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Conserved domains on  [gi|893129296|emb|CNJ90013|]
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L-ribulose-5-phosphate 4-epimerase [Yersinia mollaretii]

Protein Classification

L-ribulose-5-phosphate 4-epimerase( domain architecture ID 10013011)

L-ribulose-5-phosphate 4-epimerase catalyzes the formation of D-xylulose 5-phosphate from L-ribulose 5-phosphate

CATH:  3.40.225.10
EC:  5.1.3.4
Gene Ontology:  GO:0016832|GO:0008742|GO:0019569|GO:0008270
PubMed:  11732895
SCOP:  4000777

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 1.19e-179

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


:

Pssm-ID: 236181  Cd Length: 231  Bit Score: 491.27  E-value: 1.19e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:PRK08193 160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 1.19e-179

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 491.27  E-value: 1.19e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 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 1.50e-158

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: 438.11  E-value: 1.50e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGSKKPSSDTDTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296  161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 5.63e-92

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: 268.85  E-value: 5.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   3 NELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGsKKPSSDTDTHRV 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  83 LYLNFPQVGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRQMTPEEiagrYEWETGNVIVETFQERgikpe 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPET----GEDEIGTQRALGFPNS----- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 893129296 162 dvPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKH 223
Cdd:cd00398  150 --KAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 3.81e-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: 213.54  E-value: 3.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQsGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTP--EEIAGRyewetgnvIVETFQergi 158
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEELAEA--------IAEALG---- 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893129296 159 kpeDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLgDMQPQLLDKHYlRKHG 224
Cdd:COG0235  148 ---DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL-VLSDEEIDKLA-RKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 2.41e-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: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 187.37  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    7 QQVLAANLALPRHHLVTFTWGNVSAVDRQsGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTHRVLYLN 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   87 FPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIagryewETGNVIVETFQergikpEDVPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALG------GDRKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 893129296  167 LVNSHGPFAWGTSADNAVHNAVVLEELAYM 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 2.45e-58

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: 182.45  E-value: 2.45e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296     9 VLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGS-KKPSSDTDTHRVLYLNF 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    88 PQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRQMTPEEIAGRYEWETGNVIVETFqergikpEDVPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEAL-------PDRPAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 893129296   167 LVNSHGPFAWGTSADNAVHNAVVLEELAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-231 1.19e-179

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 491.27  E-value: 1.19e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLE-GNVVEGKLKPSSDTPTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK08193  80 LVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:PRK08193 160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 1.10e-169

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 466.22  E-value: 1.10e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGSKKPSSDTDTH 80
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 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 1.50e-158

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: 438.11  E-value: 1.50e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGSKKPSSDTDTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLETGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296  161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-231 1.55e-133

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 374.83  E-value: 1.55e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGSKKPSSDTDTH 80
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-231 3.71e-126

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 356.03  E-value: 3.71e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   2 LNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTHR 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMS-GKVVEGEYRPSSDTATHL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  82 VLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERgiKPE 161
Cdd:PRK12348  80 ELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNA--EPL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296 162 DVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:PRK12348 158 HTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-231 6.34e-115

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 327.95  E-value: 6.34e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLD-GNVVEGDLNPSSDLPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIAGRYEWETGNVIVETFQERGIKP 160
Cdd:PRK13145  81 VELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 893129296 161 EDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKHGKNAYYGQ 231
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-223 5.63e-92

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: 268.85  E-value: 5.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   3 NELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGsKKPSSDTDTHRV 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-GKVVEG-KKPSSETPLHLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  83 LYLNFPQVGGIVHTHSRHATIWSQAGL-DLPAWGTTHADYFYGTIPCTRQMTPEEiagrYEWETGNVIVETFQERgikpe 161
Cdd:cd00398   79 LYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTPET----GEDEIGTQRALGFPNS----- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 893129296 162 dvPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLGDMQPQLLDKHYLRKH 223
Cdd:cd00398  150 --KAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-224 3.81e-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: 213.54  E-value: 3.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQsGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGDLKPSSETPLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTP--EEIAGRyewetgnvIVETFQergi 158
Cdd:COG0235   80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEELAEA--------IAEALG---- 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893129296 159 kpeDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQLgDMQPQLLDKHYlRKHG 224
Cdd:COG0235  148 ---DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL-VLSDEEIDKLA-RKFG 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-231 8.08e-67

