|
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: 503.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 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 |
8.21e-173 |
|
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: 474.32 E-value: 8.21e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
3.12e-99 |
|
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: 287.34 E-value: 3.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 3 EDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGtKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 83 LYQAFPSIGGIVHTHSRHATIWAQAGQ-SIPATGTTHADYFYGTIPCTRKMTDaeingeyewETGNVIVETFEKQGIdaA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128055 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
8.73e-71 |
|
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: 215.08 E-value: 8.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRErGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMT--DAEIngeyewetGNVIVETFEKqgi 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEEL--------AEAIAEALGD--- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128055 159 daaqMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQTLLDKHYlRKHG 224
Cdd:COG0235 149 ----RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
2.79e-63 |
|
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: 195.16 E-value: 2.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 9 VLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEG--TKKPSSDTPTHRLLYQA 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLD-GNVVEGggGPKPSSETPLHLAIYRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 87 FPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYG-TIPCTRKMTDAEINGEYEWETGNVIVETFEKqgidaaqMPG 165
Cdd:smart01007 80 RPDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPD-------RPA 152
|
170 180 190
....*....|....*....|....*....|.
gi 16128055 166 VLVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:smart01007 153 VLLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
2.27e-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: 192.38 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 7 RQVLEANLALPKHNLVTLTWGNVSAVDRERGvFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG-FLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 87 FPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEIngeyewETGNVIVETFEKqgidaaQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGG------DRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 16128055 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
|
|
| |
|
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: 503.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 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 |
8.21e-173 |
|
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: 474.32 E-value: 8.21e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
4.11e-161 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 444.65 E-value: 4.11e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTH 80
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
1.00e-132 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 372.91 E-value: 1.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTH 80
Cdd:PRK13213 1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK13213 81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
2-231 |
2.79e-128 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 361.43 E-value: 2.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 2 LEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTHR 81
Cdd:PRK12348 1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMS-GKVVEGEYRPSSDTATHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 82 LLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKqgIDAA 161
Cdd:PRK12348 80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGN--AEPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
1-231 |
4.92e-118 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 335.65 E-value: 4.92e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:PRK13145 2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLD-GNVVEGDLNPSSDLPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDA 160
Cdd:PRK13145 81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
3.12e-99 |
|
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: 287.34 E-value: 3.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 3 EDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGtKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 83 LYQAFPSIGGIVHTHSRHATIWAQAGQ-SIPATGTTHADYFYGTIPCTRKMTDaeingeyewETGNVIVETFEKQGIdaA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128055 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
8.73e-71 |
|
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: 215.08 E-value: 8.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRErGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMT--DAEIngeyewetGNVIVETFEKqgi 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEEL--------AEAIAEALGD--- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128055 159 daaqMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQTLLDKHYlRKHG 224
Cdd:COG0235 149 ----RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-231 |
3.19e-69 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 211.40 E-value: 3.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:PRK06557 7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLD-GNVVEGDLKPSSDTASH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKmtdAEINGEyewETGNVIVETfekqgIDA 160
Cdd:PRK06557 86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPF---ALIGDE---AIGKGIVET-----LKG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128055 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPdMQQTLLDKHYLRKHGAkayYGQ 231
Cdd:PRK06557 155 GRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIP-IPQEEIDRLYDRYQNV---YGQ 221
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
2.79e-63 |
|
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: 195.16 E-value: 2.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 9 VLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEG--TKKPSSDTPTHRLLYQA 86
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLD-GNVVEGggGPKPSSETPLHLAIYRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 87 FPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYG-TIPCTRKMTDAEINGEYEWETGNVIVETFEKqgidaaqMPG 165
Cdd:smart01007 80 RPDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPD-------RPA 152
|
170 180 190
....*....|....*....|....*....|.
