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Conserved domains on  [gi|749035358|ref|WP_040082189|]
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MULTISPECIES: L-ribulose-5-phosphate 4-epimerase [Bacillus]

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;
1-229 8.34e-166

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


:

Pssm-ID: 236181  Cd Length: 231  Bit Score: 456.22  E-value: 8.34e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHN--YE 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGidPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358 159 QVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQS 229
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-229 8.34e-166

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 456.22  E-value: 8.34e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHN--YE 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGidPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358 159 QVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQS 229
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-228 1.44e-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: 1.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLE-GEVVEGSLKPSSDTPTH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   80 VYLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQH--NY 157
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRgiDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358  158 EQVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-221 3.14e-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: 3.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREkERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREM--YDEEIiheyelntGKVIAETFQQHnye 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAgpGTEEL--------AEAIAEALGDR--- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749035358 159 qvPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKdVTPINTVLHEKHfYRKHG 221
Cdd:COG0235  150 --PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLVLSDEEIDKL-ARKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-220 4.67e-69

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: 210.68  E-value: 4.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   3 ETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSlKPSSDTPTHVYL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK-KPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  83 YKAFPNIGGIVHTHSQWATSWAQSG-RDIPPLGTTHADYFDSAIPCTREMYDEEiiHEYELNTgkVIAETFQQHnyeqvP 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPET--GEDEIGT--QRALGFPNS-----K 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 749035358 162 GVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKH 220
Cdd:cd00398  151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-195 1.60e-63

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


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 195.46  E-value: 1.60e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    7 KEVLAANLKLQEHQLVTFTWGNVSGIDrEKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVYLYKAF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   87 PNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCtremydeeiIHEYELNT---GKVIAETFQQHNyeqvPGV 163
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPI---------IPYYTPGTeelGERIAEALGGDR----KAV 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 749035358  164 LVNNHGPFCWGTDALNAIHNAVVLETVAEMAY 195
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-195 1.05e-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: 1.05e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358     9 VLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSL--KPSSDTPTHVYLYKAF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    87 PNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYF-DSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHnyeqvPGVLV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFlGGEIPYAPYAGPGTELAEEGAELAEALAEALPDR-----PAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 749035358   166 NNHGPFCWGTDALNAIHNAVVLETVAEMAY 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-229 8.34e-166

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 456.22  E-value: 8.34e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHN--YE 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGidPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358 159 QVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQS 229
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-228 1.44e-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: 1.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLE-GEVVEGSLKPSSDTPTH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   80 VYLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQH--NY 157
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRgiDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358  158 EQVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-228 1.77e-132

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 372.21  E-value: 1.77e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   2 LETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVY 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  82 LYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHNYEQVP 161
Cdd:PRK12348  81 LYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNAEPLHTP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749035358 162 GVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:PRK12348 161 GIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-228 9.54e-120

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 339.87  E-value: 9.54e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLE-GEVVEGSLKPSSDTPTH 79
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIAsGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  80 VYLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQH--NY 157
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERgiSP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358 158 EQVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-228 1.02e-107

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 309.46  E-value: 1.02e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHNYE-- 158
Cdd:PRK13145  82 ELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDpm 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 159 QVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:PRK13145 162 AVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-228 3.71e-95

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 277.76  E-value: 3.71e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLE-GEVVEGSLKPSSDTPTH 79
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLAtGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  80 VYLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHNYE- 158
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRa 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749035358 159 -QVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKHGANAYYGQ 228
Cdd:PRK13213 161 aDIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-221 3.14e-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: 3.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREkERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTREM--YDEEIiheyelntGKVIAETFQQHnye 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAgpGTEEL--------AEAIAEALGDR--- 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749035358 159 qvPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKdVTPINTVLHEKHfYRKHG 221
Cdd:COG0235  150 --PAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGG-PLVLSDEEIDKL-ARKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-220 4.67e-69

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: 210.68  E-value: 4.67e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   3 ETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSlKPSSDTPTHVYL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK-KPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  83 YKAFPNIGGIVHTHSQWATSWAQSG-RDIPPLGTTHADYFDSAIPCTREMYDEEiiHEYELNTgkVIAETFQQHnyeqvP 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPET--GEDEIGT--QRALGFPNS-----K 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 749035358 162 GVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVTPINTVLHEKHFYRKH 220
Cdd:cd00398  151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-228 1.11e-68

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 210.25  E-value: 1.11e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCT--REMYDEEIiheyelntGKVIAETFQQHNye 158
Cdd:PRK06557  87 YVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGpfALIGDEAI--------GKGIVETLKGGR-- 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 159 qVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNkDVTPINTVLHEKHFYRKHGAnayYGQ 228
Cdd:PRK06557 157 -SPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLG-EPIPIPQEEIDRLYDRYQNV---YGQ 221
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-195 1.60e-63

