdlspmqiPAV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153
|
170 180 190
....*....|....*....|....*....|
gi 556315303 167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
3.17e-180 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 492.80 E-value: 3.17e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTH 80
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK08193 |
L-ribulose-5-phosphate 4-epimerase AraD; |
1-231 |
2.52e-175 |
|
L-ribulose-5-phosphate 4-epimerase AraD;
Pssm-ID: 236181 Cd Length: 231 Bit Score: 480.49 E-value: 2.52e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 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 |
2.11e-165 |
|
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: 455.44 E-value: 2.11e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
2.99e-130 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 366.75 E-value: 2.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTH 80
Cdd:PRK13213 1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK13213 81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
2-231 |
7.41e-128 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 360.27 E-value: 7.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 2 LDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIaTGQVVEGNKKPSSDTPTHL 81
Cdd:PRK12348 1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDM-SGKVVEGEYRPSSDTATHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 82 ALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDlsPM 161
Cdd:PRK12348 80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNAE--PL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 162 QIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
1-231 |
2.46e-117 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 334.11 E-value: 2.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIaTGQVVEGNKKPSSDTPTH 80
Cdd:PRK13145 2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDL-DGNVVEGDLNPSSDLPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK13145 81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGANAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
4-223 |
5.72e-95 |
|
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: 276.55 E-value: 5.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 4 ELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGnKKPSSDTPTHLAL 83
Cdd:cd00398 2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 84 YRRYPEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRLMTSAeiageyeyqTGEVIIKTFeeRDLSPMQ 162
Cdd:cd00398 80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQ--RALGFPN 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 163 IPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKH 223
Cdd:cd00398 149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
6.58e-72 |
|
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: 217.78 E-value: 6.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDREsGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMT--SAEIAgeyeyqtgEVIIKTFEERdl 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEELA--------EAIAEALGDR-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556315303 159 spmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPvMQQELLDKHYlRKHG 224
Cdd:COG0235 150 -----PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-231 |
7.97e-69 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 210.63 E-value: 7.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIaTGQVVEGNKKPSSDTPTH 80
Cdd:PRK06557 7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDL-DGNVVEGDLKPSSDTASH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLmtsAEIAGEyeyQTGEVIIKTfeerdLSP 160
Cdd:PRK06557 86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPF---ALIGDE---AIGKGIVET-----LKG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556315303 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQElLDKHYLRKHGAnayYGQ 231
Cdd:PRK06557 155 GRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEE-IDRLYDRYQNV---YGQ 221
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
4.44e-61 |
|
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: 189.29 E-value: 4.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 7 AEVLAANLALPAHQLVTFTWGNVSAVDRESGMmIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTHLALYRR 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGF-LITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 87 YPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTSAEIAgeyeyqTGEVIIKTFEERDlspmqiPAV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGGDR------KAV 146
|
170 180 190
....*....|....*....|....*....|
gi 556315303 167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 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 |
3.15e-60 |
|
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: 187.46 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 9 VLAANLALPAHQLVTFTWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIATGQVVEGN-KKPSSDTPTHLALYRRY 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 88 PEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRLMTSAEIAGEYEYQTGEVIIKTFEERdlspmqiPAV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153
|
170 180 190
....*....|....*....|....*....|
gi 556315303 167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
25-194 |
1.24e-25 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 99.44 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 25 TWGNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSIaTGQVVEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
Cdd:PRK06833 26 TGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDL-DGKVVEGERKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 105 SQAGLDLPAwgTTHADYFYGT-IPCTRLMTsaeiageyeYQTGEVIIKTFE---ERDlspmqipAVLVHSHGPFAWGKDA 180
Cdd:PRK06833 105 ACLGWELPA--VHYLIAVAGPnVRCAEYAT---------FGTKELAENAFEameDRR-------AVLLANHGLLAGANNL 166
|
170
....*....|....
