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Conserved domains on  [gi|930452108|ref|WP_054200170|]
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MULTISPECIES: L-ribulose-5-phosphate 4-epimerase [Clostridium]

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 5.96e-171

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


:

Pssm-ID: 236181  Cd Length: 231  Bit Score: 469.32  E-value: 5.96e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFKD--LNPD 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108 159 YIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQS 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQL-NPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-230 5.96e-171

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 469.32  E-value: 5.96e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFKD--LNPD 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108 159 YIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQS 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQL-NPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-229 2.80e-134

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: 376.86  E-value: 2.80e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLD-GNVVEGNYRPSSDTDTH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   80 IKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVE--RFKDLNP 157
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVEtfEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108  158 DYIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQ 229
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQL-NPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-222 6.73e-78

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: 233.18  E-value: 6.73e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREkGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTR--EEIegnyeyntGTVIVERFKDlnpd 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGD---- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930452108 159 yIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILanQRVNSMSEDLLNKHFtRKHG 222
Cdd:COG0235  149 -RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAL--GGPLVLSDEEIDKLA-RKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-221 7.00e-78

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: 233.03  E-value: 7.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   3 EDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGnYRPSSDTDTHIKL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  83 YKEFKNIGGVVHTHSRWATIFAQAGKGIKPYG-TTQADYFADEIPCTRDMTREeiegnyeynTGTVIVERFKDLNPDYIP 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEGLIPAGhTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGFPNSK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 162 AVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILANQrVNSMSEDLLNKHFTRKH 221
Cdd:cd00398  151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQ-LPPISLELLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-195 1.15e-70

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: 213.56  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    7 KEVYKANMLLPKYNLVTFTWGNVSAIDrEKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIKLYKEF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   87 KNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEgnyeynTGTVIVERFKdlnpDYIPAVLVK 166
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALG----GDRKAVLLR 149

                         170       180
                  ....*....|....*....|....*....
gi 930452108  167 NHGPFTWGKDANEAVHNAVVLEEVAMMAY 195
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-195 5.41e-65

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: 199.40  E-value: 5.41e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108     9 VYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEG--NYRPSSDTDTHIKLYKEF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGggGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    87 KNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYF-ADEIPCTRDMTREEIEGNYEYNTGTVIVERFKDlnpdyIPAVLV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFlGGEIPYAPYAGPGTELAEEGAELAEALAEALPD-----RPAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 930452108   166 KNHGPFTWGKDANEAVHNAVVLEEVAMMAY 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
1-230 5.96e-171

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 469.32  E-value: 5.96e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK08193   1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFKD--LNPD 158
Cdd:PRK08193  81 VLYKAFPEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDPA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108 159 YIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQS 230
Cdd:PRK08193 161 AVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQL-NPQLPDMQQTLLDKHYLRKHGKNAYYGQK 231
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 1-229 2.80e-134

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: 376.86  E-value: 2.80e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLD-GNVVEGNYRPSSDTDTH 79
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   80 IKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVE--RFKDLNP 157
Cdd:TIGR00760  81 LALYRAFPSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVEtfEKRGIDP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108  158 DYIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQ 229
Cdd:TIGR00760 161 AQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQL-NPQLPPMQQTLLDKHYLRKHGANAYYGQ 231
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-229 1.16e-132

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 372.60  E-value: 1.16e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   2 LEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIK 81
Cdd:PRK12348   1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  82 LYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFKDLNPDYIP 161
Cdd:PRK12348  81 LYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNAEPLHTP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930452108 162 AVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQ 229
Cdd:PRK12348 161 GIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGI-NPQLNHIDSYLMNKHFMRKHGPNAYYGQ 227
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-229 3.83e-125

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 353.74  E-value: 3.83e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDL-DGNVVEGNYRPSSDTDTH 79
Cdd:PRK12347   1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIaSGKVVEGSKKPSSDTPTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  80 IKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERF--KDLNP 157
Cdd:PRK12347  81 LALYRRYPEIGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFeeRGISP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108 158 DYIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILANQrVNSMSEDLLNKHFTRKHGPNAYYGQ 229
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQLAPQ-LPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-232 4.68e-114

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 325.63  E-value: 4.68e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK13145   2 NLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTHV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFK--DLNPD 158
Cdd:PRK13145  82 ELYKAWPEVGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEkrGLDPM 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930452108 159 YIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQSGA 232
Cdd:PRK13145 162 AVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQI-NPRVEPAPQYIMDKHYLRKHGPNAYYGQKGD 234
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 1-229 1.06e-102