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


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 195.46  E-value: 1.60e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    7 KEVLAANLKLQEHQLVTFTWGNVSGIDrEKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVYLYKAF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   87 PNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCtremydeeiIHEYELNT---GKVIAETFQQHNyeqvPGV 163
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPI---------IPYYTPGTeelGERIAEALGGDR----KAV 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 749035358  164 LVNNHGPFCWGTDALNAIHNAVVLETVAEMAY 195
Cdd:pfam00596 147 LLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-195 1.05e-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: 1.05e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358     9 VLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSL--KPSSDTPTHVYLYKAF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358    87 PNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYF-DSAIPCTREMYDEEIIHEYELNTGKVIAETFQQHnyeqvPGVLV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFlGGEIPYAPYAGPGTELAEEGAELAEALAEALPDR-----PAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 749035358   166 NNHGPFCWGTDALNAIHNAVVLETVAEMAY 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-197 5.66e-26

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 100.21  E-value: 5.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   1 MLETLKKEVLAANLKLQEHQLVTFTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHV 80
Cdd:PRK06833   2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  81 YLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLGTTHAdYFDSAIPCTremydeeiihEYELNTGKVIAE-TFQQhnYEQ 159
Cdd:PRK06833  82 IFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA-VAGPNVRCA----------EYATFGTKELAEnAFEA--MED 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 749035358 160 VPGVLVNNHGPFCWGTDALNAIHNAVVLETVAEMAYHS 197
Cdd:PRK06833 149 RRAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQT 186
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 22-188 4.02e-24

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 94.64  E-value: 4.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   22 VTFTWGNVSgIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVYLYKAFpNIGGIVHTHSQWAT 101
Cdd:TIGR03328  14 VPGTGGNLS-ARLDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GAGAVLHTHSVEAT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  102 ----SWAQSGR-DIPPL--------GTTHADYFDsaIPctremydeeIIHeyelNTG--KVIAETFQQH--NYEQVPGVL 164
Cdd:TIGR03328  92 vlsrLYPSNGGfELEGYemlkglpgITTHEDTLV--VP---------IIE----NTQdiARLADSVAPAlnAYPDVPGVL 156

                         170       180
                  ....*....|....*....|....
gi 749035358  165 VNNHGPFCWGTDALNAIHNAVVLE 188
Cdd:TIGR03328 157 IRGHGLYAWGRDWEEAKRHLEALE 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 9-207 4.56e-18

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 79.30  E-value: 4.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   9 VLAANLKLQEHQLVTFTWGNVSGiDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGS--LKPSSDTPTHVYLYKAF 86
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKdgRSPSTELNLHLACYRAF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  87 PNIGGIVHTHSQWATSWAQSGRDIPPLGTTHADYFDSAIPCTRemYDEEIIHEYELNTGKVIaetfqqhnyEQVPGVLVN 166
Cdd:PRK05874  90 DDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCTE--YAASGTPEVGRNAVRAL---------EGRAAALIA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 749035358 167 NHGPFCWGTDALNAIHNAVVLETVAEMAYHSIMLNKDVtPI 207
Cdd:PRK05874 159 NHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPV-PI 198
PRK08130 PRK08130
putative aldolase; Validated
 27-191 1.40e-12

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 64.51  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  27 GNVSgIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSlKPSSDTPTHVYLYKAFPNIGGIVHTHSQWATSWA-Q 105
Cdd:PRK08130  28 GNIS-ARLDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALScL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 106 SGRD----IPPLgtthADYF---DSAIPCTRemY----DEEIiheyelntGKVIAETFQQHNyeqvpGVLVNNHGPFCWG 174
Cdd:PRK08130 106 GGLDptnvLPPF----TPYYvmrVGHVPLIP--YyrpgDPAI--------AEALAGLAARYR-----AVLLANHGPVVWG 166

                        170
                 ....*....|....*..
gi 749035358 175 TDALNAIHNAVVLETVA 191
Cdd:PRK08130 167 SSLEAAVNATEELEETA 183
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
3-127 1.95e-11

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 61.29  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   3 ETLKKEVLAANLKLQEHQLVTFTWGNVSGidREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLkPSSDTPTHVYL 82
Cdd:PRK08087   4 NKLARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKL-PSSEWRFHMAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 749035358  83 YKAFPNIGGIVHTHSQWATSWAQSGRDIPPL-------GTTHadyfdsaIPC 127
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIhymiaaaGGNS-------IPC 125
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
25-176 2.53e-11

