|
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: 500.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 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 |
9.86e-168 |
|
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: 461.22 E-value: 9.86e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
6.08e-94 |
|
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: 273.86 E-value: 6.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 3 EDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGnKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 83 LYQAFPTLGGIVHTHSRHATIWAQAGQ-SIPATGTTHADYFYGPVPCTRLMTDaeingeyewETGNVIVETFRQQGIdpA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014906 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
1.64e-70 |
|
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: 214.31 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLvIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMT--DAEIngeyewetGNVIVETFRqqgi 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEEL--------AEAIAEALG---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014906 159 dpaQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPdMQQTLLDKHYlRKHG 224
Cdd:COG0235 148 ---DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| Aldolase_II |
smart01007 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
9-196 |
2.27e-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: 195.55 E-value: 2.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 9 VLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGN-KKPSSDTPTHRLLYQAF 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 88 PTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGP-VPCTRLMTDAEINGEYEWETGNVIVETFRqqgidpaQMPGV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALP-------DRPAV 153
|
170 180 190
....*....|....*....|....*....|
gi 1994014906 167 LVHSHGPFAWGKNAEDAVHNAIVLEEIAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
4.42e-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: 459862 [Multi-domain] Cd Length: 178 Bit Score: 194.30 E-value: 4.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 7 RQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLvIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 87 FPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEIngeyewETGNVIVETFRqqgidpAQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALG------GDRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 1994014906 167 LVHSHGPFAWGKNAEDAVHNAIVLEEIAYM 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: 500.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:PRK08193 1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:PRK08193 80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 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 |
9.86e-168 |
|
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: 461.22 E-value: 9.86e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTH 80
Cdd:TIGR00760 1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:TIGR00760 81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
|
|
| sgbE |
PRK12347 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
8.96e-161 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183459 Cd Length: 231 Bit Score: 443.88 E-value: 8.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTH 80
Cdd:PRK12347 1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:PRK12347 81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
|
|
| araD |
PRK13213 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
1-231 |
5.36e-133 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 106181 Cd Length: 231 Bit Score: 373.68 E-value: 5.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTH 80
Cdd:PRK13213 1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:PRK13213 81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
|
|
| sgaE |
PRK12348 |
L-ribulose-5-phosphate 4-epimerase; Reviewed |
2-231 |
7.09e-128 |
|
L-ribulose-5-phosphate 4-epimerase; Reviewed
Pssm-ID: 183460 Cd Length: 228 Bit Score: 360.66 E-value: 7.09e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 2 LEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTHR 81
Cdd:PRK12348 1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMS-GKVVEGEYRPSSDTATHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 82 LLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQqgIDPA 161
Cdd:PRK12348 80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGN--AEPL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
|
|
| araD |
PRK13145 |
L-ribulose-5-phosphate 4-epimerase; Provisional |
1-231 |
1.64e-118 |
|
L-ribulose-5-phosphate 4-epimerase; Provisional