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 205.24  E-value: 8.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLD-GNVVEGDLKPSSDTASH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCT--RQMTPEEIagryewetGNVIVETfqergI 158
Cdd:PRK06557  86 LYVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGpfALIGDEAI--------GKGIVET-----L 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893129296 159 KPEDVPAVLVNSHGPFAWGTSADNAVHNAVVLEELAYMGIFSRqlnpQLGDMQP---QLLDKHYLRKHGKnayYGQ 231
Cdd:PRK06557 153 KGGRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIAR----QLGEPIPipqEEIDRLYDRYQNV---YGQ 221
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-196 2.41e-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: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 187.37  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    7 QQVLAANLALPRHHLVTFTWGNVSAVDRQsGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTHRVLYLN 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLD-GNVVEGGLKPSSETPLHLAIYRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   87 FPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTRQMTPEEIagryewETGNVIVETFQergikpEDVPAV 166
Cdd:pfam00596  79 RPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALG------GDRKAV 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 893129296  167 LVNSHGPFAWGTSADNAVHNAVVLEELAYM 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 2.45e-58

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: 182.45  E-value: 2.45e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296     9 VLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELETGKVVEGS-KKPSSDTDTHRVLYLNF 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296    88 PQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYG-TIPCTRQMTPEEIAGRYEWETGNVIVETFqergikpEDVPAV 166
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEAL-------PDRPAV 153

                          170       180       190
                   ....*....|....*....|....*....|
gi 893129296   167 LVNSHGPFAWGTSADNAVHNAVVLEELAYM 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEI 183
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-113 1.48e-23

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 94.05  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDTH 80
Cdd:PRK06833   2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLD-GKVVEGERKPSSELDMH 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 893129296  81 RVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPA 113
Cdd:PRK06833  81 LIFYRNREDINAIVHTHSPYATTLACLGWELPA 113
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 6-194 4.89e-21

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 87.39  E-value: 4.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   6 KQQVLAANLALPRHHLVTFTWGNVSAvDRQSGLLVIKPSGVEYDVMTLDDMVVVElETGKVVEGS--KKPSSDTDTHRVL 83
Cdd:PRK05874   8 ESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVD-AGGAVLHAKdgRSPSTELNLHLAC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  84 YLNFPQVGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGTIPCTrqmtpeEIAGRYEWETGNVIVETFQERGikpedv 163
Cdd:PRK05874  86 YRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT------EYAASGTPEVGRNAVRALEGRA------ 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 893129296 164 pAVLVNSHGPFAWGTSADNAVHNAVVLEELA 194
Cdd:PRK05874 154 -AALIANHGLVAVGPRPDQVLRVTALVERTA 183
PRK08130 PRK08130
putative aldolase; Validated
 27-225 1.92e-13

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 66.82  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  27 GNVSAVDRQSGLLvIKPSGVEYDVMTLDDMVVVELEtGKVVEGsKKPSSDTDTHRVLYLNFPQVGGIVHTHSRHATIWS- 105
Cdd:PRK08130  28 GNISARLDDGGWL-VTPTGSCLGRLDPARLSKVDAD-GNWLSG-DKPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSc 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296 106 QAGLD----LPAWgtthADYFY---GTIPCTRQMTP------EEIAGRyewetgnvivetfqergikPEDVPAVLVNSHG 172
Cdd:PRK08130 105 LGGLDptnvLPPF----TPYYVmrvGHVPLIPYYRPgdpaiaEALAGL-------------------AARYRAVLLANHG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 893129296 173 PFAWGTSADNAVHNAVVLEELAYMGIFSRQLNPQ-LGDmqPQLLDkhyLRKHGK 225
Cdd:PRK08130 162 PVVWGSSLEAAVNATEELEETAKLILLLGGRPPRyLTD--EEIAE---LRSTFG 210
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
3-128 9.65e-12

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 62.07  E-value: 9.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   3 NELKQQVLAANLALPRHHLVTFTWGNVSaVDRQSGLLvIKPSGVEYDVMTLDDMVVVElETGKVVEGsKKPSSDTDTHRV 82
Cdd:PRK08087   4 NKLARQIIDTCLEMTRLGLNQGTAGNVS-VRYQDGML-ITPTGIPYEKLTESHIVFVD-GNGKHEEG-KLPSSEWRFHMA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 893129296  83 LYLNFPQVGGIVHTHSRHATIWSQAGLDLPAW-------GTTHadyfygtIPC 128
Cdd:PRK08087  80 AYQTRPDANAVVHNHAVHCTAVSILNRPIPAIhymiaaaGGNS-------IPC 125
PRK08660 PRK08660
aldolase;
19-192 6.12e-11

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 59.20  E-value: 6.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  19 HHLVTFTWGNVSAvdRQSGLLVIKPSGVEYDVMTLDDMVVVELE-TGKVvegSKKPSSDTDTHRVLYLNFPqVGGIVHTH 97
Cdd:PRK08660  15 HGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIDdDGSV---DPLASSETPVHRAIYRRTS-AKAIVHAH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  98 SRHATIWS-QAGLDLPAWGTTHadYFYGTIPCTRQMT-PEEIAgryewetgNVIVETFQERGIkpedvpaVLVNSHGPFA 175
Cdd:PRK08660  89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIPVVGGDIgSGELA--------ENVARALSEHKG-------VVVRGHGTFA 151

