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Conserved domains on  [gi|285812915|tpg|DAA08813|]
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TPA: methylthioribulose 1-phosphate dehydratase MDE1 [Saccharomyces cerevisiae S288C]

Protein Classification

class II aldolase/adducin head domain-containing protein; class II aldolase/adducin family protein( domain architecture ID 10087020)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations; class II aldolase/adducin family protein similar to 3-oxo-tetronate 4-phosphate decarboxylase, which catalyzes decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 14-238 2.86e-73

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: 221.86  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  14 CHPANLICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQtleylrsPKLY---KPSACT 90
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-------GKVVegkKPSSET 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  91 PLFLACYQKKN-AGAIIHTHSQNAVICSLLFGdefrianieqiKAIPSGKVDPVTKkpmalsffDTLKIPIIENMA---H 166
Cdd:cd00398   74 PLHLALYRARPdIGCIVHTHSTHATAVSQLKE-----------GLIPAGHTACAVY--------FTGDIPCTPYMTpetG 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285812915 167 EDELIDDLHKTFkdyPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMG------IPPDCGIGEEKKH 238
Cdd:cd00398  135 EDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqlppiSLELLNKEYLRKH 209
 
Name Accession Description Interval E-value
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 14-238 2.86e-73

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: 221.86  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  14 CHPANLICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQtleylrsPKLY---KPSACT 90
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-------GKVVegkKPSSET 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  91 PLFLACYQKKN-AGAIIHTHSQNAVICSLLFGdefrianieqiKAIPSGKVDPVTKkpmalsffDTLKIPIIENMA---H 166
Cdd:cd00398   74 PLHLALYRARPdIGCIVHTHSTHATAVSQLKE-----------GLIPAGHTACAVY--------FTGDIPCTPYMTpetG 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285812915 167 EDELIDDLHKTFkdyPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMG------IPPDCGIGEEKKH 238
Cdd:cd00398  135 EDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqlppiSLELLNKEYLRKH 209
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 20-223 1.45e-69

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: 211.74  E-value: 1.45e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   20 ICTLCKQFFHNNWCTGTGGGISIKDPnTNYYYLAPSGVQKEKMIPEDLFVMDAQTlEYLRSPKlyKPSACTPLFLACYQK 99
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD-EDEILITPSGVDKGRLTPEDFLVVDLQG-KPVSGGL--KPSAETLLHTQLYRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  100 KNAGAIIHTHSQNAVICSLLFGD--EFRIANIEQIKAIPSgkvdpvtkkpmALSFFDTLKIPIIENMAHEDELIDDLHKT 177
Cdd:TIGR03328  77 TGAGAVLHTHSVEATVLSRLYPSngGFELEGYEMLKGLPG-----------ITTHEDTLVVPIIENTQDIARLADSVAPA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 285812915  178 FKDYPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQ 223
Cdd:TIGR03328 146 LNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 20-219 1.59e-49

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: 160.50  E-value: 1.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915    20 ICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQtLEYLRSPKLYKPSACTPLFLACYQK 99
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLD-GNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   100 -KNAGAIIHTHSQNAVICSLLfGDEFRIANIEQIKAIPSGKVDpvtkkpmalsfFDTLKIPIIENMAHEDELIDDLHKTF 178
Cdd:smart01007  80 rPDVGAVVHTHSPYATALAAL-GKPLPLLPTEQAAAFLGGEIP-----------YAPYAGPGTELAEEGAELAEALAEAL 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 285812915   179 KDYPdtcAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAI 219
Cdd:smart01007 148 PDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 18-219 3.28e-48

