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Conserved domains on  [gi|727160149|ref|WP_033632583|]
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MULTISPECIES: L-ribulose-5-phosphate 4-epimerase [Serratia]

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;
1-230 4.58e-175

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


:

Pssm-ID: 236181  Cd Length: 231  Bit Score: 479.72  E-value: 4.58e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDPQ 160
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 161 QVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-230 4.58e-175

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 479.72  E-value: 4.58e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDPQ 160
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 161 QVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-230 3.45e-145

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: 404.21  E-value: 3.45e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLE-GKVREGHRKPSSDTATH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   80 LALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDP 159
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149  160 QQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-222 2.10e-89

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: 262.30  E-value: 2.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   3 NELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGhRKPSSDTATHLAL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  83 YRAFADIGGVVHTHSRNATIWAQAGQ-PIPALGTTHADYFYGDIPCTRPMSEaeiagdyegETGKVIIETFNQAGrdPQQ 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALG--FPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149 162 VPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKH 222
Cdd:cd00398  149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-223 1.24e-73

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: 222.40  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQsGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTrpmseaeiagDYEG----ETGKVIIETFnqag 156
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVV----------PYAGpgteELAEAIAEAL---- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727160149 157 rdpQQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIaPMQPELLDKHfLRKHG 223
Cdd:COG0235  147 ---GDRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL-VLSDEEIDKL-ARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-193 1.54e-62

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: 192.76  E-value: 1.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    7 RQVLAANLSLPAYGLVTFTWGNVSAIDRQsGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHLALYRAF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   87 ADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIagdyegETGKVIIETFNQAgrdpqqVPGVL 166
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAVL 147

                         170       180
                  ....*....|....*....|....*..
gi 727160149  167 VYSHGPFAWGKDAADAVHNAVVLEEVA 193
Cdd:pfam00596 148 LRNHGLLVWGKTLEEAFYLAEELERAA 174
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 1.58e-60

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


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 188.23  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149     9 VLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREG--HRKPSSDTATHLALYRAF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGggGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    87 ADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYG-DIPCTRPMSEAEIAGDYEGETGKVIIETFnqagrdpQQVPGV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEAL-------PDRPAV 153

                          170       180       190
                   ....*....|....*....|....*....|.
gi 727160149   166 LVYSHGPFAWGKDAADAVHNAVVLEEVAIMA 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEIQ 184
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-230 4.58e-175

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 479.72  E-value: 4.58e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDPQ 160
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKRGIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 161 QVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNPQLPDMQQTLLDKHYLRKHGKNAYYGQ 230
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-230 4.91e-148

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 411.52  E-value: 4.91e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLE-GKVREGHRKPSSDTATH 79
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIAsGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  80 LALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDP 159
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEERGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149 160 QQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
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 ...
 1-230 3.45e-145

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: 404.21  E-value: 3.45e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLE-GKVREGHRKPSSDTATH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   80 LALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDP 159
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149  160 QQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-230 9.22e-136

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 380.30  E-value: 9.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   2 LNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHLA 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  82 LYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQagRDPQQ 161
Cdd:PRK12348  81 LYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGN--AEPLH 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727160149 162 VPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK12348 159 TPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-230 1.39e-122

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 347.10  E-value: 1.39e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLE-GKVREGHRKPSSDTATH 79
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLAtGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  80 LALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDP 159
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEQGLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149 160 QQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-230 1.88e-117

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 334.49  E-value: 1.88e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIAGDYEGETGKVIIETFNQAGRDPQ 160
Cdd:PRK13145  82 ELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKRGLDPM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 161 QVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKHGKHAYYGQ 230
Cdd:PRK13145 162 AVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQINPRVEPAPQYIMDKHYLRKHGPNAYYGQ 231
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-222 2.10e-89

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: 262.30  E-value: 2.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   3 NELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGhRKPSSDTATHLAL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  83 YRAFADIGGVVHTHSRNATIWAQAGQ-PIPALGTTHADYFYGDIPCTRPMSEaeiagdyegETGKVIIETFNQAGrdPQQ 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVYFTGDIPCTPYMTP---------ETGEDEIGTQRALG--FPN 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727160149 162 VPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIAPMQPELLDKHFLRKH 222
Cdd:cd00398  149 SKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLELLNKEYLRKH 209
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-230 5.13e-74

