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Conserved domains on  [gi|1942515635|ref|WP_197414893|]
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L-ribulose-5-phosphate 4-epimerase [Olsenella sp. DNF00959]

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;
2-236 1.88e-158

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


:

Pssm-ID: 236181  Cd Length: 231  Bit Score: 438.11  E-value: 1.88e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHA 81
Cdd:PRK08193    1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  82 YLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFEA--LDP 159
Cdd:PRK08193   81 VLYKAF-PEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635 160 IAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGvmgkpvKEAEAPQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK08193  160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNP------QLPDMQQTLLDKHYLRKHGKNAYYGQ 230
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
2-236 1.88e-158

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 438.11  E-value: 1.88e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHA 81
Cdd:PRK08193    1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  82 YLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFEA--LDP 159
Cdd:PRK08193   81 VLYKAF-PEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635 160 IAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGvmgkpvKEAEAPQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK08193  160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNP------QLPDMQQTLLDKHYLRKHGKNAYYGQ 230
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 2-236 3.94e-114

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: 326.01  E-value: 3.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLD-GKVVEGELNPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFE--ALD 158
Cdd:TIGR00760  81 LALYRAF-PSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEkrGID 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942515635 159 PIAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGVMgKPVKeaeapQYLLDKHYMRKHGPNAYYGQ 236
Cdd:TIGR00760 160 PAQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQL-PPMQ-----QTLLDKHYLRKHGANAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-229 3.86e-72

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


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 218.55  E-value: 3.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   1 MMLKELREKVYEANMDLPKYGLVVFTWGNASELDREsGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTH 80
Cdd:COG0235     1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMR--GLTKEEIEEAyelntgkvIAEGFEald 158
Cdd:COG0235    80 LAIYRARPD-VGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPyaGPGTEELAEA--------IAEALG--- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1942515635 159 piAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETlcgvMGKPVkeaEAPQYLLDKHYmRKHG 229
Cdd:COG0235   148 --DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA----LGGPL---VLSDEEIDKLA-RKFG 208
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 5-228 3.68e-65

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: 201.05  E-value: 3.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   5 ELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELnPSSDTPTHAYLY 84
Cdd:cd00398     2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  85 RAWgDKVGGIVHTHSNCAVAWAQAG-RSIPCYGTTQADYFYGSIPCMRGLTKEeieeayelnTGKVIAEGFEALDPIAQP 163
Cdd:cd00398    81 RAR-PDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGFPNSK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1942515635 164 GCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGvmGKPVKEAEapqyLLDKHYMRKH 228
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG--QLPPISLE----LLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-193 2.17e-61

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


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 190.45  E-value: 2.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   8 EKVYEANMDLPKYGLVVFTWGNASELDREsGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAYLYRAW 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  88 GDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEeayelnTGKVIAEGFEAldpiAQPGCLV 167
Cdd:pfam00596  80 PD-AGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGG----DRKAVLL 148

                         170       180
                  ....*....|....*....|....*.
gi 1942515635 168 RNHGPFSWGKDAAQAVYHAKVMEETA 193
Cdd:pfam00596 149 RNHGLLVWGKTLEEAFYLAEELERAA 174
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-193 1.28e-58

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


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 183.61  E-value: 1.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   10 VYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGEL--NPSSDTPTHAYLYRAW 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   88 GDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYG-SIPCMRGLTKEEIEEAYELNTGKVIAEGFEaldpiAQPGCL 166
Cdd:smart01007  81 PD-VGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALP-----DRPAVL 154

                          170       180
                   ....*....|....*....|....*..
gi 1942515635  167 VRNHGPFSWGKDAAQAVYHAKVMEETA 193
Cdd:smart01007 155 LRNHGLLVWGKTLEEAFDLAEELEEAA 181
 
Name Accession Description Interval E-value
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
2-236 1.88e-158

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 438.11  E-value: 1.88e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHA 81
Cdd:PRK08193    1 MLEDLKQEVLEANLALPKHGLVTFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVVDLEGNVVEGKLKPSSDTPTHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  82 YLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFEA--LDP 159
Cdd:PRK08193   81 VLYKAF-PEIGGIVHTHSRHATAWAQAGRDIPALGTTHADYFYGDIPCTRKMTDEEINGEYEWETGKVIVETFEKrgIDP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635 160 IAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGvmgkpvKEAEAPQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK08193  160 AAVPGVLVHSHGPFTWGKDAEDAVHNAVVLEEVAKMAYFTRQLNP------QLPDMQQTLLDKHYLRKHGKNAYYGQ 230
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 1-237 2.28e-140