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 297.02  E-value: 1.06e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDL-DGNVVEGNYRPSSDTDTH 79
Cdd:PRK13213   1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLaTGKVVEGDKKPSSDTDTH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  80 IKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEGNYEYNTGTVIVERFKD--LNP 157
Cdd:PRK13213  81 LVLYRAFAEIGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFAEqgLRA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930452108 158 DYIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILaNQRVNSMSEDLLNKHFTRKHGPNAYYGQ 229
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQL-TPGVGDMQQTLLDKHYLRKHGAAAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-222 6.73e-78

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: 233.18  E-value: 6.73e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREkGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:COG0235    2 EEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTR--EEIegnyeyntGTVIVERFKDlnpd 158
Cdd:COG0235   81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPYAGPgtEEL--------AEAIAEALGD---- 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930452108 159 yIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILanQRVNSMSEDLLNKHFtRKHG 222
Cdd:COG0235  149 -RPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAL--GGPLVLSDEEIDKLA-RKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 3-221 7.00e-78

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: 233.03  E-value: 7.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   3 EDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGnYRPSSDTDTHIKL 82
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEG-KKPSSETPLHLAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  83 YKEFKNIGGVVHTHSRWATIFAQAGKGIKPYG-TTQADYFADEIPCTRDMTREeiegnyeynTGTVIVERFKDLNPDYIP 161
Cdd:cd00398   80 YRARPDIGCIVHTHSTHATAVSQLKEGLIPAGhTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGFPNSK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 162 AVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILANQrVNSMSEDLLNKHFTRKH 221
Cdd:cd00398  151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQ-LPPISLELLNKEYLRKH 209
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 1-195 9.84e-75

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 225.66  E-value: 9.84e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK06557   7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCT--RDMTREEIegnyeyntGTVIVERFKDLNPd 158
Cdd:PRK06557  87 YVYRHMPDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVGpfALIGDEAI--------GKGIVETLKGGRS- 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 930452108 159 yiPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAY 195
Cdd:PRK06557 158 --PAVLMQNHGVFTIGKDAEDAVKAAVMVEEVARTVH 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 7-195 1.15e-70

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: 213.56  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    7 KEVYKANMLLPKYNLVTFTWGNVSAIDrEKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIKLYKEF 86
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL-PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   87 KNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTRDMTREEIEgnyeynTGTVIVERFKdlnpDYIPAVLVK 166
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALG----GDRKAVLLR 149

                         170       180
                  ....*....|....*....|....*....
gi 930452108  167 NHGPFTWGKDANEAVHNAVVLEEVAMMAY 195
Cdd:pfam00596 150 NHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 9-195 5.41e-65

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: 199.40  E-value: 5.41e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108     9 VYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEG--NYRPSSDTDTHIKLYKEF 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGggGPKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108    87 KNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYF-ADEIPCTRDMTREEIEGNYEYNTGTVIVERFKDlnpdyIPAVLV 165
Cdd:smart01007  81 PDVGAVVHTHSPYATALAALGKPLPLLPTEQAAAFlGGEIPYAPYAGPGTELAEEGAELAEALAEALPD-----RPAVLL 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 930452108   166 KNHGPFTWGKDANEAVHNAVVLEEVAMMAY 195
Cdd:smart01007 156 RNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-229 2.77e-29

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 109.07  E-value: 2.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   1 MLEDLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHI 80
Cdd:PRK06833   2 LLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMHL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  81 KLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQAdYFADEIPCTRDMTreeiegnyeYNTGTVIVERFKDLNPDYi 160
Cdd:PRK06833  82 IFYRNREDINAIVHTHSPYATTLACLGWELPAVHYLIA-VAGPNVRCAEYAT---------FGTKELAENAFEAMEDRR- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 161 pAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILANQRVNSMSE-DLLNKHFTRkhgpnayYGQ 229
Cdd:PRK06833 151 -AVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQTKSIGEPKLLPEDEmENMAEKFKT-------YGQ 212
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 22-188 1.44e-27

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: 103.88  E-value: 1.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   22 VTFTWGNVSAIDREKGlIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIKLYKEFkNIGGVVHTHSRWAT 101
Cdd:TIGR03328  14 VPGTGGNLSARLDEDE-ILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRLT-GAGAVLHTHSVEAT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  102 I----FAQAGK-GIKPYGTTQAdyfadeipctrdmtreeIEGNYEYNTGTVI---------------VERFKDLNPDyIP 161
Cdd:TIGR03328  92 VlsrlYPSNGGfELEGYEMLKG-----------------LPGITTHEDTLVVpiientqdiarladsVAPALNAYPD-VP 153

                         170       180
                  ....*....|....*....|....*..
gi 930452108  162 AVLVKNHGPFTWGKDANEAVHNAVVLE 188
Cdd:TIGR03328 154 GVLIRGHGLYAWGRDWEEAKRHLEALE 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 2-222 5.12e-21