                        170
                 ....*....|....*..
gi 893129296 176 WGTSADNAVHNAVVLEE 192
Cdd:PRK08660 152 IGKTLEEAYIYTSQLEH 168
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-105 6.92e-10

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 56.87  E-value: 6.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296   1 MLNELKQQVLAANLALPRHHLVTFTWGNVSAvdRQS-GLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDTDT 79
Cdd:PRK09220   2 TLEELLQQLIAAGRWIGARGWVPATSGNMSV--RLDeQHCAITVSGKDKGSLTAEDFLQVDIA-GNAVPSGRKPSAETLL 78

                         90       100
                 ....*....|....*....|....*.
gi 893129296  80 HRVLYLNFPQVGGIVHTHSRHATIWS 105
Cdd:PRK09220  79 HTQLYRLFPEIGAVLHTHSVNATVLS 104
PRK06357 PRK06357
hypothetical protein; Provisional
 27-195 8.92e-10

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 56.71  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  27 GNVSavdrqsgLLVIKPSGVEYDVMTL-------------DDMVVVELETGKVVEGSKKPSSDTDTHRVLYLNFPQVGGI 93
Cdd:PRK06357  28 GNIS-------VRMTAEKNKEYIIMTPtlmseaklcdlspYQILVVDLNTGEVIEGVGRVTREINMHEAAYVANPKIKCV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  94 VHTHSRHATIWSQAGLDLPawGTTHADYFYGTIPCT--RQMTPEEIAgryewetgNVIVETFQERGIKPEDVpAVLVNSH 171
Cdd:PRK06357 101 YHSHAKESMFWATLGLEMP--NLTEATQKLGKIPTLpfAPATSPELA--------EIVRKHLIELGDKAVPS-AFLLNSH 169

                        170       180
                 ....*....|....*....|....*
gi 893129296 172 GPFAwgtsADNAVHNAV-VLEELAY 195
Cdd:PRK06357 170 GIVI----TDTSLHKAYdILETIEW 190
PRK08333 PRK08333
aldolase;
27-194 3.11e-08

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.75  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  27 GNVSAvdRQSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEgSKKPSSDTDTHRVLYLNFPQVGGIVHTHSRHATIWSQ 106
Cdd:PRK08333  26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLN-GNQLS-SVRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVAST 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296 107 A-GLDLPAWgTTHADYFYGTIPctrqMTPEEIAGryEWETGNVIVETFqergikpEDVPAVLVNSHGPFAWGTSADNAVH 185
Cdd:PRK08333 102 LlEEELPII-TPEAELYLKKIP----ILPFRPAG--SVELAEQVAEAM-------KEYDAVIMERHGIVTVGRSLREAFY 167


                 ....*....
gi 893129296 186 NAVVLEELA 194
Cdd:PRK08333 168 KAELVEESA 176
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 27-212 2.19e-03

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 38.08  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  27 GNVSAVDRQSGLLVIKPSGVEYDVMTLDDMVVVElETGKVVEGSKKPSSDTDTHRVLYLNFPQVGGIVHTHSRHATIWSQ 106
Cdd:PRK07090  53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVD-EDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSM 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296 107 AGLDLPawgTTHADyfygtipctrqMTP--EEIAGRYEW-------ETGNVIVETFQergikpeDVPAVLVNSHGPFAWG 177
Cdd:PRK07090 132 LEVPLV---VSHMD-----------TCPlyDDCAFLKDWpgvpvgnEEGEIISAALG-------DKRAILLSHHGQLVAG 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 893129296 178 TSADNAVHNAVVLEELAYMGIFSRqlnpQLGDMQP 212
Cdd:PRK07090 191 KSIEEACVLALLIERAARLQLLAM----AAGPIKP 221
PRK06486 PRK06486
aldolase;
35-126 4.94e-03

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 37.38  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893129296  35 QSGLLVIKPSGVEYDVMTLDDMVVVELEtGKVVEGSKKPSSDT-DTHRVLYLNFPQVGGIVHTHSRHATIWSQAGLDLPA 113
Cdd:PRK06486  58 HDDLFLVNPYGYAFSEITASDLLICDFD-GNVLAGRGEPEATAfFIHARIHRAIPRAKAAFHTHMPYATALSLTEGRPLT 136

                         90
                 ....*....|...
gi 893129296 114 WGTTHADYFYGTI 126
Cdd:PRK06486 137 TLGQTALKFYGRT 149
 
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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