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Conserved domains on  [gi|446815918|ref|WP_000893174|]
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MULTISPECIES: L-ribulose-5-phosphate 4-epimerase [Salmonella]

Protein Classification

L-ribulose-5-phosphate 4-epimerase( domain architecture ID 10793637)

L-ribulose-5-phosphate 4-epimerase catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 0e+00

L-ribulose-5-phosphate 4-epimerase; Reviewed


:

Pssm-ID: 183459  Cd Length: 231  Bit Score: 494.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 0e+00

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 494.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 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 3.13e-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: 455.06  E-value: 3.13e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918  161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 1.26e-97

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: 283.10  E-value: 1.26e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   3 EQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGnKKPSSDTATHLA 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDA-QGKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  83 LYRRYPQIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGAIPCTRLMTVEeingeyeyqTGEVIIKTFEERGldPA 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALG--FP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446815918 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKH 223
Cdd:cd00398  148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 8.63e-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: 8.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSA-VDETRklMVIKPSGVEYEVMTADDMVVVEIAsGKVVEGNKKPSSDTAT 79
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVrLDDDR--FLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  80 HLALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTV--EEIngeyeyqtGEVIIKTFEERg 157
Cdd:COG0235   79 HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGDR- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446815918 158 ldpaqiPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPdMQPELLDKHYlRKHG 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 7.42e-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: 188.52  E-value: 7.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    7 AEVLAANLALPAHGLVTFTWGNVSAVDETRkLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD-GFLITPSGVDFGELTPEDLVVVDL-DGNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   87 YPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEIngeyeyQTGEVIIKTFEERgldpaqIPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 446815918  167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 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 1.55e-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: 188.23  E-value: 1.55e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918     9 VLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGN-KKPSSDTATHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    88 PQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGA-IPCTRLMTVEEINGEYEYQTGEVIIKTFEERgldpaqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 446815918   167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 0e+00

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 494.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 5.86e-176

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 482.03  E-value: 5.86e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIAsGKVVEGNKKPSSDTATH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 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 3.13e-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: 455.06  E-value: 3.13e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918  161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 1.40e-129

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 106181  Cd Length: 231  Bit Score: 364.82  E-value: 1.40e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGNKKPSSDTATH 80
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-231 4.79e-129

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 363.35  E-value: 4.79e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   2 LEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATHL 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDM-SGKVVEGEYRPSSDTATHL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  82 ALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERglDPA 161
Cdd:PRK12348  80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNA--EPL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-231 3.00e-114

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 326.41  E-value: 3.00e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATH 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDL-DGNVVEGDLNPSSDLPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEINGEYEYQTGEVIIKTFEERGLDP 160
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446815918 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKHGANAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 1.26e-97

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: 283.10  E-value: 1.26e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   3 EQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGnKKPSSDTATHLA 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDA-QGKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  83 LYRRYPQIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGAIPCTRLMTVEeingeyeyqTGEVIIKTFEERGldPA 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALG--FP 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446815918 162 QIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPDMQPELLDKHYLRKH 223
Cdd:cd00398  148 NSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 8.63e-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: 8.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSA-VDETRklMVIKPSGVEYEVMTADDMVVVEIAsGKVVEGNKKPSSDTAT 79
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVrLDDDR--FLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  80 HLALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTV--EEIngeyeyqtGEVIIKTFEERg 157
Cdd:COG0235   79 HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGDR- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446815918 158 ldpaqiPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPdMQPELLDKHYlRKHG 224
Cdd:COG0235  150 ------PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-231 4.68e-70

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 213.72  E-value: 4.68e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATH 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDL-DGNVVEGDLKPSSDTASH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCT--RLMTVEEIngeyeyqtGEVIIKTfeergL 158
Cdd:PRK06557  86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGpfALIGDEAI--------GKGIVET-----L 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446815918 159 DPAQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPdMQPELLDKHYLRKHGAnayYGQ 231
Cdd:PRK06557 153 KGGRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIP-IPQEEIDRLYDRYQNV---YGQ 221
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 7.42e-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: 188.52  E-value: 7.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    7 AEVLAANLALPAHGLVTFTWGNVSAVDETRkLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGD-GFLITPSGVDFGELTPEDLVVVDL-DGNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   87 YPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTVEEIngeyeyQTGEVIIKTFEERgldpaqIPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 446815918  167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 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 1.55e-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: 188.23  E-value: 1.55e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918     9 VLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIASGKVVEGN-KKPSSDTATHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918    88 PQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGA-IPCTRLMTVEEINGEYEYQTGEVIIKTFEERgldpaqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGGeIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 446815918   167 LVHSHGPFAWGKNAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-194 2.58e-24

