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Conserved domains on  [gi|258613873|ref|NP_062709|]
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methylthioribulose-1-phosphate dehydratase isoform 1 [Mus musculus]

Protein Classification

methylthioribulose-1-phosphate dehydratase( domain architecture ID 10022368)

methylthioribulose-1-phosphate dehydratase catalyzes the formation of diketo methylthiopentyl phosphate from methylribulose phosphate in the methionine salvage pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 27-225 1.33e-99

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: 288.01  E-value: 1.33e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   27 IPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAYT 105
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  106 MRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYP 184
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 258613873  185 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 225
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 27-225 1.33e-99

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: 288.01  E-value: 1.33e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   27 IPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAYT 105
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  106 MRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYP 184
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 258613873  185 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 225
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 27-221 8.96e-51

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: 163.49  E-value: 8.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   27 IPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPPaskklKKSQCTPLFMNAYT 105
Cdd:pfam00596   3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  106 MR-GAGAVIHTHSKAAVMATLLFPGqeFKITHQEMIKgirkctsggyYRYDDmlvVPIIEN-TPEEKDLKERMAHAMNEy 183
Cdd:pfam00596  78 ARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 258613873  184 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 221
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 27-221 2.97e-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: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 157.03  E-value: 2.97e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873    27 IPELCKQFYHLGWVTGTGGGISLKHGNE--IYIAPSGVQKERIQPEDMFVCDINEQDISGPPAskkLKKSQCTPLFMNAY 104
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   105 TMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMIKGIrkctSGGYYRYDDmLVVPIIENTPEEKDLKERMAHAMNEY 183
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 258613873   184 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 221
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 21-234 1.48e-33

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: 119.93  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  21 EHPRFLIPELCKQFYHLGWVTGTGGGISLKH-GNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPpaskkLKKSQCTPL 99
Cdd:COG0235    4 EELREELAAAGRRLARRGLVDGTAGNISVRLdDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD-----LKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 100 FMNAYTMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMikgirkctsgGYYRYDDmlvVPIIE-NTPEEKDLKERMA 177
Cdd:COG0235   79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 258613873 178 HAMNEYPdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMGlDPTQLP 234
Cdd:COG0235  144 EALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 21-237 1.65e-32

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: 117.47  E-value: 1.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  21 EHPRFLIPELCKQFYHLGWVTGTGGGIS--LKHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPpaskklKKSQCTP 98
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSarDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK------KPSSETP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  99 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGQ--EFKITHqemikgirkctsgGYYRYDDmlvVPIIENTPEEKDLKER 175
Cdd:cd00398   75 LHLALYRARpDIGCIVHTHSTHATAVSQLKEGLipAGHTAC-------------AVYFTGD---IPCTPYMTPETGEDEI 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258613873 176 MAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMG-----LDPTQLPVGE 237
Cdd:cd00398  139 GTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqlppISLELLNKEY 205
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
29-217 9.77e-28

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 105.13  E-value: 9.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  29 ELCKQFYHLGWVTGTGGGISLKHGNE---IYIAPSGVQKERIQPED-MFVcdineqDISGPPASK-KLKKSQCTPLFMNA 103
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDfLLV------DHDGKPVEEtELKPSAETLLHTHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 104 YTMRGAGAVIHTHSKAA-VMATLLFPGQEFKITHQEMIKGIrkctsgGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNe 182
Cdd:PRK06754  87 YNNTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ- 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 258613873 183 yPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 217
Cdd:PRK06754 160 -GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 27-225 1.33e-99

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: 288.01  E-value: 1.33e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   27 IPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAYT 105
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  106 MRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYP 184
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 258613873  185 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 225
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 27-221 8.96e-51

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: 163.49  E-value: 8.96e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   27 IPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPPaskklKKSQCTPLFMNAYT 105
Cdd:pfam00596   3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  106 MR-GAGAVIHTHSKAAVMATLLFPGqeFKITHQEMIKgirkctsggyYRYDDmlvVPIIEN-TPEEKDLKERMAHAMNEy 183
Cdd:pfam00596  78 ARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 258613873  184 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 221
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 27-221 2.97e-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: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 157.03  E-value: 2.97e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873    27 IPELCKQFYHLGWVTGTGGGISLKHGNE--IYIAPSGVQKERIQPEDMFVCDINEQDISGPPAskkLKKSQCTPLFMNAY 104
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873   105 TMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMIKGIrkctSGGYYRYDDmLVVPIIENTPEEKDLKERMAHAMNEY 183
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 258613873   184 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 221
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 21-234 1.48e-33