Pssm-ID: 183870 [Multi-domain] Cd Length: 234 Bit Score: 337.19 E-value: 1.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:PRK13145 2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLD-GNVVEGDLNPSSDLPTH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEINGEYEWETGNVIVETFRQQGIDP 160
Cdd:PRK13145 81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
|
|
| Aldolase_II |
cd00398 |
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ... |
3-223 |
6.08e-94 |
|
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: 273.86 E-value: 6.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 3 EDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGnKKPSSDTPTHRL 82
Cdd:cd00398 1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 83 LYQAFPTLGGIVHTHSRHATIWAQAGQ-SIPATGTTHADYFYGPVPCTRLMTDaeingeyewETGNVIVETFRQQGIdpA 161
Cdd:cd00398 79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALGF--P 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994014906 162 QMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPDMQQTLLDKHYLRKH 223
Cdd:cd00398 148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
|
|
| AraD |
COG0235 |
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ... |
1-224 |
1.64e-70 |
|
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: 214.31 E-value: 1.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLvIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:COG0235 2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMT--DAEIngeyewetGNVIVETFRqqgi 158
Cdd:COG0235 80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEEL--------AEAIAEALG---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014906 159 dpaQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPdMQQTLLDKHYlRKHG 224
Cdd:COG0235 148 ---DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
|
|
| PRK06557 |
PRK06557 |
L-ribulose-5-phosphate 4-epimerase; Validated |
1-231 |
1.60e-69 |
|
L-ribulose-5-phosphate 4-epimerase; Validated
Pssm-ID: 235829 [Multi-domain] Cd Length: 221 Bit Score: 212.18 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:PRK06557 7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLD-GNVVEGDLKPSSDTASH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLmtdAEINGEyewETGNVIVETfrqqgIDP 160
Cdd:PRK06557 86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPF---ALIGDE---AIGKGIVET-----LKG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 161 AQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLPdMQQTLLDKHYLRKHGAkayYGQ 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 |
2.27e-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: 195.55 E-value: 2.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 9 VLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGN-KKPSSDTPTHRLLYQAF 87
Cdd:smart01007 1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 88 PTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGP-VPCTRLMTDAEINGEYEWETGNVIVETFRqqgidpaQMPGV 166
Cdd:smart01007 81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALP-------DRPAV 153
|
170 180 190
....*....|....*....|....*....|
gi 1994014906 167 LVHSHGPFAWGKNAEDAVHNAIVLEEIAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
|
|
| Aldolase_II |
pfam00596 |
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ... |
7-196 |
4.42e-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: 459862 [Multi-domain] Cd Length: 178 Bit Score: 194.30 E-value: 4.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 7 RQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLvIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTHRLLYQA 86
Cdd:pfam00596 1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFL-ITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 87 FPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCTRLMTDAEIngeyewETGNVIVETFRqqgidpAQMPGV 166
Cdd:pfam00596 79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALG------GDRKAV 146
|
170 180 190
....*....|....*....|....*....|
gi 1994014906 167 LVHSHGPFAWGKNAEDAVHNAIVLEEIAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
|
|
| PRK06833 |
PRK06833 |
L-fuculose-phosphate aldolase; |
1-201 |
1.11e-25 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 180717 [Multi-domain] Cd Length: 214 Bit Score: 99.44 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 1 MLEDLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTPTH 80
Cdd:PRK06833 2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLD-GKVVEGERKPSSELDMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 81 RLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHAdyFYGP-VPCTRLMTdaeingeyeWETGNVIVETFRQQGID 159
Cdd:PRK06833 81 LIFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA--VAGPnVRCAEYAT---------FGTKELAENAFEAMEDR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1994014906 160 PAqmpgVLVHSHGPFAWGKNAEDAVHnaiVLEEIAYMG-IFCR 201
Cdd:PRK06833 150 RA----VLLANHGLLAGANNLKNAFN---IAEEIEFCAeIYYQ 185
|
|
| PRK05874 |
PRK05874 |
L-fuculose-phosphate aldolase; Validated |