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 223.73  E-value: 5.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTrPMseAEIAGDyegETGKVIIETFnQAGRDpq 160
Cdd:PRK06557  87 YVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVG-PF--ALIGDE---AIGKGIVETL-KGGRS-- 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 161 qvPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLApAIAPMQPELLDKHFLRKHGKhayYGQ 230
Cdd:PRK06557 158 --PAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVHIARQLG-EPIPIPQEEIDRLYDRYQNV---YGQ 221
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-223 1.24e-73

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: 222.40  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQsGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTrpmseaeiagDYEG----ETGKVIIETFnqag 156
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVV----------PYAGpgteELAEAIAEAL---- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727160149 157 rdpQQVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIaPMQPELLDKHfLRKHG 223
Cdd:COG0235  147 ---GDRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGPL-VLSDEEIDKL-ARKFG 208
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-193 1.54e-62

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: 192.76  E-value: 1.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    7 RQVLAANLSLPAYGLVTFTWGNVSAIDRQsGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHLALYRAF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   87 ADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCTRPMSEAEIagdyegETGKVIIETFNQAgrdpqqVPGVL 166
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTE------ELGERIAEALGGD------RKAVL 147

                         170       180
                  ....*....|....*....|....*..
gi 727160149  167 VYSHGPFAWGKDAADAVHNAVVLEEVA 193
Cdd:pfam00596 148 LRNHGLLVWGKTLEEAFYLAEELERAA 174
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-196 1.58e-60

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


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 188.23  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149     9 VLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREG--HRKPSSDTATHLALYRAF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGggGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    87 ADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYG-DIPCTRPMSEAEIAGDYEGETGKVIIETFnqagrdpQQVPGV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEAL-------PDRPAV 153

                          170       180       190
                   ....*....|....*....|....*....|.
gi 727160149   166 LVYSHGPFAWGKDAADAVHNAVVLEEVAIMA 196
Cdd:smart01007 154 LLRNHGLLVWGKTLEEAFDLAEELEEAAEIQ 184
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 9-223 1.06e-28

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 107.42  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   9 VLAANLSLPAYGLVTFTWGNVSAiDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGH--RKPSSDTATHLALYRAF 86
Cdd:PRK05874  11 VLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKdgRSPSTELNLHLACYRAF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  87 ADIGGVVHTHSRNATIWAQAGQPIPALGTTHADYFYGDIPCtrpmseAEIAGDYEGETGKviietfnQAGRDPQQVPGVL 166
Cdd:PRK05874  90 DDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRC------TEYAASGTPEVGR-------NAVRALEGRAAAL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 727160149 167 VYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPAIaPMqPELLDKHFLRKHG 223
Cdd:PRK05874 157 IANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPV-PI-PEDVCRNFTGVYG 211
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-230 1.74e-26

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 101.75  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHL 80
Cdd:PRK06833   2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  81 ALYRAFADIGGVVHTHSRNATIWAQAGQPIPALGTTHAdyFYG-DIPCTRpmseaeiagdYEGETGKVIIETFNQAGRDP 159
Cdd:PRK06833  82 IFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA--VAGpNVRCAE----------YATFGTKELAENAFEAMEDR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727160149 160 QqvpGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLApaiapmQPELL-DKHFLRKHGKHAYYGQ 230
Cdd:PRK06833 150 R---AVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQTKSIG------EPKLLpEDEMENMAEKFKTYGQ 212
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 2-190 1.33e-25

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: 98.49  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149    2 LNELKRQvlaanlsLPAYGLVTFTWGNVSAIDRQSGLVvIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHLA 81
Cdd:TIGR03328   1 LIEAGRD-------LYKRGWVPGTGGNLSARLDEDEIL-ITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   82 LYRAFaDIGGVVHTHSRNATI----WAQAGqPIPALG----------TTHADYFygDIPC-TRPMSEAEIAgdyegetgk 146
Cdd:TIGR03328  73 LYRLT-GAGAVLHTHSVEATVlsrlYPSNG-GFELEGyemlkglpgiTTHEDTL--VVPIiENTQDIARLA--------- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 727160149  147 viiETFNQAGRDPQQVPGVLVYSHGPFAWGKDAADAVHNAVVLE 190
Cdd:TIGR03328 140 ---DSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALE 180
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
3-127 2.13e-20

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 85.56  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   3 NELKRQVLAANLSLPAYGLVTFTWGNVSAidRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGhRKPSSDTATHLAL 82
Cdd:PRK08087   4 NKLARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEG-KLPSSEWRFHMAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727160149  83 YRAFADIGGVVHTHSRNATIWAQAGQPIPAL-------GTTHadyfygdIPC 127
Cdd:PRK08087  81 YQTRPDANAVVHNHAVHCTAVSILNRPIPAIhymiaaaGGNS-------IPC 125
PRK08130 PRK08130
putative aldolase; Validated
 3-224 2.78e-15

