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Conserved domains on  [gi|836588569|ref|WP_047745813|]
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L-ribulose-5-phosphate 4-epimerase [Enterobacter roggenkampii]

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 2.26e-179

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


:

Pssm-ID: 183459  Cd Length: 231  Bit Score: 490.87  E-value: 2.26e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 2.26e-179

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 490.87  E-value: 2.26e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 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 5.36e-164

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: 451.97  E-value: 5.36e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569  161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 4-223 1.06e-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: 275.78  E-value: 1.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   4 ELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGnKKPSSDTPTHLAL 83
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  84 YRRYPEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRLMTTAeiageyeyqTGEVIIKTFeeRDLSPMQ 162
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQ--RALGFPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 163 IPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKH 223
Cdd:cd00398  149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 3.77e-72

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 218.55  E-value: 3.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKsGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSDTPTH 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMT--TAEIAgeyeyqtgEVIIKTFEERdl 158
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEELA--------EAIAEALGDR-- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 836588569 159 spmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPvMQQELLDKHYlRKHG 224
Cdd:COG0235  150 -----PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 3.82e-61

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 189.29  E-value: 3.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    7 AEVLAANLALPAHQLVTFTWGNVSAVDRKSGMmVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSDTPTHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGF-LITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   87 YPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAgeyeyqTGEVIIKTFEERDlspmqiPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGGDR------KAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 836588569  167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 1.34e-59

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: 185.92  E-value: 1.34e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569     9 VLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGN-KKPSSDTPTHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    88 PEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERdlspmqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 836588569   167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
 
Name Accession Description Interval E-value
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 2.26e-179

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 490.87  E-value: 2.26e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 3.08e-174

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 477.79  E-value: 3.08e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSDTPTH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 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 5.36e-164

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: 451.97  E-value: 5.36e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569  161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 5.16e-129

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 363.66  E-value: 5.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGNKKPSSDTPTH 80
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-231 9.02e-127

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 357.57  E-value: 9.02e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   2 LDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIaTGQVIEGNKKPSSDTPTHL 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDM-SGKVVEGEYRPSSDTATHL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  82 ALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDlsPM 161
Cdd:PRK12348  80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNAE--PL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 162 QIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-231 1.97e-116

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 331.80  E-value: 1.97e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIaTGQVIEGNKKPSSDTPTH 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDL-DGNVVEGDLNPSSDLPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERDLSP 160
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKHGVNAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 4-223 1.06e-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: 275.78  E-value: 1.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   4 ELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGnKKPSSDTPTHLAL 83
Cdd:cd00398    2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  84 YRRYPEIGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRLMTTAeiageyeyqTGEVIIKTFeeRDLSPMQ 162
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQ--RALGFPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 163 IPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQELLDKHYLRKH 223
Cdd:cd00398  149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 3.77e-72

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 218.55  E-value: 3.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKsGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSDTPTH 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMT--TAEIAgeyeyqtgEVIIKTFEERdl 158
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGpgTEELA--------EAIAEALGDR-- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 836588569 159 spmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPvMQQELLDKHYlRKHG 224
Cdd:COG0235  150 -----PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPLV-LSDEEIDKLA-RKFG 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-231 2.38e-69

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 211.79  E-value: 2.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   1 MLDELKAEVLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIaTGQVIEGNKKPSSDTPTH 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDL-DGNVVEGDLKPSSDTASH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLmttAEIAGEyeyQTGEVIIKTfeerdLSP 160
Cdd:PRK06557  86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGPF---ALIGDE---AIGKGIVET-----LKG 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 836588569 161 MQIPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQElLDKHYLRKHGVnayYGQ 231
Cdd:PRK06557 155 GRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLGEPIPIPQEE-IDRLYDRYQNV---YGQ 221
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 3.82e-61

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 189.29  E-value: 3.82e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    7 AEVLAANLALPAHQLVTFTWGNVSAVDRKSGMmVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSDTPTHLALYRR 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGF-LITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   87 YPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRLMTTAEIAgeyeyqTGEVIIKTFEERDlspmqiPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGGDR------KAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 836588569  167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEI 176
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 1.34e-59

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: 185.92  E-value: 1.34e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569     9 VLAANLALPAHQLVTFTWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGN-KKPSSDTPTHLALYRRY 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569    88 PEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRLMTTAEIAGEYEYQTGEVIIKTFEERdlspmqiPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALPDR-------PAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 836588569   167 LVHSHGPFAWGKDAADAVHNAVVLEECAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
25-194 4.58e-26

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 100.59  E-value: 4.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  25 TWGNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNIaTGQVIEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
Cdd:PRK06833  26 TGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDL-DGKVVEGERKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 105 SQAGLDLPAwgTTHADYFYGT-IPCTRLMT--TAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHGPFAWGKDAA 181
Cdd:PRK06833 105 ACLGWELPA--VHYLIAVAGPnVRCAEYATfgTKELA--------ENAFEAMEDRR-------AVLLANHGLLAGANNLK 167