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: 156.94  E-value: 3.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   18 NLICTLCKQFFHNNWCTGTGGGISIKDPnTNYYYLAPSGVQKEKMIPEDLFVMDAQTlEYLRSPklYKPSACTPLFLACY 97
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP-GDGFLITPSGVDFGELTPEDLVVVDLDG-NVVEGG--LKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   98 QK-KNAGAIIHTHSQNAVICSLLfgdefrianieqIKAIPsgkvdPVTkkPMALSFFdTLKIPIIENMAHEDELI-DDLH 175
Cdd:pfam00596  77 RArPDAGAVVHTHSPYATALSLA------------KEGLP-----PIT--QEAADFL-GGDIPIIPYYTPGTEELgERIA 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 285812915  176 KTFKDypDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAI 219
Cdd:pfam00596 137 EALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 20-227 6.04e-35

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: 123.79  E-value: 6.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  20 ICTLCKQFFHNNWCTGTGGGISIKDPNtNYYYLAPSGVQKEKMIPEDLFVMDAQtLEYLRSPklYKPSACTPLFLACYQK 99
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGD--LKPSSETPLHLAIYRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 100 -KNAGAIIHTHSQNAVICSLLfGDEFRIanIEQikaipsgkvdpvtkkPMALSFFDtlKIPIIENM-AHEDELIDDLHKT 177
Cdd:COG0235   86 rPDVGAVVHTHSPYATALSAL-GEPLPP--LEQ---------------TEAAAFLG--DVPVVPYAgPGTEELAEAIAEA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 285812915 178 FKDYPdtcAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMGIP 227
Cdd:COG0235  146 LGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
25-228 1.95e-29

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 109.37  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  25 KQFFHNNWCTGTGGGISIK---DPNTnyYYLAPSGVQKEKMIPEDLFVMDAQTLEYLRSPklYKPSACTPLFLACYQKKN 101
Cdd:PRK06754  16 KELAARDWFPATSGNLSIKvsdDPLT--FLVTASGKDKRKTTPEDFLLVDHDGKPVEETE--LKPSAETLLHTHIYNNTN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 102 AGAIIHTHSQNAVICSLLFGD--EFRIANIEQIKAIPSGKVDPvtkkpmalsffdTLKIPIIENMAHedelIDDLHKTFK 179
Cdd:PRK06754  92 AGCVLHVHTVDNNVISELYGDdgAVTFQGQEIIKALGIWEENA------------EIHIPIIENHAD----IPTLAEEFA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 285812915 180 DY--PDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKM--YQMGIPP 228
Cdd:PRK06754 156 KHiqGDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLlsIQGGVSK 208
 
Name Accession Description Interval E-value
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 14-238 2.86e-73

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: 221.86  E-value: 2.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  14 CHPANLICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQtleylrsPKLY---KPSACT 90
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYFLITPSGVDYEEMTASDLVVVDAQ-------GKVVegkKPSSET 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  91 PLFLACYQKKN-AGAIIHTHSQNAVICSLLFGdefrianieqiKAIPSGKVDPVTKkpmalsffDTLKIPIIENMA---H 166
Cdd:cd00398   74 PLHLALYRARPdIGCIVHTHSTHATAVSQLKE-----------GLIPAGHTACAVY--------FTGDIPCTPYMTpetG 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285812915 167 EDELIDDLHKTFkdyPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMG------IPPDCGIGEEKKH 238
Cdd:cd00398  135 EDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqlppiSLELLNKEYLRKH 209
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 20-223 1.45e-69

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: 211.74  E-value: 1.45e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   20 ICTLCKQFFHNNWCTGTGGGISIKDPnTNYYYLAPSGVQKEKMIPEDLFVMDAQTlEYLRSPKlyKPSACTPLFLACYQK 99
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLD-EDEILITPSGVDKGRLTPEDFLVVDLQG-KPVSGGL--KPSAETLLHTQLYRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  100 KNAGAIIHTHSQNAVICSLLFGD--EFRIANIEQIKAIPSgkvdpvtkkpmALSFFDTLKIPIIENMAHEDELIDDLHKT 177
Cdd:TIGR03328  77 TGAGAVLHTHSVEATVLSRLYPSngGFELEGYEMLKGLPG-----------ITTHEDTLVVPIIENTQDIARLADSVAPA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 285812915  178 FKDYPDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQ 223
Cdd:TIGR03328 146 LNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 20-219 1.59e-49