gi 556315303 181 ADAVHNAVVLEECA 194
Cdd:PRK06833 167 KNAFNIAEEIEFCA 180
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
2-209 |
2.05e-19 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 83.15 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 2 LDELKAEVLAANLALPAHQLVTFTWGNVSAvDRESGMMIIKPSGVEYDVMTAEDMVVVSiATGQVVEG--NKKPSSDTPT 79
Cdd:PRK05874 4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVD-AGGAVLHAkdGRSPSTELNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 80 HLALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCtrlmtsAEIAGEYEYQTGEVIIKTFEERdls 159
Cdd:PRK05874 82 HLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGRNAVRALEGR--- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556315303 160 pmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPV 209
Cdd:PRK05874 153 ----AAALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVPI 198
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
27-206 |
2.13e-15 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 72.21 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 27 GNVSAvdR-ESGMMIIKPSGVEYDVMTAEDMVVVSiATGQVVEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWS 105
Cdd:PRK08130 28 GNISA--RlDDGGWLVTPTGSCLGRLDPARLSKVD-ADGNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 106 -QAGLD----LPAWgtthADYFY---GTIPCTRLMT--SAEIAGEYeyqtgeviiktfeeRDLSPmQIPAVLVHSHGPFA 175
Cdd:PRK08130 104 cLGGLDptnvLPPF----TPYYVmrvGHVPLIPYYRpgDPAIAEAL--------------AGLAA-RYRAVLLANHGPVV 164
|
170 180 190
....*....|....*....|....*....|.
gi 556315303 176 WGKDAADAVHNAVVLEECAYMGLFSRQLAPQ 206
Cdd:PRK08130 165 WGSSLEAAVNATEELEETAKLILLLGGRPPR 195
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
25-213 |
1.18e-13 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 67.46 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 25 TWGNVSAvdRESGMMIIKPSGVEYDVMTaEDMVVVSIATGQVVEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
Cdd:PRK08087 26 TAGNVSV--RYQDGMLITPTGIPYEKLT-ESHIVFVDGNGKHEEG-KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 105 SQAGLDLPAW-------GTTHadyfygtIPCTRLMT--SAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHGPFA 175
Cdd:PRK08087 102 SILNRPIPAIhymiaaaGGNS-------IPCAPYATfgTRELS--------EHVALALKNRK-------ATLLQHHGLIA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 556315303 176 WGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQE 213
Cdd:PRK08087 160 CEVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDE 197
|
|
| PRK08660 |
PRK08660 |
aldolase; |
16-203 |
4.02e-13 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 65.36 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 16 LPAHQLVTFTWGNVSAvdRESGMMIIKPSGVEYDVMTAEDMVVVSI-ATGQVvegNKKPSSDTPTHLALYRRYPEiGGIV 94
Cdd:PRK08660 12 LFAHGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIdDDGSV---DPLASSETPVHRAIYRRTSA-KAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 95 HTHSRHATIWS-QAGLDLPAWGTTHadYFYGTIPCTRLMT-SAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHG 172
Cdd:PRK08660 86 HAHPPYAVALSlLEDEIVPLDSEGL--YFLGTIPVVGGDIgSGELA--------ENVARALSEHK-------GVVVRGHG 148
|
170 180 190
....*....|....*....|....*....|.
gi 556315303 173 PFAWGKDAADAVHNAVVLEECAYMGLFSRQL 203
Cdd:PRK08660 149 TFAIGKTLEEAYIYTSQLEHSCKVLYLVRTA 179
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
25-183 |
6.51e-12 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 62.26 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 25 TWGNVSAvdRES-GMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATI 103
Cdd:PRK09220 26 TSGNMSV--RLDeQHCAITVSGKDKGSLTAEDFLQVDIA-GNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTHSVNATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 104 WSqagldlpawgtthadyfygtipctRLMTSAEIAGE-YEYQTGEVIIKTFEER-----------------------DLS 159
Cdd:PRK09220 103 LS------------------------RVEKSDALVLEgYELQKAFAGQTTHETAvvvpifdndqdiarlaarvapylDAQ 158
|
170 180
....*....|....*....|....