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 60.72  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  25 TWGNVSgIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVYLYKAFPNIGGIVHTHSQWAT--S 102
Cdd:PRK09220  26 TSGNMS-VRLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTHSVNATvlS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 103 WAQSGRDIPPLG----------TTHADYFDSAIPCTremyDEEIIHeyelnTGKVIAETFQQHNYeqVPGVLVNNHGPFC 172
Cdd:PRK09220 105 RVEKSDALVLEGyelqkafagqTTHETAVVVPIFDN----DQDIAR-----LAARVAPYLDAQPL--RYGYLIRGHGLYC 173


                 ....
gi 749035358 173 WGTD 176
Cdd:PRK09220 174 WGRD 177
PRK06208 PRK06208
class II aldolase/adducin family protein;
43-169 1.76e-09

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 56.54  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  43 PSGVEYSDLTADDLVVLNLEGEVVEGslkpssDTPT-------HVYLYKAFPNIGGIVHTHSQWATSWAQSGRDIPPLgt 115
Cdd:PRK06208  82 PLGVHFSQIKVSDLLLVDHDGEVVEG------DRPLnraafaiHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPI-- 153

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749035358 116 TH---ADYFDSAIpctremYDEEIIHEYELNTGKVIAETFQQHNyeqvpGVLVNNHG 169
Cdd:PRK06208 154 TQdacAFYEDHAL------FDDFTGVVVDTSEGRRIAAALGTHK-----AVILQNHG 199
PRK06357 PRK06357
hypothetical protein; Provisional
 27-202 3.76e-09

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 54.78  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  27 GNVS---GIDREKERIVIKP---SGVEYSDLTADDLVVLNLE-GEVVEGSLKPSSDTPTHVYLYKAFPNIGGIVHTHSQW 99
Cdd:PRK06357  28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNtGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 100 ATSWAQSGRDIPPLgtTHAdyfdsaipcTREMYDEEIIhEYELNTGKVIAETFQQHNYE----QVPGV-LVNNHGPFCWG 174
Cdd:PRK06357 108 SMFWATLGLEMPNL--TEA---------TQKLGKIPTL-PFAPATSPELAEIVRKHLIElgdkAVPSAfLLNSHGIVITD 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 749035358 175 TDalnaIHNAV-VLETV---AEMAYHSIMLNK 202
Cdd:PRK06357 176 TS----LHKAYdILETIewnAYIAYQATVFDK 203
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
44-180 4.75e-09

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 54.29  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  44 SGVEYSDLTADDLVVLNLEGEVVEG-SLKPSSDTPTHVYLYKAfPNIGGIVHTHSQWATSwaqsgrdIPPLgtthadYFD 122
Cdd:PRK06754  47 SGKDKRKTTPEDFLLVDHDGKPVEEtELKPSAETLLHTHIYNN-TNAGCVLHVHTVDNNV-------ISEL------YGD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749035358 123 -SAIPCT-REM-----YDEE-------IIHEY-ELNTgkvIAETFQQHNYEQVPGVLVNNHGPFCWGTDALNA 180
Cdd:PRK06754 113 dGAVTFQgQEIikalgIWEEnaeihipIIENHaDIPT---LAEEFAKHIQGDSGAVLIRNHGITVWGRDAFEA 182
PRK08333 PRK08333
aldolase;
27-195 3.25e-08

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.75  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  27 GNVSgiDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEgSLKPSSDTPTHVYLYKAFPNIGGIVHTHSQWATSWAQS 106
Cdd:PRK08333  26 GNLS--IRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLS-SVRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 107 GRDIPPLGTTHADYFDSAIPCT--REMYDEEIiheyelntGKVIAETFQQHNyeqvpGVLVNNHGPFCWGTDALNAIHNA 184
Cdd:PRK08333 103 LEEELPIITPEAELYLKKIPILpfRPAGSVEL--------AEQVAEAMKEYD-----AVIMERHGIVTVGRSLREAFYKA 169

                        170
                 ....*....|.
gi 749035358 185 VVLETVAEMAY 195
Cdd:PRK08333 170 ELVEESAKLWY 180
PRK08660 PRK08660
aldolase;
15-202 1.22e-07

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 49.96  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  15 KLQEHQLVTFTWGNVSgiDREKERIVIKPSGVEYSDLTADDLVVLNLEGevvEGSLKP--SSDTPTHVYLYKAFPNiGGI 92
Cdd:PRK08660  11 KLFAHGLVSSHFGNIS--VRTGDGLLITRTGSMLDEITEGDVIEVGIDD---DGSVDPlaSSETPVHRAIYRRTSA-KAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  93 VHTHSQWATswAQS--GRDIPPLgTTHADYFDSAIPCTremydEEIIHEYELntGKVIAETFQQHNyeqvpGVLVNNHGP 170
Cdd:PRK08660  85 VHAHPPYAV--ALSllEDEIVPL-DSEGLYFLGTIPVV-----GGDIGSGEL--AENVARALSEHK-----GVVVRGHGT 149