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 95.97  E-value: 2.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSAVDETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGNKKPSSDTATH 80
Cdd:PRK06833   2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDL-DGKVVEGERKPSSELDMH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  81 LALYRRYPQIGGIVHTHSRHATIWSQAGLDLPAwgTTHADYFYGA-IPCTRLMTveeingeyeYQTGEVIIKTFEerGLD 159
Cdd:PRK06833  81 LIFYRNREDINAIVHTHSPYATTLACLGWELPA--VHYLIAVAGPnVRCAEYAT---------FGTKELAENAFE--AME 147

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446815918 160 PAQipAVLVHSHGPFAWGKNAADAVHNAVVLEECA 194
Cdd:PRK06833 148 DRR--AVLLANHGLLAGANNLKNAFNIAEEIEFCA 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 9-224 1.28e-18

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 80.84  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   9 VLAANLALPAHGLVTFTWGNVSAVDETRKLmVIKPSGVEYEVMTADDMVVVEiASGKVVEG--NKKPSSDTATHLALYRR 86
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISARRSDGNV-VITPSSVDYAEMLLHDLVLVD-AGGAVLHAkdGRSPSTELNLHLACYRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  87 YPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTrlmtveEINGEYEYQTGEVIIKTFEERGldpaqipAV 166
Cdd:PRK05874  89 FDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT------EYAASGTPEVGRNAVRALEGRA-------AA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446815918 167 LVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPdmQPELLDKHYLRKHG 224
Cdd:PRK05874 156 LIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVP--IPEDVCRNFTGVYG 211
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-105 2.28e-15

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 71.89  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   1 MLEQLKAEVLAANLALPAHGLVTFTWGNVSA-VDETRKLmvIKPSGVEYEVMTADDMVVVEIAsGKVVEGNKKPSSDTAT 79
Cdd:PRK09220   2 TLEELLQQLIAAGRWIGARGWVPATSGNMSVrLDEQHCA--ITVSGKDKGSLTAEDFLQVDIA-GNAVPSGRKPSAETLL 78

                         90       100
                 ....*....|....*....|....*.
gi 446815918  80 HLALYRRYPQIGGIVHTHSRHATIWS 105
Cdd:PRK09220  79 HTQLYRLFPEIGAVLHTHSVNATVLS 104
PRK08130 PRK08130
putative aldolase; Validated
 20-219 2.72e-14

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 69.13  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  20 GLVTFTWGNVSA-VDETRKLmvIKPSGVEYEVMTADDMVVVEiASGKVVEGnKKPSSDTATHLALYRRYPQIGGIVHTHS 98
Cdd:PRK08130  21 GYTVGSAGNISArLDDGGWL--VTPTGSCLGRLDPARLSKVD-ADGNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  99 RHATIWS-QAGLD----LPAWgtthADYFY---GAIPCTRlmtveeingeYeYQTGEVIIKTfEERGLDPaQIPAVLVHS 170
Cdd:PRK08130  97 THLTALScLGGLDptnvLPPF----TPYYVmrvGHVPLIP----------Y-YRPGDPAIAE-ALAGLAA-RYRAVLLAN 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446815918 171 HGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQ-LPDMQPELLDKHY 219
Cdd:PRK08130 160 HGPVVWGSSLEAAVNATEELEETAKLILLLGGRPPRyLTDEEIAELRSTF 209
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
3-128 3.07e-13

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 66.30  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918   3 EQLKAEVLAANLALPAHGLVTFTWGNVSAvdETRKLMVIKPSGVEYEVMTADDMVVVEiASGKVVEGnKKPSSDTATHLA 82
Cdd:PRK08087   4 NKLARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVD-GNGKHEEG-KLPSSEWRFHMA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446815918  83 LYRRYPQIGGIVHTHSRHATIWSQAGLDLPAW-------GTTHadyfygaIPC 128
Cdd:PRK08087  80 AYQTRPDANAVVHNHAVHCTAVSILNRPIPAIhymiaaaGGNS-------IPC 125
PRK08660 PRK08660
aldolase;
16-203 3.56e-11