2-208 |
1.61e-20 |
|
L-fuculose-phosphate aldolase; Validated
Pssm-ID: 102036 [Multi-domain] Cd Length: 217 Bit Score: 85.85 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 2 LEDLKRQVLEANLALPQHNLVTLTWGNVSAvDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEG--NKKPSSDTPT 79
Cdd:PRK05874 4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAG-GAVLHAkdGRSPSTELNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 80 HRLLYQAFPTLGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGPVPCtrlmtdAEINGEYEWETGNVIVETFRQQGid 159
Cdd:PRK05874 82 HLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGRNAVRALEGRA-- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1994014906 160 paqmpGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLP 208
Cdd:PRK05874 154 -----AALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVP 197
|
|
| PRK08130 |
PRK08130 |
putative aldolase; Validated |
27-219 |
2.31e-14 |
|
putative aldolase; Validated
Pssm-ID: 181241 [Multi-domain] Cd Length: 213 Bit Score: 69.13 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 27 GNVSAVDRDKGVLvIKPSGVDYGLMTADDMVVVSLDtGEVVEGnKKPSSDTPTHRLLYQAFPTLGGIVHTHSRHATIWAQ 106
Cdd:PRK08130 28 GNISARLDDGGWL-VTPTGSCLGRLDPARLSKVDAD-GNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 107 AGqsipatGTTHADyfygpvpCTRLMTDAeingeYEWETGNVIVETFRQQGiDPA----------QMPGVLVHSHGPFAW 176
Cdd:PRK08130 105 LG------GLDPTN-------VLPPFTPY-----YVMRVGHVPLIPYYRPG-DPAiaealaglaaRYRAVLLANHGPVVW 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1994014906 177 GKNAEDAVHNAIVLEEIAYMGIFCRQLAPQ-LPDMQQTLLDKHY 219
Cdd:PRK08130 166 GSSLEAAVNATEELEETAKLILLLGGRPPRyLTDEEIAELRSTF 209
|
|
| PRK08087 |
PRK08087 |
L-fuculose-phosphate aldolase; |
5-208 |
4.46e-13 |
|
L-fuculose-phosphate aldolase;
Pssm-ID: 181226 [Multi-domain] Cd Length: 215 Bit Score: 65.92 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 5 LKRQVLEANLALPQHNLVTLTWGNVSAvdRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGnKKPSSDTPTHRLLY 84
Cdd:PRK08087 6 LARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGN-GKHEEG-KLPSSEWRFHMAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 85 QAFPTLGGIVHTHSRHATIWAQAGQSIPA-------TGTTHadyfygpVPCTRLMTdaeingeyeweTGNVIVETFRQQG 157
Cdd:PRK08087 82 QTRPDANAVVHNHAVHCTAVSILNRPIPAihymiaaAGGNS-------IPCAPYAT-----------FGTRELSEHVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1994014906 158 IdpAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEIAYMGIFCRQLAPQLP 208
Cdd:PRK08087 144 L--KNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLKTLAITDPVP 192
|
|
| PRK09220 |
PRK09220 |
methylthioribulose 1-phosphate dehydratase; |
25-103 |
3.60e-12 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 236415 [Multi-domain] Cd Length: 204 Bit Score: 63.03 E-value: 3.60e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1994014906 25 TWGNVSaVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGnKKPSSDTPTHRLLYQAFPTLGGIVHTHSRHATI 103
Cdd:PRK09220 26 TSGNMS-VRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSG-RKPSAETLLHTQLYRLFPEIGAVLHTHSVNATV 102
|
|
| PRK08660 |
PRK08660 |
aldolase; |
19-192 |
1.25e-11 |
|
aldolase;
Pssm-ID: 181527 [Multi-domain] Cd Length: 181 Bit Score: 61.13 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 19 HNLVTLTWGNVSAvdRDKGVLVIKPSGVDYGLMTADDMVVVSLD-TGEVvegNKKPSSDTPTHRLLYQAFPTLGgIVHTH 97
Cdd:PRK08660 15 HGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIDdDGSV---DPLASSETPVHRAIYRRTSAKA-IVHAH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 98 SRHATIWA-QAGQSIPATGTTHadYFYGPVPctrlMTDAEINGEyewETGNVIVETFRQQGIdpaqmpgVLVHSHGPFAW 176
Cdd:PRK08660 89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIP----VVGGDIGSG---ELAENVARALSEHKG-------VVVRGHGTFAI 152
|
170
....*....|....*.
gi 1994014906 177 GKNAEDAVHNAIVLEE 192
Cdd:PRK08660 153 GKTLEEAYIYTSQLEH 168
|
|
| PRK06357 |
PRK06357 |
hypothetical protein; Provisional |
27-128 |
1.49e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 180541 [Multi-domain] Cd Length: 216 Bit Score: 53.24 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 27 GNVS---AVDRDKGVLVIKP---SGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTHRLLYQAFPTLGGIVHTHSRH 100
Cdd:PRK06357 28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107
|
90 100
....*....|....*....|....*...
gi 1994014906 101 ATIWAQAGQSIPatGTTHADYFYGPVPC 128
Cdd:PRK06357 108 SMFWATLGLEMP--NLTEATQKLGKIPT 133
|
|
| PRK06661 |
PRK06661 |
hypothetical protein; Provisional |
4-98 |
1.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168637 Cd Length: 231 Bit Score: 42.13 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 4 DLKRQVLEANLALPQHNLVTLTWGNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSSDTP--THR 81
Cdd:PRK06661 2 DIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLD-GQILEGEEYQYNKTGyfIHG 80
|
90
....*....|....*..