                        170
                 ....*....|...
gi 836588569 182 DAVHNAVVLEECA 194
Cdd:PRK06833 168 NAFNIAEEIEFCA 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 2-209 3.06e-20

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 85.47  E-value: 3.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   2 LDELKAEVLAANLALPAHQLVTFTWGNVSAvDRKSGMMVIKPSGVEYDVMTAEDMVVVNiATGQVIEG--NKKPSSDTPT 79
Cdd:PRK05874   4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVD-AGGAVLHAkdGRSPSTELNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  80 HLALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCtrlmttAEIAGEYEYQTGEVIIKTFEERdls 159
Cdd:PRK05874  82 HLACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGRNAVRALEGR--- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 836588569 160 pmqiPAVLVHSHGPFAWGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPV 209
Cdd:PRK05874 153 ----AAALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPVPI 198
PRK08130 PRK08130
putative aldolase; Validated
 27-224 1.28e-14

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 69.90  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  27 GNVSAVDRKSGMMvIKPSGVEYDVMTAEDMVVVNiATGQVIEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWS- 105
Cdd:PRK08130  28 GNISARLDDGGWL-VTPTGSCLGRLDPARLSKVD-ADGNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSc 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 106 QAGLD----LPAWgtthADYFygtipctrLMTTAEIAGEYEYQTGEVIIKTfEERDLSPmQIPAVLVHSHGPFAWGKDAA 181
Cdd:PRK08130 105 LGGLDptnvLPPF----TPYY--------VMRVGHVPLIPYYRPGDPAIAE-ALAGLAA-RYRAVLLANHGPVVWGSSLE 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 836588569 182 DAVHNAVVLEECAYMGLFSRQLAPQlPVMQQELLDkhyLRKHG 224
Cdd:PRK08130 171 AAVNATEELEETAKLILLLGGRPPR-YLTDEEIAE---LRSTF 209
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
25-213 1.56e-13

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 67.07  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  25 TWGNVSAvdRKSGMMVIKPSGVEYDVMTaEDMVVVNIATGQVIEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIW 104
Cdd:PRK08087  26 TAGNVSV--RYQDGMLITPTGIPYEKLT-ESHIVFVDGNGKHEEG-KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 105 SQAGLDLPAW-------GTTHadyfygtIPCTRLMT--TAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHGPFA 175
Cdd:PRK08087 102 SILNRPIPAIhymiaaaGGNS-------IPCAPYATfgTRELS--------EHVALALKNRK-------ATLLQHHGLIA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 836588569 176 WGKDAADAVHNAVVLEECAYMGLFSRQLAPQLPVMQQE 213
Cdd:PRK08087 160 CEVNLEKALWLAHEVEVLAQLYLKTLAITDPVPVLSDE 197
PRK08660 PRK08660
aldolase;
16-203 1.39e-12

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 63.82  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  16 LPAHQLVTFTWGNVSAvdRKSGMMVIKPSGVEYDVMTAEDMVVVNI-ATGQVIegnKKPSSDTPTHLALYRRYPEiGGIV 94
Cdd:PRK08660  12 LFAHGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIdDDGSVD---PLASSETPVHRAIYRRTSA-KAIV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  95 HTHSRHATIWS-QAGLDLPAWGTTHadYFYGTIPctrlMTTAEIAGEyeyQTGEVIIKTFEERDlspmqipAVLVHSHGP 173
Cdd:PRK08660  86 HAHPPYAVALSlLEDEIVPLDSEGL--YFLGTIP----VVGGDIGSG---ELAENVARALSEHK-------GVVVRGHGT 149

                        170       180       190
                 ....*....|....*....|....*....|
gi 836588569 174 FAWGKDAADAVHNAVVLEECAYMGLFSRQL 203
Cdd:PRK08660 150 FAIGKTLEEAYIYTSQLEHSCKVLYLVRTA 179
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
25-183 1.20e-11

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 61.49  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  25 TWGNVSAvdRKS-GMMVIKPSGVEYDVMTAEDMVVVNIATGQVIEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATI 103
Cdd:PRK09220  26 TSGNMSV--RLDeQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSG-RKPSAETLLHTQLYRLFPEIGAVLHTHSVNATV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 104 WS----QAGLDLPAW--------GTTHADyfygTIPCTRLMTTAEIAgeyeyQTGEVIIKTFEERDLSpmqiPAVLVHSH 171
Cdd:PRK09220 103 LSrvekSDALVLEGYelqkafagQTTHET----AVVVPIFDNDQDIA-----RLAARVAPYLDAQPLR----YGYLIRGH 169

                        170
                 ....*....|..
gi 836588569 172 GPFAWGKDAADA 183
Cdd:PRK09220 170 GLYCWGRDMAEA 181
PRK06357 PRK06357
hypothetical protein; Provisional
 27-128 9.29e-09