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: 160.50  E-value: 1.59e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915    20 ICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQtLEYLRSPKLYKPSACTPLFLACYQK 99
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEDLFLITPSGVDFGELTASDLVVVDLD-GNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   100 -KNAGAIIHTHSQNAVICSLLfGDEFRIANIEQIKAIPSGKVDpvtkkpmalsfFDTLKIPIIENMAHEDELIDDLHKTF 178
Cdd:smart01007  80 rPDVGAVVHTHSPYATALAAL-GKPLPLLPTEQAAAFLGGEIP-----------YAPYAGPGTELAEEGAELAEALAEAL 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 285812915   179 KDYPdtcAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAI 219
Cdd:smart01007 148 PDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 18-219 3.28e-48

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: 156.94  E-value: 3.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   18 NLICTLCKQFFHNNWCTGTGGGISIKDPnTNYYYLAPSGVQKEKMIPEDLFVMDAQTlEYLRSPklYKPSACTPLFLACY 97
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP-GDGFLITPSGVDFGELTPEDLVVVDLDG-NVVEGG--LKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915   98 QK-KNAGAIIHTHSQNAVICSLLfgdefrianieqIKAIPsgkvdPVTkkPMALSFFdTLKIPIIENMAHEDELI-DDLH 175
Cdd:pfam00596  77 RArPDAGAVVHTHSPYATALSLA------------KEGLP-----PIT--QEAADFL-GGDIPIIPYYTPGTEELgERIA 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 285812915  176 KTFKDypDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAI 219
Cdd:pfam00596 137 EALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 20-227 6.04e-35

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: 123.79  E-value: 6.04e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  20 ICTLCKQFFHNNWCTGTGGGISIKDPNtNYYYLAPSGVQKEKMIPEDLFVMDAQtLEYLRSPklYKPSACTPLFLACYQK 99
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRLDD-DRFLITPSGVDFGELTPEDLVVVDLD-GNVVEGD--LKPSSETPLHLAIYRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 100 -KNAGAIIHTHSQNAVICSLLfGDEFRIanIEQikaipsgkvdpvtkkPMALSFFDtlKIPIIENM-AHEDELIDDLHKT 177
Cdd:COG0235   86 rPDVGAVVHTHSPYATALSAL-GEPLPP--LEQ---------------TEAAAFLG--DVPVVPYAgPGTEELAEAIAEA 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 285812915 178 FKDYPdtcAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQMGIP 227
Cdd:COG0235  146 LGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
25-228 1.95e-29

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 109.37  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  25 KQFFHNNWCTGTGGGISIK---DPNTnyYYLAPSGVQKEKMIPEDLFVMDAQTLEYLRSPklYKPSACTPLFLACYQKKN 101
Cdd:PRK06754  16 KELAARDWFPATSGNLSIKvsdDPLT--FLVTASGKDKRKTTPEDFLLVDHDGKPVEETE--LKPSAETLLHTHIYNNTN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 102 AGAIIHTHSQNAVICSLLFGD--EFRIANIEQIKAIPSGKVDPvtkkpmalsffdTLKIPIIENMAHedelIDDLHKTFK 179
Cdd:PRK06754  92 AGCVLHVHTVDNNVISELYGDdgAVTFQGQEIIKALGIWEENA------------EIHIPIIENHAD----IPTLAEEFA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 285812915 180 DY--PDTCAVIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKM--YQMGIPP 228
Cdd:PRK06754 156 KHiqGDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLlsIQGGVSK 208
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
32-224 1.62e-15