gi 16128055 166 VLVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:smart01007 153 VLLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
2.27e-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: 192.38 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 7 RQVLEANLALPKHNLVTLTWGNVSAVDRERGvFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDG-FLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 87 FPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEIngeyewETGNVIVETFEKqgidaaQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGG------DRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 16128055 167 LVHSHGPFAWGKNAEDAVHNAIVLEEVAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
1-201 |
4.19e-24 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 95.20 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 1 MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTPTH 80
Cdd:PRK06833 2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLD-GKVVEGERKPSSELDMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 81 RLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHAdyFYGT-IPCTRKMTdaeingeyeWETGNVIVETFEKQGID 159
Cdd:PRK06833 81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA--VAGPnVRCAEYAT---------FGTKELAENAFEAMEDR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128055 160 AAqmpgVLVHSHGPFAWGKNAEDAVHnaiVLEEVAYMG-IFCR 201
Cdd:PRK06833 150 RA----VLLANHGLLAGANNLKNAFN---IAEEIEFCAeIYYQ 185
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
2-208 |
4.10e-21 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 87.78 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 2 LEDLKRQVLEANLALPKHNLVTLTWGNVSAvDRERGVFVIKPSGVDYSVMTADDMVVVSiETGEVVEGT--KKPSSDTPT 79
Cdd:PRK05874 4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVD-AGGAVLHAKdgRSPSTELNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 80 HRLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCtrkmtdAEINGEYEWETGNVIVETFEKQGid 159
Cdd:PRK05874 82 HLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGRNAVRALEGRA-- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128055 160 aaqmpGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLP 208
Cdd:PRK05874 154 -----AALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVP 197
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
5-208 |
1.37e-13 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 67.07 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 5 LKRQVLEANLALPKHNLVTLTWGNVSAvdRERGVFVIKPSGVDYSVMTADDMVVVSiETGEVVEGtKKPSSDTPTHRLLY 84
Cdd:PRK08087 6 LARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVD-GNGKHEEG-KLPSSEWRFHMAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 85 QAFPSIGGIVHTHSRHATIWAQAGQSIPA-------TGTTHadyfygtIPC-------TRKMTDaeingeyewetgnviv 150
Cdd:PRK08087 82 QTRPDANAVVHNHAVHCTAVSILNRPIPAihymiaaAGGNS-------IPCapyatfgTRELSE---------------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128055 151 etFEKQGIdaAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLP 208
Cdd:PRK08087 139 --HVALAL--KNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLKTLAITDPVP 192
|
|
| PRK08660 |
PRK08660 |
aldolase; |
19-192 |
2.19e-12 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 63.44 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 19 HNLVTLTWGNVSaVDRERGvFVIKPSGVDYSVMTADDMVVVSIE-TGEVvegTKKPSSDTPTHRLLYQAfPSIGGIVHTH 97
Cdd:PRK08660 15 HGLVSSHFGNIS-VRTGDG-LLITRTGSMLDEITEGDVIEVGIDdDGSV---DPLASSETPVHRAIYRR-TSAKAIVHAH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 98 SRHATIWA-QAGQSIPATGTTHadYFYGTIPctrkMTDAEINGEyewETGNVIVETFEKQGIdaaqmpgVLVHSHGPFAW 176
Cdd:PRK08660 89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIP----VVGGDIGSG---ELAENVARALSEHKG-------VVVRGHGTFAI 152
|
170
....*....|....*.
gi 16128055 177 GKNAEDAVHNAIVLEE 192
Cdd:PRK08660 153 GKTLEEAYIYTSQLEH 168
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
25-183 |
1.60e-11 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 61.49 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 25 TWGNVSA-VDRERgvFVIKPSGVDYSVMTADDMVVVSIETGEVVEGtKKPSSDTPTHRLLYQAFPSIGGIVHTHSRHATI 103
Cdd:PRK09220 26 TSGNMSVrLDEQH--CAITVSGKDKGSLTAEDFLQVDIAGNAVPSG-RKPSAETLLHTQLYRLFPEIGAVLHTHSVNATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 104 WAQAGQSipaTGTTHADYfygtipctrKMTDAeINGEYEWETgNVIVETFEK-QGIDA---------AQMP---GVLVHS 170
Cdd:PRK09220 103 LSRVEKS---DALVLEGY---------ELQKA-FAGQTTHET-AVVVPIFDNdQDIARlaarvapylDAQPlryGYLIRG 168
|
170
....*....|...