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 53.63  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  27 GNVSavdrksgMMVIKPSGVEYDVMT-------------AEDMVVVNIATGQVIEGNKKPSSDTPTHLALYRRYPEIGGI 93
Cdd:PRK06357  28 GNIS-------VRMTAEKNKEYIIMTptlmseaklcdlsPYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCV 100

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 836588569  94 VHTHSRHATIWSQAGLDLPawGTTHADYFYGTIPC 128
Cdd:PRK06357 101 YHSHAKESMFWATLGLEMP--NLTEATQKLGKIPT 133
PRK08333 PRK08333
aldolase;
27-194 4.42e-08

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.36  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  27 GNVSAvdRKSGMMVIKPSGVEYDVMTAEDMVVVNIaTGQVIEGnKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQ 106
Cdd:PRK08333  26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDL-NGNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 107 A-GLDLPAWgTTHADYFYGTIPCT--RLMTTAEIAgeyeyqtgEVIIKTFEERDlspmqipAVLVHSHGPFAWGKDAADA 183
Cdd:PRK08333 102 LlEEELPII-TPEAELYLKKIPILpfRPAGSVELA--------EQVAEAMKEYD-------AVIMERHGIVTVGRSLREA 165

                        170
                 ....*....|.
gi 836588569 184 VHNAVVLEECA 194
Cdd:PRK08333 166 FYKAELVEESA 176
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
2-203 8.32e-07

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 48.12  E-value: 8.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569   2 LDELKAEvLAANLALPAhqlvtfTWGNVS-AVDRKSGMMVIKPSGVEYDVMTAEDMVVVNiATGQVIEGNK-KPSSDTPT 79
Cdd:PRK06754  11 LAEIKKE-LAARDWFPA------TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVD-HDGKPVEETElKPSAETLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  80 HLALYRRyPEIGGIVHTHS-------------RHATIWSQ---AGLDLpaWG----------TTHADyfygtIPctrlmT 133
Cdd:PRK06754  83 HTHIYNN-TNAGCVLHVHTvdnnviselygddGAVTFQGQeiiKALGI--WEenaeihipiiENHAD-----IP-----T 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569 134 TAEIAGeyEYQTGEViiktfeerdlspmqiPAVLVHSHGPFAWGKDAADAVHnavVLEecAYMGLFSRQL 203
Cdd:PRK06754 150 LAEEFA--KHIQGDS---------------GAVLIRNHGITVWGRDAFEAKK---HLE--AYEFLFSYHI 197
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 27-111 1.38e-04

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 41.93  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  27 GNVSAVDRKSGMMVIKPSGVEYDVMTAEDMVVVNiATGQVIEGNKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQ 106
Cdd:PRK07090  53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVD-EDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSM 131


                 ....*
gi 836588569 107 AGLDL 111
Cdd:PRK07090 132 LEVPL 136
PRK06486 PRK06486
aldolase;
36-126 6.16e-04

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 40.08  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  36 SGMMVIKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSsdtPT----HLALYRRYPEIGGIVHTHSRHATIWSQAGLDL 111
Cdd:PRK06486  59 DDLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATALSLTEGRP 134

                         90
                 ....*....|....*
gi 836588569 112 PAWGTTHADYFYGTI 126
Cdd:PRK06486 135 LTTLGQTALKFYGRT 149
PRK06208 PRK06208
class II aldolase/adducin family protein;
43-111 1.10e-03

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 39.20  E-value: 1.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  43 PSGVEYDVMTAEDMVVVNiATGQVIEGNKKPS-SDTPTHLALYRRYPEIGGIVHTHSRHATIWSQAGLDL 111
Cdd:PRK06208  82 PLGVHFSQIKVSDLLLVD-HDGEVVEGDRPLNrAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPL 150
PRK07490 PRK07490
hypothetical protein; Provisional
 41-102 3.39e-03

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 37.78  E-value: 3.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 836588569  41 IKPSGVEYDVMTAEDMVVVNIATGQVIEGnkkPSSDTPT----HLALYRRYPEIGGIVHTHSRHAT 102
Cdd:PRK07490  48 LNPKWKHFSRIRASDLLLLDADDPSTAER---PDVPDATawaiHGQIHRRLPHARCVMHVHSVYAT 110
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 41-183 4.75e-03

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 37.13  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588569  41 IKPSGVEYDVMTAEDMVVVNIAtGQVIEGNKKPSSdtPT----HLALYRRYPEIGGIVHTHSRH--ATIWSQAGLdLPAw 114
Cdd:PRK07044  54 INPYGLLFDEITASNLVKIDLD-GNVVDDSPYPVN--PAgftiHSAIHAARPDAHCVMHTHTTAgvAVSAQRDGL-LPL- 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 836588569 115 gTTHADYFYGTIpctrlmttaeiageyEYQTGEVIIKTFEER-----DLSPMqiPAVLVHSHGPFAWGKDAADA 183
Cdd:PRK07044 129 -SQHALQFYGRL---------------AYHDYEGIALDLDEGerlvaDLGDK--PAMLLRNHGLLTVGRTVAEA 184
 
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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