gi 1994014906 82 LLYQAFPTLGGIVHTHS 98
Cdd:PRK06661 81 SIYKTRPDISAIFHYHT 97
|
|
| PRK06486 |
PRK06486 |
aldolase; |
37-139 |
3.29e-04 |
|
aldolase;
Pssm-ID: 235814 Cd Length: 262 Bit Score: 40.85 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 37 GVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGNKKPSsdtPT----HRLLYQAFPTLGGIVHTHSRHATIWAQ-AGQSI 111
Cdd:PRK06486 60 DLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLtEGRPL 135
|
90 100
....*....|....*....|....*...
gi 1994014906 112 PATGTThADYFYGpvpctRLMTDAEING 139
Cdd:PRK06486 136 TTLGQT-ALKFYG-----RTAVDEDYNG 157
|
|
| mtnB |
PRK06754 |
methylthioribulose 1-phosphate dehydratase; |
25-183 |
4.08e-04 |
|
methylthioribulose 1-phosphate dehydratase;
Pssm-ID: 180679 [Multi-domain] Cd Length: 208 Bit Score: 40.03 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 25 TWGNVS-AVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTGEVVEGNKKPSSDTPTHRLLYQAfPTLGGIVHTHS----- 98
Cdd:PRK06754 27 TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEETELKPSAETLLHTHIYNN-TNAGCVLHVHTvdnnv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 99 --------RHATIWAQagQSIPATGTTHADYFYgPVP----CTRLMTDAEingeyewETGNVIvetfrqqgidPAQMPGV 166
Cdd:PRK06754 106 iselygddGAVTFQGQ--EIIKALGIWEENAEI-HIPiienHADIPTLAE-------EFAKHI----------QGDSGAV 165
|
170
....*....|....*..
gi 1994014906 167 LVHSHGPFAWGKNAEDA 183
Cdd:PRK06754 166 LIRNHGITVWGRDAFEA 182
|
|
| PRK07090 |
PRK07090 |
class II aldolase/adducin domain protein; Provisional |
27-102 |
1.86e-03 |
|
class II aldolase/adducin domain protein; Provisional
Pssm-ID: 180832 Cd Length: 260 Bit Score: 38.46 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994014906 27 GNVSAVDRDKGVLVIKPSGVDYGLMTADDMVVVSLDTgEVVEGNKKPSSDTPTHRLLYQAFPTLGGIVHTHSRHAT 102
Cdd:PRK07090 53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVDEDL-NVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVA 127
|
|
| PRK06208 |
PRK06208 |
class II aldolase/adducin family protein; |
43-109 |
2.26e-03 |
|
class II aldolase/adducin family protein;
Pssm-ID: 235743 Cd Length: 274 Bit Score: 38.43 E-value: 2.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1994014906 43 PSGVDYGLMTADDMVVVSLDtGEVVEGNKKPS-SDTPTHRLLYQAFPTLGGIVHTHSRHATIWAQAGQ 109
Cdd:PRK06208 82 PLGVHFSQIKVSDLLLVDHD-GEVVEGDRPLNrAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGR 148
|
|
| PRK08333 |
PRK08333 |
aldolase; |
27-194 |
2.42e-03 |
|
aldolase;
Pssm-ID: 181393 [Multi-domain] Cd Length: 184 Bit Score: 37.49 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 27 GNVSAvdRDKGVLVIKPSGVDYGLMTADDMVVVSLDtGEVVEGnKKPSSDTPTHRLLYQAFPTLGGIVHTHSRHATIWAQ 106
Cdd:PRK08333 26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLN-GNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994014906 107 AGQSIPATGTTHADYFYGPVPCtrlmtdAEINGEYEWETGNVIVETFRQQGidpaqmpGVLVHSHGPFAWGKNAEDAVHN 186
Cdd:PRK08333 102 LLEEELPIITPEAELYLKKIPI------LPFRPAGSVELAEQVAEAMKEYD-------AVIMERHGIVTVGRSLREAFYK 168
|
....*...
gi 1994014906 187 AIVLEEIA 194
Cdd:PRK08333 169 AELVEESA 176
|
|
| |