gi 16128055 171 HGPFAWGKNAEDA 183
Cdd:PRK09220 169 HGLYCWGRDMAEA 181
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
27-219 |
2.58e-11 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 61.04 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 27 GNVSAvdR-ERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGtKKPSSDTPTHRLLYQAFPSIGGIVHTHSRHATIWA 105
Cdd:PRK08130 28 GNISA--RlDDGGWLVTPTGSCLGRLDPARLSKVDAD-GNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 106 QAGqsipatGTTHAD-------YFY---GTIPCTRKMT--DAEINGEyewetgnvIVETfekqgidAAQMPGVLVHSHGP 173
Cdd:PRK08130 104 CLG------GLDPTNvlppftpYYVmrvGHVPLIPYYRpgDPAIAEA--------LAGL-------AARYRAVLLANHGP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128055 174 FAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQ-LPDMQQTLLDKHY 219
Cdd:PRK08130 163 VVWGSSLEAAVNATEELEETAKLILLLGGRPPRyLTDEEIAELRSTF 209
|
|
| PRK06357 |
PRK06357 |
hypothetical protein; Provisional |
27-128 |
2.91e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 180541 [Multi-domain] Cd Length: 216 Bit Score: 52.47 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 27 GNVS---AVDRERGVFVIKP---SGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTHRLLYQAFPSIGGIVHTHSRH 100
Cdd:PRK06357 28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107
|
90 100
....*....|....*....|....*...
gi 16128055 101 ATIWAQAGQSIPatGTTHADYFYGTIPC 128
Cdd:PRK06357 108 SMFWATLGLEMP--NLTEATQKLGKIPT 133
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
27-191 |
3.85e-06 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 46.52 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 27 GNVSAVDRER-GVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGtKKP--SSDTPTHRLLYQAFPSIGGIVHTHSRHATI 103
Cdd:PRK06208 65 GHITARDPELpDHFWVNPLGVHFSQIKVSDLLLVDHD-GEVVEG-DRPlnRAAFAIHSAIHEARPDVVAAAHTHSTYGKA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 104 WAQAGQSI-PATGTTHAdyFYGtipctrkmtDAEINGEYeweTGnVIVETFEKQGIDAAQMP--GVLVHSHGPFAWGKNA 180
Cdd:PRK06208 143 WSTLGRPLdPITQDACA--FYE---------DHALFDDF---TG-VVVDTSEGRRIAAALGThkAVILQNHGLLTVGPSV 207
|
170
....*....|.
gi 16128055 181 EDAVHNAIVLE 191
Cdd:PRK06208 208 DAAAWWFIALE 218
|
|
| PRK06486 |
PRK06486 |
aldolase; |
37-139 |
3.42e-05 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 43.55 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 37 GVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSsdtPT----HRLLYQAFPSIGGIVHTHSRHATIWAQ-AGQSI 111
Cdd:PRK06486 60 DLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLtEGRPL 135
|
90 100
....*....|....*....|....*...
gi 16128055 112 PATGTThADYFYGtipctRKMTDAEING 139
Cdd:PRK06486 136 TTLGQT-ALKFYG-----RTAVDEDYNG 157
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
27-102 |
1.88e-04 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 41.55 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128055 27 GNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSiETGEVVEGTKKPSSDTPTHRLLYQAFPSIGGIVHTHSRHAT 102
Cdd:PRK07090 53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVD-EDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVA 127
|
|
| PRK06661 |
PRK06661 |
hypothetical protein; Provisional |
4-98 |
3.75e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168637 Cd Length: 231 Bit Score: 40.59 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 4 DLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKKPSSDTP--THR 81
Cdd:PRK06661 2 DIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLD-GQILEGEEYQYNKTGyfIHG 80
|
90
....*....|....*..
gi 16128055 82 LLYQAFPSIGGIVHTHS 98
Cdd:PRK06661 81 SIYKTRPDISAIFHYHT 97
|
|
| PRK08333 |
PRK08333 |
aldolase; |
27-194 |
2.35e-03 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 37.88 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 27 GNVSAvdRERGVFVIKPSGVDYSVMTADDMVVVSIEtGEVVEGTKkPSSDTPTHRLLYQAFPSIGGIVHTHSRHATIWAQ 106
Cdd:PRK08333 26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLN-GNQLSSVR-PSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128055 107 AGQSIPATGTTHADYFYGTIPCtrkmtdAEINGEYEWETGNVIVETFEkqGIDAaqmpgVLVHSHGPFAWGKNAEDAVHN 186
Cdd:PRK08333 102 LLEEELPIITPEAELYLKKIPI------LPFRPAGSVELAEQVAEAMK--EYDA-----VIMERHGIVTVGRSLREAFYK 168
|
....*...
gi 16128055 187 AIVLEEVA 194
Cdd:PRK08333 169 AELVEESA 176
|
|
| |