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 392.66  E-value: 2.28e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   1 MMLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTH 80
Cdd:PRK13145    1 KNLQEMRERVCAANKSLPKHGLVKFTWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEGDLNPSSDLPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFEA--LD 158
Cdd:PRK13145   81 VELYKAWPE-VGGIVHTHSTEAVGWAQAGRDIPFYGTTHADYFYGPIPCARSLTKDEVNGAYEKETGSVIIEEFEKrgLD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1942515635 159 PIAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLcgvmgKPVKEaEAPQYLLDKHYMRKHGPNAYYGQG 237
Cdd:PRK13145  160 PMAVPGIVVRNHGPFTWGKNPEQAVYHSVVLEEVAKMNRLTEQI-----NPRVE-PAPQYIMDKHYLRKHGPNAYYGQK 232
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 3-236 2.09e-122

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 346.79  E-value: 2.09e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   3 LKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAY 82
Cdd:PRK12348    1 MQKLKQQVFEANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  83 LYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFEALDPIAQ 162
Cdd:PRK12348   81 LYRRYPS-LGGIVHTHSTHATAWAQAGLAIPALGTTHADYFFGDIPCTRGLSEEEVQGEYELNTGKVIIETLGNAEPLHT 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1942515635 163 PGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGVMgKPVKeaeapQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK12348  160 PGIVVYQHGPFAWGKDAHDAVHNAVVMEEVAKMAWIARGINPQL-NHID-----SYLMNKHFMRKHGPNAYYGQ 227
araD TIGR00760
L-ribulose-5-phosphate 4-epimerase; E. coli has two genes, sgaE and sgbE (YiaS), that are very ...
 2-236 3.94e-114

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: 326.01  E-value: 3.94e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLD-GKVVEGELNPSSDTPTH 80
Cdd:TIGR00760   1 MLEQLKKEVLEANLALPKHQLVTFTWGNVSAIDRERGLVVIKPSGVEYDVMTADDMVVVDLEtGNVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFE--ALD 158
Cdd:TIGR00760  81 LALYRAF-PSIGGIVHTHSRHATIWAQAGKDIPALGTTHADYFYGTIPCTRPMTDEEINGEYELETGKVIVETFEkrGID 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942515635 159 PIAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGVMgKPVKeaeapQYLLDKHYMRKHGPNAYYGQ 236
Cdd:TIGR00760 160 PAQIPGVLVHSHGPFAWGKDAANAVHNAVVLEEVAYMALFSRQLNPQL-PPMQ-----QTLLDKHYLRKHGANAYYGQ 231
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-236 1.32e-107

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 309.44  E-value: 1.32e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDL-DGKVVEGELNPSSDTPTH 80
Cdd:PRK12347    1 MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIaSGKVVEGSKKPSSDTPTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGFE--ALD 158
Cdd:PRK12347   81 LALYRRYPE-IGGIVHTHSRHATIWSQAGLDLPAWGTTHADYFYGAIPCTRLMTAEEINGEYEYQTGEVIIETFEerGIS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942515635 159 PIAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLcgvmgKPvKEAEAPQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK12347  160 PAQIPAVLVHSHGPFAWGKNAADAVHNAVVLEECAYMGLFSRQL-----AP-QLPAMQNELLDKHYLRKHGANAYYGQ 231
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 2-236 1.29e-89

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 264.28  E-value: 1.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDL-DGKVVEGELNPSSDTPTH 80
Cdd:PRK13213    1 MLEQLKQQVFEANLALPKYKLVTFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLaTGKVVEGDKKPSSDTDTH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEEAYELNTGKVIAEGF--EALD 158
Cdd:PRK13213   81 LVLYRAFAE-IGGIVHTHSRHATIWAQAGKSLSALGTTHADYFYGPIPCTRLMTEAEITGDYEHETGKVIVETFaeQGLR 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1942515635 159 PIAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGVMGkpvkeaEAPQYLLDKHYMRKHGPNAYYGQ 236
Cdd:PRK13213  160 AADIPAVLVNGHGPFAWGSNAANAVHNAVVLEEIAYMNLFTHQLTPGVG------DMQQTLLDKHYLRKHGAAAYYGQ 231
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-229 3.86e-72