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 71.83  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   3 NELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVvIKPSGIAYEAMTLEDLVVVDLEGKVREGHrKPSSDTATHLAL 82
Cdd:PRK08130   4 QALREEIVRLGRSLFQRGYTVGSAGNISARLDDGGWL-VTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  83 YRAFADIGGVVHTHSRNATIWAQAG-----QPIPALgtthADYFY---GD---IPCTRPMSEAeIAGDYEGETGKviiet 151
Cdd:PRK08130  82 YRNNPECGAVVHLHSTHLTALSCLGgldptNVLPPF----TPYYVmrvGHvplIPYYRPGDPA-IAEALAGLAAR----- 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727160149 152 fnqagrdpqqVPGVLVYSHGPFAWGKDAADAVHNAVVLEEVAIMAMATRQLAPaiAPMQPELLDKhfLRKHGK 224
Cdd:PRK08130 152 ----------YRAVLLANHGPVVWGSSLEAAVNATEELEETAKLILLLGGRPP--RYLTDEEIAE--LRSTFG 210
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
1-182 2.27e-14

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 69.20  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   1 MLNELKRQVLAANLSLPAYGLVTFTWGNVSAidRQS-GLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATH 79
Cdd:PRK09220   2 TLEELLQQLIAAGRWIGARGWVPATSGNMSV--RLDeQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  80 LALYRAFADIGGVVHTHSRNATIW------------------AQAGQpipalgTTHADYFygDIPCtrpmseaeIAGDYE 141
Cdd:PRK09220  80 TQLYRLFPEIGAVLHTHSVNATVLsrveksdalvlegyelqkAFAGQ------TTHETAV--VVPI--------FDNDQD 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 727160149 142 GETGKVIIETFNQAGRDPqqvPGVLVYSHGPFAWGKDAADA 182
Cdd:PRK09220 144 IARLAARVAPYLDAQPLR---YGYLIRGHGLYCWGRDMAEA 181
PRK08333 PRK08333
aldolase;
20-193 2.78e-12

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 62.92  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  20 GLVTFTWGNVSAidRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRkPSSDTATHLALYRAFADIGGVVHTHsrn 99
Cdd:PRK08333  19 GLTAAFGGNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSSVR-PSSEYRLHLAVYRNRPDVRAIAHLH--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 100 atiwaqagqpiPALGTTHADYFYGDIPCTRPmsEAEIAgdyegeTGKVIIETFNQAGRD--PQQVPG-------VLVYSH 170
Cdd:PRK08333  93 -----------PPYSIVASTLLEEELPIITP--EAELY------LKKIPILPFRPAGSVelAEQVAEamkeydaVIMERH 153

                        170       180
                 ....*....|....*....|...
gi 727160149 171 GPFAWGKDAADAVHNAVVLEEVA 193
Cdd:PRK08333 154 GIVTVGRSLREAFYKAELVEESA 176
PRK06486 PRK06486
aldolase;
7-123 2.41e-08

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 53.18  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   7 RQVLAANLSLPA-YGLVTFTWGNVSA-IDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSdTA--THLAL 82
Cdd:PRK06486  28 RVDLAACFRAAArHGLEEGICNHFSAvLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPEA-TAffIHARI 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 727160149  83 YRAFADIGGVVHTHSRNATIWA-QAGQPIPALGTThADYFYG 123
Cdd:PRK06486 107 HRAIPRAKAAFHTHMPYATALSlTEGRPLTTLGQT-ALKFYG 147
PRK08660 PRK08660
aldolase;
16-191 3.22e-08

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 51.50  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  16 LPAYGLVTFTWGNVSAidRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREgHRKPSSDTATHLALYRAfADIGGVVHT 95
Cdd:PRK08660  12 LFAHGLVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSV-DPLASSETPVHRAIYRR-TSAKAIVHA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  96 HSRNATIWA-QAGQPIPALGTTHadYFYGDIPCTrpmsEAEIAgdyEGETGKVIIETFNQAGrdpqqvpGVLVYSHGPFA 174
Cdd:PRK08660  88 HPPYAVALSlLEDEIVPLDSEGL--YFLGTIPVV----GGDIG---SGELAENVARALSEHK-------GVVVRGHGTFA 151

                        170
                 ....*....|....*..
gi 727160149 175 WGKDAADAVHNAVVLEE 191
Cdd:PRK08660 152 IGKTLEEAYIYTSQLEH 168
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
2-182 1.19e-07