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 72.66  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  32 WCTGTGGGISIKDPNTnYYYLAPSGVQKEKMIPEDLFVMDAQTlEYLRSPKlyKPSACTPLFLACYQKKN-AGAIIHTHS 110
Cdd:PRK09220  22 WVPATSGNMSVRLDEQ-HCAITVSGKDKGSLTAEDFLQVDIAG-NAVPSGR--KPSAETLLHTQLYRLFPeIGAVLHTHS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 111 QNAVICSLLF-GDEFRIANIEQIKAIPSGKvdpvtkkpmalSFFDTLKIPIIEN---MAHEDELIDDLHKTFkdyPDTCA 186
Cdd:PRK09220  98 VNATVLSRVEkSDALVLEGYELQKAFAGQT-----------THETAVVVPIFDNdqdIARLAARVAPYLDAQ---PLRYG 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 285812915 187 VIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKMYQM 224
Cdd:PRK09220 164 YLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLL 201
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
34-204 1.71e-11

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 61.77  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  34 TGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFV--MDAQTLEylrspKLYKPSACTPLFLACYQK-KNAGAIIHTHS 110
Cdd:PRK08193  23 TFTWGNVSAIDRERGLFVIKPSGVDYDKMTAEDMVVvdLEGNVVE-----GKLKPSSDTPTHLVLYKAfPEIGGIVHTHS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 111 QNAVIcsllfgdeFRIANieqiKAIPS----------GKVdPVTkKPMAlsffdtlKIPIIENMAHE--DELIDDLHKTF 178
Cdd:PRK08193  98 RHATA--------WAQAG----RDIPAlgtthadyfyGDI-PCT-RKMT-------DEEINGEYEWEtgKVIVETFEKRG 156

                        170       180
                 ....*....|....*....|....*.
gi 285812915 179 KDYPDTCAVIVRRHGIFVWGPTIDKA 204
Cdd:PRK08193 157 IDPAAVPGVLVHSHGPFTWGKDAEDA 182
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 34-204 4.56e-11

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 60.60  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  34 TGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQTLEYLRSPKlyKPSACTPLFLACYQK-KNAGAIIHTHSQN 112
Cdd:PRK12347  23 TFTWGNVSAVDETRQLMVIKPSGVEYDVMTADDMVVVEIASGKVVEGSK--KPSSDTPTHLALYRRyPEIGGIVHTHSRH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 113 AVICSllfgdefrianieqikaiPSGKVDPVTKKPMALSFFDTlkIPIIENM-----AHEDEL------IDDLHKTFKDY 181
Cdd:PRK12347 101 ATIWS------------------QAGLDLPAWGTTHADYFYGA--IPCTRLMtaeeiNGEYEYqtgeviIETFEERGISP 160

                        170       180
                 ....*....|....*....|...
gi 285812915 182 PDTCAVIVRRHGIFVWGPTIDKA 204
Cdd:PRK12347 161 AQIPAVLVHSHGPFAWGKNAADA 183
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 34-229 4.11e-10

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 57.89  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  34 TGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFV--MDAQTLEylrspKLYKPSACTPLFLACYQK-KNAGAIIHTHS 110
Cdd:PRK12348  22 TFTWGNVSAIDRERGLVVIKPSGVAYETMKADDMVVvdMSGKVVE-----GEYRPSSDTATHLELYRRyPSLGGIVHTHS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 111 QNAV--------ICSL-------LFGDefrianIEQIKAIPSGKVDPVTKKpmalsffDTLKIpIIENMAHedelIDDLH 175
Cdd:PRK12348  97 THATawaqaglaIPALgtthadyFFGD------IPCTRGLSEEEVQGEYEL-------NTGKV-IIETLGN----AEPLH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 285812915 176 ktfkdypdTCAVIVRRHGIFVWGPTIDKAkIFNEAIdylMELAIKM--YQMGIPPD 229
Cdd:PRK12348 159 --------TPGIVVYQHGPFAWGKDAHDA-VHNAVV---MEEVAKMawIARGINPQ 202
PRK08660 PRK08660
aldolase;
90-213 8.05e-10