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


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 218.55  E-value: 3.86e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   1 MMLKELREKVYEANMDLPKYGLVVFTWGNASELDREsGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTH 80
Cdd:COG0235     1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKPSSETPLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMR--GLTKEEIEEAyelntgkvIAEGFEald 158
Cdd:COG0235    80 LAIYRARPD-VGAVVHTHSPYATALSALGEPLPPLEQTEAAAFLGDVPVVPyaGPGTEELAEA--------IAEALG--- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1942515635 159 piAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETlcgvMGKPVkeaEAPQYLLDKHYmRKHG 229
Cdd:COG0235   148 --DRPAVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA----LGGPL---VLSDEEIDKLA-RKFG 208
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 2-236 1.26e-71

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 217.95  E-value: 1.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   2 MLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHA 81
Cdd:PRK06557    7 MVEKLREEVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKPSSDTASHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  82 YLYRAWgDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPC--MRGLTKEEIeeayelntGKVIAegfEALDP 159
Cdd:PRK06557   87 YVYRHM-PDVGGVVHTHSTYATAWAARGEPIPCVLTAMADEFGGPIPVgpFALIGDEAI--------GKGIV---ETLKG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635 160 IAQPGCLVRNHGPFSWGKDAAQAVYHAKVMEETAlmglRTETLCGVMGKPvkeAEAPQYLLDKHYMRKHgpNAyYGQ 236
Cdd:PRK06557  155 GRSPAVLMQNHGVFTIGKDAEDAVKAAVMVEEVA----RTVHIARQLGEP---IPIPQEEIDRLYDRYQ--NV-YGQ 221
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 5-228 3.68e-65

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: 201.05  E-value: 3.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   5 ELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELnPSSDTPTHAYLY 84
Cdd:cd00398     2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK-PSSETPLHLALY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  85 RAWgDKVGGIVHTHSNCAVAWAQAG-RSIPCYGTTQADYFYGSIPCMRGLTKEeieeayelnTGKVIAEGFEALDPIAQP 163
Cdd:cd00398    81 RAR-PDIGCIVHTHSTHATAVSQLKeGLIPAGHTACAVYFTGDIPCTPYMTPE---------TGEDEIGTQRALGFPNSK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1942515635 164 GCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLCGvmGKPVKEAEapqyLLDKHYMRKH 228
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG--QLPPISLE----LLNKEYLRKH 209
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-193 2.17e-61

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


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 190.45  E-value: 2.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   8 EKVYEANMDLPKYGLVVFTWGNASELDREsGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAYLYRAW 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPG-DGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYRAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  88 GDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMRGLTKEEIEeayelnTGKVIAEGFEAldpiAQPGCLV 167
Cdd:pfam00596  80 PD-AGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIPYYTPGTEE------LGERIAEALGG----DRKAVLL 148

                         170       180
                  ....*....|....*....|....*.
gi 1942515635 168 RNHGPFSWGKDAAQAVYHAKVMEETA 193
Cdd:pfam00596 149 RNHGLLVWGKTLEEAFYLAEELERAA 174
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-193 1.28e-58

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


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 183.61  E-value: 1.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   10 VYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGEL--NPSSDTPTHAYLYRAW 87
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIYRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   88 GDkVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYG-SIPCMRGLTKEEIEEAYELNTGKVIAEGFEaldpiAQPGCL 166
Cdd:smart01007  81 PD-VGAVVHTHSPYATALAALGKPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAELAEALAEALP-----DRPAVL 154

                          170       180
                   ....*....|....*....|....*..
gi 1942515635  167 VRNHGPFSWGKDAAQAVYHAKVMEETA 193
Cdd:smart01007 155 LRNHGLLVWGKTLEEAFDLAEELEEAA 181
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-210 2.08e-23

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 93.66  E-value: 2.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   1 MMLKELREKVYEANMDLPKYGLVVFTWGNASELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTH 80
Cdd:PRK06833    1 MLLQKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKPSSELDMH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHSNCAVA-----W---------AQAGRSIPC--YGTtqadyfYGsipcmrglTKEEIEEAYEL 144
Cdd:PRK06833   81 LIFYRNRED-INAIVHTHSPYATTlaclgWelpavhyliAVAGPNVRCaeYAT------FG--------TKELAENAFEA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1942515635 145 NTGKviaegfealdpiaqPGCLVRNHGPFSWGKDAAQAVYHAKVMEETALMGLRTETLcgvmGKPV 210
Cdd:PRK06833  146 MEDR--------------RAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQTKSI----GEPK 193
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 12-190 7.74e-21