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 59.97  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  16 LPAHGLVTFTWGNVSAVDETRklMVIKPSGVEYEVMTADDMVVVEIASGKVVEgnKKPSSDTATHLALYRRYPQiGGIVH 95
Cdd:PRK08660  12 LFAHGLVSSHFGNISVRTGDG--LLITRTGSMLDEITEGDVIEVGIDDDGSVD--PLASSETPVHRAIYRRTSA-KAIVH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  96 THSRHATIWS-QAGLDLPAWGTTHadYFYGAIPctrlMTVEEINGEyeyQTGEVIIKTFEERGldpaqipAVLVHSHGPF 174
Cdd:PRK08660  87 AHPPYAVALSlLEDEIVPLDSEGL--YFLGTIP----VVGGDIGSG---ELAENVARALSEHK-------GVVVRGHGTF 150

                        170       180
                 ....*....|....*....|....*....
gi 446815918 175 AWGKNAADAVHNAVVLEECAYMGLFSRQL 203
Cdd:PRK08660 151 AIGKTLEEAYIYTSQLEHSCKVLYLVRTA 179
PRK06357 PRK06357
hypothetical protein; Provisional
 27-172 6.82e-08

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 51.31  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  27 GNVSavdetrkLMVIKPSGVEYEVMT-------------ADDMVVVEIASGKVVEGNKKPSSDTATHLALYRRYPQIGGI 93
Cdd:PRK06357  28 GNIS-------VRMTAEKNKEYIIMTptlmseaklcdlsPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  94 VHTHSRHATIWSQAGLDLPawGTTHADYFYGAIPCTRL--MTVEEIngeyeyqtGEVIIKTFEERGlDPAQIPAVLVHSH 171
Cdd:PRK06357 101 YHSHAKESMFWATLGLEMP--NLTEATQKLGKIPTLPFapATSPEL--------AEIVRKHLIELG-DKAVPSAFLLNSH 169


                 .
gi 446815918 172 G 172
Cdd:PRK06357 170 G 170
PRK08333 PRK08333
aldolase;
18-194 2.68e-05

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 43.27  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  18 AH--GLVTFTWGNVSAvdETRKLMVIKPSGVEYEVMTADDMVVVEIaSGKVVEGnKKPSSDTATHLALYRRYPQIGGIVH 95
Cdd:PRK08333  15 AHerGLTAAFGGNLSI--RVGNLVFIKATGSVMDELTREQVAVIDL-NGNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  96 THSRHATIWSQA-GLDLPAWgTTHADYFYGAIPCTRLMTVEEIngEYEYQTGEVIiktfeeRGLDpaqipAVLVHSHGPF 174
Cdd:PRK08333  91 LHPPYSIVASTLlEEELPII-TPEAELYLKKIPILPFRPAGSV--ELAEQVAEAM------KEYD-----AVIMERHGIV 156

                        170       180
                 ....*....|....*....|
gi 446815918 175 AWGKNAADAVHNAVVLEECA 194
Cdd:PRK08333 157 TVGRSLREAFYKAELVEESA 176
PRK06486 PRK06486
aldolase;
10-139 3.27e-05

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 43.93  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  10 LAANLALPA-HGLVTFTWGNVSAVDETRK-LMVIKPSGVEYEVMTADDMVVVEiASGKVVEGNKKPSSdTA--THLALYR 85
Cdd:PRK06486  31 LAACFRAAArHGLEEGICNHFSAVLPGHDdLFLVNPYGYAFSEITASDLLICD-FDGNVLAGRGEPEA-TAffIHARIHR 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446815918  86 RYPQIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGaipctRLMTVEEING 139
Cdd:PRK06486 109 AIPRAKAAFHTHMPYATALSLTEGRPLTTLGQTALKFYG-----RTAVDEDYNG 157
PRK06208 PRK06208
class II aldolase/adducin family protein;
43-111 8.49e-04

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 39.59  E-value: 8.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446815918  43 PSGVEYEVMTADDMVVVEiASGKVVEGNKKPS-SDTATHLALYRRYPQIGGIVHTHSRHATIWSQAGLDL 111
Cdd:PRK06208  82 PLGVHFSQIKVSDLLLVD-HDGEVVEGDRPLNrAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPL 150
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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