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 56.50  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  90 TPLFLACYQKKNAGAIIHTHSQNAVICSLLfgdefrianIEQIKAIPS-GKVdpvtkkpmalsFFDTlkIPIIENMAHED 168
Cdd:PRK08660  69 TPVHRAIYRRTSAKAIVHAHPPYAVALSLL---------EDEIVPLDSeGLY-----------FLGT--IPVVGGDIGSG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 285812915 169 ELIDDLHKTFKDYPdtcAVIVRRHGIFVWGPTIDKAKIFNEAIDY 213
Cdd:PRK08660 127 ELAENVARALSEHK---GVVVRGHGTFAIGKTLEEAYIYTSQLEH 168
PRK06755 PRK06755
hypothetical protein; Validated
 31-221 2.32e-09

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 55.42  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  31 NWCTGTGGGISI---KDPNTnyYYLAPSGVQKEKMIPEDLFVMDAQTLEYLRSPKlyKPSACTPLFLACYQKKNAGAIIH 107
Cdd:PRK06755  22 DWFYGTKISLSLctsKEPLT--FLVNVEGRDKGLFSEEDFIVVNCMCEPVFENEE--KPAAESFMHADIYKKSSAECILQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 108 THSQNAVICSLLFGDEFRIAnieqikaIPSGKVDPVTKKpmalSFFDTLKIPIIENmahEDELIDDLHKTFKDYP-DTCA 186
Cdd:PRK06755  98 VQTVDSHLISELYGEEGEVT-------FDKRSVERVFGK----EGITEMTIPIVED---EKKFADLLENNVPNFIeGGGV 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 285812915 187 VIVRRHGIFVWGPTIDKAKIFNEAIDYLMELAIKM 221
Cdd:PRK06755 164 VLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 19-229 4.84e-08

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 51.93  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  19 LICTLCKQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDaqtLEYLRSPKLYKPSACTPLFLACYQ 98
Cdd:PRK06557  14 EVCKLHLELPKYGLVVWTSGNVSARDPGTDLVVIKPSGVSYDDLTPEDMVVVD---LDGNVVEGDLKPSSDTASHLYVYR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  99 KKN-AGAIIHTHSQNA---------VICSL-LFGDEFrianieqikaipsGKVDPVTkkPMALSFFDTLKIPIIENMAhe 167
Cdd:PRK06557  91 HMPdVGGVVHTHSTYAtawaargepIPCVLtAMADEF-------------GGPIPVG--PFALIGDEAIGKGIVETLK-- 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285812915 168 deliddlhktfkdYPDTCAVIVRRHGIFVWGPTID---KAKIFNEAIDYLMELAIkmyQMG----IPPD 229
Cdd:PRK06557 154 -------------GGRSPAVLMQNHGVFTIGKDAEdavKAAVMVEEVARTVHIAR---QLGepipIPQE 206
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
25-119 9.91e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 48.21  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  25 KQFFHNNWCTGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMD--AQTLEYLRspklyKPSACTPLFLACYQ-KKN 101
Cdd:PRK06833  15 KKLISSGLTKGTGGNISIFNREQGLMAITPSGIDYFEIKPEDIVIMDldGKVVEGER-----KPSSELDMHLIFYRnRED 89

                         90
                 ....*....|....*...
gi 285812915 102 AGAIIHTHSQNAVICSLL 119
Cdd:PRK06833  90 INAIVHTHSPYATTLACL 107
PRK08130 PRK08130
putative aldolase; Validated
 20-204 1.94e-06