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: 86.55  E-value: 7.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  12 EANMDLPKYGLVVFTWGNASEldRESGL-FVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAYLYRAwgDK 90
Cdd:TIGR03328   3 EAGRDLYKRGWVPGTGGNLSA--RLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVSGGLKPSAETLLHTQLYRL--TG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  91 VGGIVHTHSNCAVA----WAQAGR-SIPCYGTTQADYfygsipcmrGLTKEE-------IE-EAYELNTGKVIAEGFEAL 157
Cdd:TIGR03328  79 AGAVLHTHSVEATVlsrlYPSNGGfELEGYEMLKGLP---------GITTHEdtlvvpiIEnTQDIARLADSVAPALNAY 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1942515635 158 dPIAqPGCLVRNHGPFSWGKDAAQAVYHAKVME 190
Cdd:TIGR03328 150 -PDV-PGVLIRGHGLYAWGRDWEEAKRHLEALE 180
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 10-193 1.31e-15

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 73.14  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  10 VYEANMDLPKYGLVVFTWGNASElDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGE--LNPSSDTPTHAYLYRAW 87
Cdd:PRK05874   11 VLAAAKDMLRRGLVEGTAGNISA-RRSDGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHAKdgRSPSTELNLHLACYRAF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  88 gDKVGGIVHTHSNCAVAWAQAGRSIPCYGTTQADYFYGSIPCMrgltkeeieEAYELNTGKVIAEGFEALDpiAQPGCLV 167
Cdd:PRK05874   90 -DDIGSVIHSHPVWATMFAVAHEPIPACIDEFAIYCGGDVRCT---------EYAASGTPEVGRNAVRALE--GRAAALI 157

                         170       180
                  ....*....|....*....|....*.
gi 1942515635 168 RNHGPFSWGKDAAQAVYHAKVMEETA 193
Cdd:PRK05874  158 ANHGLVAVGPRPDQVLRVTALVERTA 183
PRK08130 PRK08130
putative aldolase; Validated
 21-202 5.40e-12

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 62.97  E-value: 5.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  21 GLVVFTWGNAS-ELDreSGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGElNPSSDTPTHAYLYRAWGDkVGGIVHTHS 99
Cdd:PRK08130   21 GYTVGSAGNISaRLD--DGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHRAIYRNNPE-CGAVVHLHS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635 100 NCAVAWAqagrsipCYGTTQADyfygsiPCMRGLTKeeieeAYELNTGKV------------IAEGFEALDPIAQpGCLV 167
Cdd:PRK08130   97 THLTALS-------CLGGLDPT------NVLPPFTP-----YYVMRVGHVplipyyrpgdpaIAEALAGLAARYR-AVLL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1942515635 168 RNHGPFSWGKDAAQAVYHAKVMEETA-----LMGLRTETL 202
Cdd:PRK08130  158 ANHGPVVWGSSLEAAVNATEELEETAklillLGGRPPRYL 197
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
1-129 4.32e-10

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 57.44  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635   1 MMLKELREKVYEANMDLPKYGLVVFTWGNASEldRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELnPSSDTPTH 80
Cdd:PRK08087    1 MERNKLARQIIDTCLEMTRLGLNQGTAGNVSV--RYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKL-PSSEWRFH 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1942515635  81 AYLYRAWGDkVGGIVHTHS-NCAvAWAQAGRSIPCYGTTQADYFYGSIPC 129
Cdd:PRK08087   78 MAAYQTRPD-ANAVVHNHAvHCT-AVSILNRPIPAIHYMIAAAGGNSIPC 125
PRK08333 PRK08333
aldolase;
35-193 8.29e-09