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: 119.93  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  21 EHPRFLIPELCKQFYHLGWVTGTGGGISLKH-GNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPpaskkLKKSQCTPL 99
Cdd:COG0235    4 EELREELAAAGRRLARRGLVDGTAGNISVRLdDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD-----LKPSSETPL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 100 FMNAYTMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMikgirkctsgGYYRYDDmlvVPIIE-NTPEEKDLKERMA 177
Cdd:COG0235   79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIA 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 258613873 178 HAMNEYPdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMGlDPTQLP 234
Cdd:COG0235  144 EALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 21-237 1.65e-32

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: 117.47  E-value: 1.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  21 EHPRFLIPELCKQFYHLGWVTGTGGGIS--LKHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPpaskklKKSQCTP 98
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSarDRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGK------KPSSETP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  99 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGQ--EFKITHqemikgirkctsgGYYRYDDmlvVPIIENTPEEKDLKER 175
Cdd:cd00398   75 LHLALYRARpDIGCIVHTHSTHATAVSQLKEGLipAGHTAC-------------AVYFTGD---IPCTPYMTPETGEDEI 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258613873 176 MAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMG-----LDPTQLPVGE 237
Cdd:cd00398  139 GTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqlppISLELLNKEY 205
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
29-217 9.77e-28

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 105.13  E-value: 9.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  29 ELCKQFYHLGWVTGTGGGISLKHGNE---IYIAPSGVQKERIQPED-MFVcdineqDISGPPASK-KLKKSQCTPLFMNA 103
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDfLLV------DHDGKPVEEtELKPSAETLLHTHI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 104 YTMRGAGAVIHTHSKAA-VMATLLFPGQEFKITHQEMIKGIrkctsgGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNe 182
Cdd:PRK06754  87 YNNTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ- 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 258613873 183 yPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 217
Cdd:PRK06754 160 -GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
26-226 7.40e-21

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 86.91  E-value: 7.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  26 LIPELCKQFYHLGWVTGTGGGISLKHG-NEIYIAPSGVQKERIQPEDmfvcdINEQDISGPPASKKLKKSQCTPLFMNAY 104
Cdd:PRK09220   9 QLIAAGRWIGARGWVPATSGNMSVRLDeQHCAITVSGKDKGSLTAED-----FLQVDIAGNAVPSGRKPSAETLLHTQLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 105 TMR-GAGAVIHTHSKAAVMATLLFPGQEFKITHQEMIKgirkcTSGGYYRYDDMLVVPIIENTPEEKDLKERMAHAMNEY 183
Cdd:PRK09220  84 RLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQK-----AFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQ 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 258613873 184 PDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKM 226
Cdd:PRK09220 159 PLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLL 201
PRK08130 PRK08130
putative aldolase; Validated
 24-206 2.34e-10

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 58.35  E-value: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  24 RFLIPELCKQFYHLGWVTGTGGGISLK-HGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPPASKKLkksqctPLFMN 102
Cdd:PRK08130   7 REEIVRLGRSLFQRGYTVGSAGNISARlDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEV------PLHRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 103 AYTMRG-AGAVIHTHSKAAVMATLLfPGqefkITHQEMIKGIrkcTSggYY--RYDDMLVVPIIEntPEEKDLKERMAHA 179
Cdd:PRK08130  81 IYRNNPeCGAVVHLHSTHLTALSCL-GG----LDPTNVLPPF---TP--YYvmRVGHVPLIPYYR--PGDPAIAEALAGL 148

                        170       180
                 ....*....|....*....|....*..
gi 258613873 180 MNEYPdscAVLVRRHGVYVWGETWEKA 206
Cdd:PRK08130 149 AARYR---AVLLANHGPVVWGSSLEAA 172
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 38-237 9.55e-09