gi 556315303 160 PMQiPAVLVHSHGPFAWGKDAADA 183
Cdd:PRK09220 159 PLR-YGYLIRGHGLYCWGRDMAEA 181
|
|
| PRK06357 |
PRK06357 |
hypothetical protein; Provisional |
27-128 |
9.38e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 180541 [Multi-domain] Cd Length: 216 Bit Score: 53.63 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 27 GNVS---AVDRESGMMIIKP---SGVEYDVMTAEDMVVVSIATGQVVEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRH 100
Cdd:PRK06357 28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107
|
90 100
....*....|....*....|....*...
gi 556315303 101 ATIWSQAGLDLPawGTTHADYFYGTIPC 128
Cdd:PRK06357 108 SMFWATLGLEMP--NLTEATQKLGKIPT 133
|
|
| PRK08333 |
PRK08333 |
aldolase; |
27-194 |
6.67e-08 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 50.98 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 27 GNVSAvdRESGMMIIKPSGVEYDVMTAEDMVVVSIaTGQVVEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQ 106
Cdd:PRK08333 26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDL-NGNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 107 A-GLDLPAWgTTHADYFYGTIPCT--RLMTSAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHGPFAWGKDAADA 183
Cdd:PRK08333 102 LlEEELPII-TPEAELYLKKIPILpfRPAGSVELA--------EQVAEAMKEYD-------AVIMERHGIVTVGRSLREA 165
|
170
....*....|.
gi 556315303 184 VHNAVVLEECA 194
Cdd:PRK08333 166 FYKAELVEESA 176
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
2-203 |
5.25e-07 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 48.51 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 2 LDELKAEvLAANLALPAhqlvtfTWGNVS-AVDRESGMMIIKPSGVEYDVMTAEDMVVVSiATGQVVEGNK-KPSSDTPT 79
Cdd:PRK06754 11 LAEIKKE-LAARDWFPA------TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVD-HDGKPVEETElKPSAETLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 80 HLALYRRyPEIGGIVHTHS-------------RHATIWSQ---AGLDLpaWG----------TTHADyfygtIPctrlmT 133
Cdd:PRK06754 83 HTHIYNN-TNAGCVLHVHTvdnnviselygddGAVTFQGQeiiKALGI--WEenaeihipiiENHAD-----IP-----T 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 134 SAEIAGeyEYQTGEViiktfeerdlspmqiPAVLVHSHGPFAWGKDAADAVHnavVLEecAYMGLFSRQL 203
Cdd:PRK06754 150 LAEEFA--KHIQGDS---------------GAVLIRNHGITVWGRDAFEAKK---HLE--AYEFLFSYHI 197
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
27-111 |
6.27e-04 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 40.00 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 27 GNVSAVDRESGMMIIKPSGVEYDVMTAEDMVVVSiATGQVVEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQ 106
Cdd:PRK07090 53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVD-EDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSM 131
|
....*
gi 556315303 107 AGLDL 111
Cdd:PRK07090 132 LEVPL 136
|
|
| PRK06486 |
PRK06486 |
aldolase; |
36-126 |
7.97e-04 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 39.70 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 36 SGMMIIKPSGVEYDVMTAEDMVVVSIAtGQVVEGNKKPSsdtPT----HLALYRRYPEIGGIVHTHSRHATIWSQAGLDL 111
Cdd:PRK06486 59 DDLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLTEGRP 134
|
90
....*....|....*
gi 556315303 112 PAWGTTHADYFYGTI 126
Cdd:PRK06486 135 LTTLGQTALKFYGRT 149
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
43-111 |
4.97e-03 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 37.28 E-value: 4.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315303 43 PSGVEYDVMTAEDMVVVSiATGQVVEGNKKPS-SDTPTHLALYRRYPEIGGIVHTHSRHATIWSQAGLDL 111
Cdd:PRK06208 82 PLGVHFSQIKVSDLLLVD-HDGEVVEGDRPLNrAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPL 150
|
|
| |