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 53.67  E-value: 8.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  35 RESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGeLNPSSDTPTHAYLYRAWGDkVGGIVHTHSNCA-VAWAQAGRSIP 113
Cdd:PRK08333   31 RVGNLVFIKATGSVMDELTREQVAVIDLNGNQLSS-VRPSSEYRLHLAVYRNRPD-VRAIAHLHPPYSiVASTLLEEELP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635 114 CYgTTQADYFYGSIPCM--RGLTKEEIEEayelntgkVIAEGFEALDPIaqpgcLVRNHGPFSWGKDAAQAVYHAKVMEE 191
Cdd:PRK08333  109 II-TPEAELYLKKIPILpfRPAGSVELAE--------QVAEAMKEYDAV-----IMERHGIVTVGRSLREAFYKAELVEE 174


                  ..
gi 1942515635 192 TA 193
Cdd:PRK08333  175 SA 176
PRK08660 PRK08660
aldolase;
21-182 2.31e-08

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 52.27  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  21 GLVVFTWGNASELDRESglFVIKPSGVDYDELSPDKLVICDLDGkvvEGELNP--SSDTPTHAYLYRAWGDKvgGIVHTH 98
Cdd:PRK08660   16 GLVSSHFGNISVRTGDG--LLITRTGSMLDEITEGDVIEVGIDD---DGSVDPlaSSETPVHRAIYRRTSAK--AIVHAH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  99 SNCAVAWA-QAGRSIPCYGTTQadYFYGSIPCMRGLT-KEEIEEAyelntgkvIAEGFEAldpiaQPGCLVRNHGPFSWG 176
Cdd:PRK08660   89 PPYAVALSlLEDEIVPLDSEGL--YFLGTIPVVGGDIgSGELAEN--------VARALSE-----HKGVVVRGHGTFAIG 153


                  ....*.
gi 1942515635 177 KDAAQA 182
Cdd:PRK08660  154 KTLEEA 159
PRK06208 PRK06208
class II aldolase/adducin family protein;
39-180 1.43e-07

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 50.76  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  39 LFVIKPSGVDYDELSPDKLVICDLDGKVVEGE--LNPSSDTpTHAYLYRAWGDKVgGIVHTHSNCAVAWAQAGRsiPCYG 116
Cdd:PRK06208   77 HFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDrpLNRAAFA-IHSAIHEARPDVV-AAAHTHSTYGKAWSTLGR--PLDP 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635 117 TTQ-ADYFYGSipcmRGLTKEEIEEAYELNTGKVIAegfEALDPiaQPGCLVRNHGPFSWGK--DAA 180
Cdd:PRK06208  153 ITQdACAFYED----HALFDDFTGVVVDTSEGRRIA---AALGT--HKAVILQNHGLLTVGPsvDAA 210
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
26-190 1.48e-07

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 50.43  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  26 TWGNAS-ELDRESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEG-ELNPSSDTPTHAYLYRAwgDKVGGIVHTHS---N 100
Cdd:PRK06754   27 TSGNLSiKVSDDPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEEtELKPSAETLLHTHIYNN--TNAGCVLHVHTvdnN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635 101 CAVAWaqagrsipcYGTTQADYFYG-SIPCMRGLTKEE-------IEEAYELNTgkvIAEGFEALDPIAQPGCLVRNHGP 172
Cdd:PRK06754  105 VISEL---------YGDDGAVTFQGqEIIKALGIWEENaeihipiIENHADIPT---LAEEFAKHIQGDSGAVLIRNHGI 172

                         170
                  ....*....|....*...
gi 1942515635 173 FSWGKDAAQAVYHAKVME 190
Cdd:PRK06754  173 TVWGRDAFEAKKHLEAYE 190
PRK06486 PRK06486
aldolase;
37-127 2.72e-07

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 50.10  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  37 SGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSsdtPT----HAYLYRAWGdKVGGIVHTHSNCAVAWAQ-AGRS 111
Cdd:PRK06486   59 DDLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPE---ATaffiHARIHRAIP-RAKAAFHTHMPYATALSLtEGRP 134

                          90
                  ....*....|....*.
gi 1942515635 112 IPCYGTTqADYFYGSI 127
Cdd:PRK06486  135 LTTLGQT-ALKFYGRT 149
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
26-185 1.67e-06

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 47.24  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  26 TWGNAS-ELDRESGLfvIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAYLYRaWGDKVGGIVHTHSncaVA 104
Cdd:PRK09220   26 TSGNMSvRLDEQHCA--ITVSGKDKGSLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYR-LFPEIGAVLHTHS---VN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635 105 WAQAGRSIPCYGTTQADYfygsipcmrgltkeEIEEAYELNT--------------------GKVIAEGFEALDPiaQPG 164
Cdd:PRK09220  100 ATVLSRVEKSDALVLEGY--------------ELQKAFAGQTthetavvvpifdndqdiarlAARVAPYLDAQPL--RYG 163