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 87.39  E-value: 5.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   2 LEDLKKEVYKANMLLPKYNLVTFTWGNVSAiDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEG--NYRPSSDTDTH 79
Cdd:PRK05874   4 VDDPESAVLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAkdGRSPSTELNLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  80 IKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYGTTQADYFADEIPCTrdmtreeiegnyEY-NTGTVIVERFKDLNPD 158
Cdd:PRK05874  83 LACYRAFDDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT------------EYaASGTPEVGRNAVRALE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 930452108 159 YIPAVLVKNHGPFTWGKDANEAVHNAVVLEEVAMMAYNTEILANQRvnSMSEDlLNKHFTRKHG 222
Cdd:PRK05874 151 GRAAALIANHGLVAVGPRPDQVLRVTALVERTAQIVWGARALGGPV--PIPED-VCRNFTGVYG 211
PRK08333 PRK08333
aldolase;
27-199 2.73e-17

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 76.79  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  27 GNVSAidREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGnYRPSSDTDTHIKLYKEFKNIGGVVHTHSRWATIFAQA 106
Cdd:PRK08333  26 GNLSI--RVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSS-VRPSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 107 GKGIKPYGTTQADYFADEIPCT--RDMTREEIegnyeyntGTVIVERFKDLNpdyipAVLVKNHGPFTWGKDANEAVHNA 184
Cdd:PRK08333 103 LEEELPIITPEAELYLKKIPILpfRPAGSVEL--------AEQVAEAMKEYD-----AVIMERHGIVTVGRSLREAFYKA 169

                        170
                 ....*....|....*
gi 930452108 185 VVLEEVAMMAYNTEI 199
Cdd:PRK08333 170 ELVEESAKLWYLKFK 184
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
25-180 1.63e-14

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 69.58  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  25 TWGNVSAiDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIKLYKEFKNIGGVVHTHSRWATIFA 104
Cdd:PRK09220  26 TSGNMSV-RLDEQHCAITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTHSVNATVLS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 105 QAGKG----IKPY-------G-TTQADyfADEIPC---TRDMTREeiegnyeyntgTVIVERFKDLNPDYiPAVLVKNHG 169
Cdd:PRK09220 105 RVEKSdalvLEGYelqkafaGqTTHET--AVVVPIfdnDQDIARL-----------AARVAPYLDAQPLR-YGYLIRGHG 170

                        170
                 ....*....|.
gi 930452108 170 PFTWGKDANEA 180
Cdd:PRK09220 171 LYCWGRDMAEA 181
PRK08130 PRK08130
putative aldolase; Validated
 27-211 1.05e-12

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 64.90  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  27 GNVSAidR-EKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNyRPSSDTDTHIKLYKEFKNIGGVVHTHSRWATIFAQ 105
Cdd:PRK08130  28 GNISA--RlDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAIYRNNPECGAVVHLHSTHLTALSC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 106 AG--------KGIKPYGTTQadyfADEIPCTRdmtreeiegnYeYNTG-TVIVERFKDLNPDYiPAVLVKNHGPFTWGKD 176
Cdd:PRK08130 105 LGgldptnvlPPFTPYYVMR----VGHVPLIP----------Y-YRPGdPAIAEALAGLAARY-RAVLLANHGPVVWGSS 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 930452108 177 ANEAVHNAVVLEEVAMMAYnteILANQRVNSMSED 211
Cdd:PRK08130 169 LEAAVNATEELEETAKLIL---LLGGRPPRYLTDE 200
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
25-127 3.14e-11

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 60.91  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  25 TWGNVSAidREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYrPSSDTDTHIKLYKEFKNIGGVVHTHSRWATIFA 104
Cdd:PRK08087  26 TAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKL-PSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVS 102

                         90       100
                 ....*....|....*....|...
gi 930452108 105 QAGKGIKPYGTTQADYFADEIPC 127
Cdd:PRK08087 103 ILNRPIPAIHYMIAAAGGNSIPC 125
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
2-180 7.01e-11

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 59.68  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   2 LEDLKKEVYKANMLLPkynlvtfTWGNVS-AIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEG-NYRPSSDTDTH 79
Cdd:PRK06754  11 LAEIKKELAARDWFPA-------TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEEtELKPSAETLLH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  80 IKLYKEfKNIGGVVHTHSRWATIFAQAgkgikpYGTTQADYFADEipctrdmtrEEIE--GNYEYN-TGTV-IVERFKDL 155
Cdd:PRK06754  84 THIYNN-TNAGCVLHVHTVDNNVISEL------YGDDGAVTFQGQ---------EIIKalGIWEENaEIHIpIIENHADI 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 930452108 156 -----------NPDyIPAVLVKNHGPFTWGKDANEA 180
Cdd:PRK06754 148 ptlaeefakhiQGD-SGAVLIRNHGITVWGRDAFEA 182
PRK06357 PRK06357
hypothetical protein; Provisional
 27-107 2.08e-07