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 47.18  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  20 ICTLCKQFFHNNWCTGTGGGISIKDPNTNYyyLA-PSGVQKEKMIPEDLFVMDAQTlEYLRSPKlykPSACTPLFLACYQ 98
Cdd:PRK08130  10 IVRLGRSLFQRGYTVGSAGNISARLDDGGW--LVtPTGSCLGRLDPARLSKVDADG-NWLSGDK---PSKEVPLHRAIYR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  99 KK-NAGAIIHTHSQNAVICSLLfgdefriANIEQIKAIPsgkvdPVTkkP---MALSffdtlKIPIIENMAHEDELI-DD 173
Cdd:PRK08130  84 NNpECGAVVHLHSTHLTALSCL-------GGLDPTNVLP-----PFT--PyyvMRVG-----HVPLIPYYRPGDPAIaEA 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 285812915 174 LHKTFKDYPdtcAVIVRRHGIFVWGPTIDKA 204
Cdd:PRK08130 145 LAGLAARYR---AVLLANHGPVVWGSSLEAA 172
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 36-229 4.67e-05

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 43.28  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  36 TGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFV--MDAQTLEylrspKLYKPSACTPLFLACYQK-KNAGAIIHTHSQN 112
Cdd:PRK13145  26 TWGNVSEVCRELGRIVIKPSGVDYDELTPENMVVtdLDGNVVE-----GDLNPSSDLPTHVELYKAwPEVGGIVHTHSTE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 113 AVICSllfgdefrianieqikaiPSGKVDPVTKKPMALSFFDTlkIPIIE-------NMAHEDE----LIDDLHKTFKDY 181
Cdd:PRK13145 101 AVGWA------------------QAGRDIPFYGTTHADYFYGP--IPCARsltkdevNGAYEKEtgsvIIEEFEKRGLDP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 285812915 182 PDTCAVIVRRHGIFVWGPTIDKAkIFNEAIdylMELAIKM--YQMGIPPD 229
Cdd:PRK13145 161 MAVPGIVVRNHGPFTWGKNPEQA-VYHSVV---LEEVAKMnrLTEQINPR 206
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 34-239 4.92e-05

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 43.18  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  34 TGTGGGISIKDPNTNYYYLAPSGVQKEKMIPEDLFVMDAQTLEYLRSPKlyKPSACTPLFLACYQK-KNAGAIIHTHSQN 112
Cdd:PRK13213  23 TFTWGNVSGIDREHGLVVIKPSGVEYDVMSVNDMVVVDLATGKVVEGDK--KPSSDTDTHLVLYRAfAEIGGIVHTHSRH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915 113 AVICSllfgdefrianieqikaiPSGKVDPVTKKPMALSFFDtlKIPIIENMAHEDELIDDLHKTFK-----------DY 181
Cdd:PRK13213 101 ATIWA------------------QAGKSLSALGTTHADYFYG--PIPCTRLMTEAEITGDYEHETGKvivetfaeqglRA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 285812915 182 PDTCAVIVRRHGIFVWGPTIDKAkIFNEAIdyLMELA-IKMYQMGIPPdcGIGEEKKHL 239
Cdd:PRK13213 161 ADIPAVLVNGHGPFAWGSNAANA-VHNAVV--LEEIAyMNLFTHQLTP--GVGDMQQTL 214
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
173-216 2.42e-03

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 38.67  E-value: 2.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 285812915 173 DLHKTFKDYPDTCAVIVRRHGIFVWGPTIDKA-----KIFNEAIDYLME 216
Cdd:PRK08324 171 AIAEAVRANPGAEGVVLGKHGLFTWGDTAKEAyertiEIITRAEEYIEA 219
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
35-119 4.23e-03

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 37.41  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285812915  35 GTGGGISIKdpNTNYYYLAPSGVQKEKMIPEDLFVMDAQTLEylRSPKLykPSACTPLFLACYQKK-NAGAIIHTHSQNA 113
Cdd:PRK08087  25 GTAGNVSVR--YQDGMLITPTGIPYEKLTESHIVFVDGNGKH--EEGKL--PSSEWRFHMAAYQTRpDANAVVHNHAVHC 98


                 ....*.
gi 285812915 114 VICSLL 119
Cdd:PRK08087  99 TAVSIL 104
 
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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