                         170       180
                  ....*....|....*....|.
gi 1942515635 165 CLVRNHGPFSWGKDAAQAVYH 185
Cdd:PRK09220  164 YLIRGHGLYCWGRDMAEARRH 184
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 40-182 1.78e-06

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 47.54  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  40 FVIKPSGVDYDELSPDKLVICDLDGKVVEG---ELNPSSDTpTHAYLYRAWGDkVGGIVHTHS--NCAVAwAQAGRSIPc 114
Cdd:PRK07044   52 FLINPYGLLFDEITASNLVKIDLDGNVVDDspyPVNPAGFT-IHSAIHAARPD-AHCVMHTHTtaGVAVS-AQRDGLLP- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635 115 yGTTQADYFYGSIpcmrgltkeeieeAYelntgkviaEGFE--ALDP------IA----QPGCLVRNHGPFSWGKDAAQA 182
Cdd:PRK07044  128 -LSQHALQFYGRL-------------AY---------HDYEgiALDLdegerlVAdlgdKPAMLLRNHGLLTVGRTVAEA 184
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
69-182 5.11e-06

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 46.76  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  69 GELNPSSDTPTHAYLYRAWGDkvggivHTHSNCAVAWAQA--GRSI--PCYGTTqadyfYGSIPCMR-GltkeeieeaYE 143
Cdd:PRK08324  108 NAPAPSIETLLHAFLPFKHVD------HTHPDAIIAIANApdGEELtrEIFGDR-----VGWVPYVRpG---------FD 167

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1942515635 144 LntGKVIAEGFEAlDPIAQpGCLVRNHGPFSWGKDAAQA 182
Cdd:PRK08324  168 L--ALAIAEAVRA-NPGAE-GVVLGKHGLFTWGDTAKEA 202
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 36-104 1.40e-05

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 45.01  E-value: 1.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1942515635  36 ESGLFVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTPTHAYLYRAWGDkVGGIVHTHSNCAVA 104
Cdd:PRK07090   61 APGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGEGMPNPANRFHSWIYRARPD-VNCIIHTHPPHVAA 128
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
 72-182 4.25e-05

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


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 44.14  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  72 NPSSDTPTHAYLYRAWGDkvggivHTHSNCAVAWAQA--GRSI--PCYGTTqadyfYGSIPCMR-GltkeeieeaYELnt 146
Cdd:COG3347   113 APSIETLLHAFLPHKHVD------HTHPDAVIAIANApdGEELtrEIFGDR-----VGWVPYVRpG---------FDL-- 170

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1942515635 147 GKVIAEGFEAlDPIAQpGCLVRNHGPFSWGKDAAQA 182
Cdd:COG3347   171 ALALAEAFRA-NPGAE-GVVLGKHGLFTWGDTAKES 204
PRK06357 PRK06357
hypothetical protein; Provisional
 28-152 5.00e-05

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 42.84  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942515635  28 GNASE---LDRESGLFVIKP---SGVDYDELSPDKLVICDLD-GKVVEGELNPSSDTPTHAYLYRAwGDKVGGIVHTHSN 100
Cdd:PRK06357   28 GNISVrmtAEKNKEYIIMTPtlmSEAKLCDLSPYQILVVDLNtGEVIEGVGRVTREINMHEAAYVA-NPKIKCVYHSHAK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1942515635 101 CAVAWAQAGRSIPcyGTTQADYFYGSIPCMrgltkeeieeAYELNTGKVIAE 152
Cdd:PRK06357  107 ESMFWATLGLEMP--NLTEATQKLGKIPTL----------PFAPATSPELAE 146
PRK06661 PRK06661
hypothetical protein; Provisional
 40-104 1.78e-03

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 38.66  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1942515635  40 FVIKPSGVDYDELSPDKLVICDLDGKVVEGELNPSSDTP--THAYLYRAWGDkVGGIVHTHSNCAVA 104
Cdd:PRK06661   37 YYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGyfIHGSIYKTRPD-ISAIFHYHTPASIA 102
 
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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