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 50.43  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   2 LNELKRQvLAANLSLPAyglvtfTWGNVSAIDRQSGLV-VIKPSGIAYEAMTLEDLVVVDLEGK-VREGHRKPSSDTATH 79
Cdd:PRK06754  11 LAEIKKE-LAARDWFPA------TSGNLSIKVSDDPLTfLVTASGKDKRKTTPEDFLLVDHDGKpVEETELKPSAETLLH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  80 LALYRAfADIGGVVHTHSRN----ATIWAQAGQP-------IPALGTTHADYF--------YGDIPctrpmSEAEiagdy 140
Cdd:PRK06754  84 THIYNN-TNAGCVLHVHTVDnnviSELYGDDGAVtfqgqeiIKALGIWEENAEihipiienHADIP-----TLAE----- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 727160149 141 egETGKVIIEtfnqagrdpqQVPGVLVYSHGPFAWGKDAADA 182
Cdd:PRK06754 153 --EFAKHIQG----------DSGAVLIRNHGITVWGRDAFEA 182
PRK06357 PRK06357
hypothetical protein; Provisional
 54-134 1.28e-07

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 50.54  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  54 EDLVVVDLE-GKVREGHRKPSSDTATHLALYRAFADIGGVVHTHSRNATIWAQAGQPIPALgtTHADYFYGDIPCTrPMS 132
Cdd:PRK06357  61 YQILVVDLNtGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNL--TEATQKLGKIPTL-PFA 137


                 ..
gi 727160149 133 EA 134
Cdd:PRK06357 138 PA 139
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 27-213 3.68e-06

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 46.55  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  27 GNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTATHLALYRAFADIGGVVHTHSRNATIWAQA 106
Cdd:PRK07090  53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSML 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 107 GQPipaLGTTHADY--FYGD---------IPctrpmseaeiAGDYEGEtgkvIIETFNQAGRdpqqvpGVLVYSHGPFAW 175
Cdd:PRK07090 133 EVP---LVVSHMDTcpLYDDcaflkdwpgVP----------VGNEEGE----IISAALGDKR------AILLSHHGQLVA 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 727160149 176 GKDAADAVHNAVVLEEVA---IMAMAtrqlAPAIAPMQPEL 213
Cdd:PRK07090 190 GKSIEEACVLALLIERAArlqLLAMA----AGPIKPIPPEL 226
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 41-217 7.08e-06

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 45.61  E-value: 7.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  41 IKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDT--ATHLALYRAFADIGGVVHTHSRNAT-IWAQAG--QPIpalgT 115
Cdd:PRK07044  54 INPYGLLFDEITASNLVKIDLDGNVVDDSPYPVNPAgfTIHSAIHAARPDAHCVMHTHTTAGVaVSAQRDglLPL----S 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149 116 THADYFYGDipctrpmseaeIA-GDYEG-----ETGKVIIetfnqagRDPQQVPGVLVYSHGPFAWGKDAADAVHNAVVL 189
Cdd:PRK07044 130 QHALQFYGR-----------LAyHDYEGialdlDEGERLV-------ADLGDKPAMLLRNHGLLTVGRTVAEAFLLMYTL 191

                        170       180
                 ....*....|....*....|....*...
gi 727160149 190 EEVAIMAMATRQLAPAIAPMQPELLDKH 217
Cdd:PRK07044 192 ERACEIQVAAQAGGGELVLPPPEVAERT 219
PRK06208 PRK06208
class II aldolase/adducin family protein;
43-124 1.55e-05

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 44.59  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149  43 PSGIAYEAMTLEDLVVVDLEGKVREG-HRKPSSDTATHLALYRAFADIGGVVHTHSRNATIWAQAGQPIPALgTTHADYF 121
Cdd:PRK06208  82 PLGVHFSQIKVSDLLLVDHDGEVVEGdRPLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPI-TQDACAF 160


                 ...
gi 727160149 122 YGD 124
Cdd:PRK06208 161 YED 163
PRK06661 PRK06661
hypothetical protein; Provisional
 4-97 1.56e-05

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 44.44  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727160149   4 ELKRQVLAANLSLPAYGLVTFTWGNVSAIDRQSGLVVIKPSGIAYEAMTLEDLVVVDLEGKVREGHRKPSSDTA--THLA 81
Cdd:PRK06661   2 DIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGyfIHGS 81

                         90
                 ....*....|....*.
gi 727160149  82 LYRAFADIGGVVHTHS 97
Cdd:PRK06661  82 IYKTRPDISAIFHYHT 97
 
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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