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 49.77  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  27 GNVS---AIDREKGLIVIKP---SGVEYDAMQPEDMVVVDLD-GNVVEGNYRPSSDTDTHIKLYKEFKNIGGVVHTHSRW 99
Cdd:PRK06357  28 GNISvrmTAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNtGEVIEGVGRVTREINMHEAAYVANPKIKCVYHSHAKE 107


                 ....*...
gi 930452108 100 ATIFAQAG 107
Cdd:PRK06357 108 SMFWATLG 115
PRK06661 PRK06661
hypothetical protein; Provisional
 4-206 7.08e-07

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 48.67  E-value: 7.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108   4 DLKKEVYKANMLLPKYNLVTFTWGNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTD--THIK 81
Cdd:PRK06661   2 DIKYNLAAAYRIMAYLSLDDHTYTHLSARPKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGyfIHGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  82 LYKEFKNIGGVVHTHSRWATIFAQAGKGIKPYgTTQADYFADEIpctrdmtreeieGNYEYNT--------GTVIVerfK 153
Cdd:PRK06661  82 IYKTRPDISAIFHYHTPASIAVSALKCGLLPI-SQWALHFYDRI------------SYHNYNSlaldadkqSSRLV---N 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 930452108 154 DLNPDYipAVLVKNHGPFTWGKDANEAVHNAVVLEEvammAYNTEILANQRVN 206
Cdd:PRK06661 146 DLKQNY--VMLLRNHGAITCGKTIHEAMFYTYHLEQ----ACKTQCLLNSTKK 192
PRK08660 PRK08660
aldolase;
21-200 4.09e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 45.72  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  21 LVTFTWGNVSAidREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNvveGNYRP--SSDTDTHIKLYKEfKNIGGVVHTHSR 98
Cdd:PRK08660  17 LVSSHFGNISV--RTGDGLLITRTGSMLDEITEGDVIEVGIDDD---GSVDPlaSSETPVHRAIYRR-TSAKAIVHAHPP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  99 WATIFAQAGKGIKPYgTTQADYFADEIPCTR-DMTREEIEGNyeyntgtvIVERFKDLNpdyipAVLVKNHGPFTWGKDA 177
Cdd:PRK08660  91 YAVALSLLEDEIVPL-DSEGLYFLGTIPVVGgDIGSGELAEN--------VARALSEHK-----GVVVRGHGTFAIGKTL 156

                        170       180
                 ....*....|....*....|...
gi 930452108 178 NEAVHNAVVLEEVAMMAYNTEIL 200
Cdd:PRK08660 157 EEAYIYTSQLEHSCKVLYLVRTA 179
PRK06208 PRK06208
class II aldolase/adducin family protein;
43-188 1.69e-05

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 44.59  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  43 PSGVEYDAMQPEDMVVVDLDGNVVEGNYRPS-SDTDTHIKLYKEFKNIGGVVHTHSRWATIFAQAGKGIKPygTTQ---A 118
Cdd:PRK06208  82 PLGVHFSQIKVSDLLLVDHDGEVVEGDRPLNrAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDP--ITQdacA 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 930452108 119 DY-----FADEipctRDMTREEIEgnyeyntGTVIVERFKDLNpdyipAVLVKNHGPFTWGKDANEAVHNAVVLE 188
Cdd:PRK06208 160 FYedhalFDDF----TGVVVDTSE-------GRRIAAALGTHK-----AVILQNHGLLTVGPSVDAAAWWFIALE 218
PRK06486 PRK06486
aldolase;
37-101 8.72e-05

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 42.39  E-value: 8.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 930452108  37 GLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSdtdT----HIKLYKEFKNIGGVVHTHSRWAT 101
Cdd:PRK06486  60 DLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPEA---TaffiHARIHRAIPRAKAAFHTHMPYAT 125
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 27-193 2.82e-04

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 40.77  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108  27 GNVSAIDREKGLIVIKPSGVEYDAMQPEDMVVVDLDGNVVEGNYRPSSDTDTHIKLYKEFKNIGGVVHTHSRWATIFAQA 106
Cdd:PRK07090  53 GQITARAEAPGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPDVNCIIHTHPPHVAALSML 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930452108 107 GkgiKPYGTTQAD---------YFAD--EIPCtrdmtreeieGNYEyntGTVIVERFKDLNpdyipAVLVKNHGPFTWGK 175
Cdd:PRK07090 133 E---VPLVVSHMDtcplyddcaFLKDwpGVPV----------GNEE---GEIISAALGDKR-----AILLSHHGQLVAGK 191

                        170
                 ....*....|....*...
gi 930452108 176 DANEAVHNAVVLEEVAMM 193
Cdd:PRK07090 192 SIEEACVLALLIERAARL 209
 
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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