                        170       180       190
                 ....*....|....*....|....*....|..
gi 749035358 171 FCWGTDALNAIHNAVVLETVAEMAYHSIMLNK 202
Cdd:PRK08660 150 FAIGKTLEEAYIYTSQLEHSCKVLYLVRTAKK 181
PRK06486 PRK06486
aldolase;
38-102 4.79e-06

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 46.24  E-value: 4.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749035358  38 RIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSsdtPT----HVYLYKAFPNIGGIVHTHSQWATS 102
Cdd:PRK06486  61 LFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPE---ATaffiHARIHRAIPRAKAAFHTHMPYATA 126
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 45-226 7.62e-06

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 45.78  E-value: 7.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  45 GVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTPTHVYLYKAFPNIGGIVHTHSQWATSWAQSGRdipPLGTTHAD----Y 120
Cdd:PRK07090  71 GLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSMLEV---PLVVSHMDtcplY 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358 121 FDSA-------IPctreMYDEEiiheyelntGKVIAETFQQHNyeqvpGVLVNNHGPFCWGTDALNAIHNAVVLETVAEM 193
Cdd:PRK07090 148 DDCAflkdwpgVP----VGNEE---------GEIISAALGDKR-----AILLSHHGQLVAGKSIEEACVLALLIERAARL 209

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 749035358 194 AYHSiMLNKDVTPINTVL-HEKHFY----RKHGAN-AYY 226
Cdd:PRK07090 210 QLLA-MAAGPIKPIPPELaREAHDWistpKRSAATfAYY 247
PRK06661 PRK06661
hypothetical protein; Provisional
 4-98 7.16e-05

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 42.51  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   4 TLKKEVLAA-----NLKLQEHqlvtfTWGNVSGIDREKERIVIKPSGVEYSDLTADDLVVLNLEGEVVEGSLKPSSDTP- 77
Cdd:PRK06661   2 DIKYNLAAAyrimaYLSLDDH-----TYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGy 76

                         90       100
                 ....*....|....*....|..
gi 749035358  78 -THVYLYKAFPNIGGIVHTHSQ 98
Cdd:PRK06661  77 fIHGSIYKTRPDISAIFHYHTP 98
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 34-177 8.49e-05

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 42.98  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  34 REKERIVIKPSGVEYSDLTADDLVVLNL-------------EGEVVE---------GSLKPSSDTPTHVYLYKAFpnigg 91
Cdd:COG3347   54 EEVEVLWVKGSGGDLATIEPAGFAALRLdplralrelgvlsDDEMVNllrhclfdlNAPAPSIETLLHAFLPHKH----- 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  92 IVHTHSQWATSWAQS--GRDIpplgtthadyfdsaipcTREMYDEEIIH------EYELntGKVIAETFQQHnyEQVPGV 163
Cdd:COG3347  129 VDHTHPDAVIAIANApdGEEL-----------------TREIFGDRVGWvpyvrpGFDL--ALALAEAFRAN--PGAEGV 187

                        170
                 ....*....|....
gi 749035358 164 LVNNHGPFCWGTDA 177
Cdd:COG3347  188 VLGKHGLFTWGDTA 201
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
2-192 8.54e-05

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 42.91  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358   2 LETLKKEVLAANLKLQEHQLVTFTWGNVS----GID---REKERIVIKPSGVEYSDLTADDLVVLNL------------- 61
Cdd:PRK08324  13 LDELALLVYRSRLLGADPRLVNHGGGNTSvkttETDltgEPVEVLWVKGSGGDLATITAAGFAALRLdplralkelgvls 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749035358  62 EGEVVE---------GSLKPSSDTPTHVYLYKAFpniggIVHTHSQW--ATSWAQSGRDIpplgtthadyfdsaipcTRE 130
Cdd:PRK08324  93 DDEMVAylrhclfdpNAPAPSIETLLHAFLPFKH-----VDHTHPDAiiAIANAPDGEEL-----------------TRE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749035358 131 MYDEEIIH------EYELntGKVIAETFQQHnyEQVPGVLVNNHGPFCWGTDALNAIHNAVVLETVAE 192
Cdd:PRK08324 151 IFGDRVGWvpyvrpGFDL--ALAIAEAVRAN--PGAEGVVLGKHGLFTWGDTAKEAYERTIEIITRAE 214
 
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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