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 53.86  E-value: 9.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  38 GWVTGTGGGIS--LKHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAYT-MRGAGAVIH 114
Cdd:PRK06557  26 GLVVWTSGNVSarDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEG-----DLKPSSDTASHLYVYRhMPDVGGVVH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 115 THSK-AAVMATLlfpGQEFKIThqemikgirkCTS-----GGyyryddmlVVPIienTPEEKDLKERMAHAMNEY---PD 185
Cdd:PRK06557 101 THSTyATAWAAR---GEPIPCV----------LTAmadefGG--------PIPV---GPFALIGDEAIGKGIVETlkgGR 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 258613873 186 SCAVLVRRHGVYVWGETWE---KAKTMCEcydylfDIAVSM---KKMGlDPTQLPVGE 237
Cdd:PRK06557 157 SPAVLMQNHGVFTIGKDAEdavKAAVMVE------EVARTVhiaRQLG-EPIPIPQEE 207
PRK08660 PRK08660
aldolase;
38-206 7.43e-08

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 50.73  E-value: 7.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  38 GWVTGTGGGISLKHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGPPASKKlkksqcTPLFMNAYTMRGAGAVIHTHS 117
Cdd:PRK08660  16 GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLASSE------TPVHRAIYRRTSAKAIVHAHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 118 KAAVMATLLfpgqefkithQEMIKGIrkCTSGGYYryddMLVVPIIENTPEEKDLKERMAHAMNEYPdscAVLVRRHGVY 197
Cdd:PRK08660  90 PYAVALSLL----------EDEIVPL--DSEGLYF----LGTIPVVGGDIGSGELAENVARALSEHK---GVVVRGHGTF 150


                 ....*....
gi 258613873 198 VWGETWEKA 206
Cdd:PRK08660 151 AIGKTLEEA 159
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 35-200 2.75e-07

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 49.82  E-value: 2.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  35 YHLgwVTGTGGGISL--KHGNEIYIAPSGVQKERIQPEDMFVCDIneqdISGPPASKKLKKSQCTPLFMNAY-TMRGAGA 111
Cdd:PRK12347  19 HHL--VTFTWGNVSAvdETRQLMVIKPSGVEYDVMTADDMVVVEI----ASGKVVEGSKKPSSDTPTHLALYrRYPEIGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 112 VIHTHSKAAVM---ATLLFPgqEFKITHQEMIKGIRKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLKERmahamn 181
Cdd:PRK12347  93 IVHTHSRHATIwsqAGLDLP--AWGTTHADYFYGAIPCTRlmtaeeiNGEYEYQTGEV--IIE-TFEERGISPA------ 161

                        170
                 ....*....|....*....
gi 258613873 182 eypDSCAVLVRRHGVYVWG 200
Cdd:PRK12347 162 ---QIPAVLVHSHGPFAWG 177
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 38-201 3.26e-07

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 49.41  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  38 GWVTGTGGGISL--KHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAY-TMRGAGAVIH 114
Cdd:PRK12348  19 GLVTFTWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEG-----EYRPSSDTATHLELYrRYPSLGGIVH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 115 THSKAAV---MATLLFPGqeFKITHQEMIKGIRKCTSG-------GYYRYDDMLVvpIIENTPEEKDLkermahamnEYP 184
Cdd:PRK12348  94 THSTHATawaQAGLAIPA--LGTTHADYFFGDIPCTRGlseeevqGEYELNTGKV--IIETLGNAEPL---------HTP 160

                        170
                 ....*....|....*..
gi 258613873 185 dscAVLVRRHGVYVWGE 201
Cdd:PRK12348 161 ---GIVVYQHGPFAWGK 174
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 26-206 1.04e-06

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 48.29  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  26 LIPELCKQFYHL-------GWVTGTGGGISL--KHGNEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQC 96
Cdd:PRK13145   2 NLQEMRERVCAAnkslpkhGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEG-----DLNPSSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  97 TPLFMNAYTMRG-AGAVIHTHSKAAV---MATLLFPGqeFKITHQEMIKG----IRKCTSG---GYYRYDDMLVvpIIEN 165
Cdd:PRK13145  77 LPTHVELYKAWPeVGGIVHTHSTEAVgwaQAGRDIPF--YGTTHADYFYGpipcARSLTKDevnGAYEKETGSV--IIEE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 258613873 166 TpEEKDLkERMAHAmneypdscAVLVRRHGVYVWGETWEKA 206
Cdd:PRK13145 153 F-EKRGL-DPMAVP--------GIVVRNHGPFTWGKNPEQA 183
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
33-206 1.37e-06

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 47.91  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  33 QFYHLGWVTGTGG---GISLKHGnEIYIAPSGVQKERIQPEDMFVCDINEQDISGppaskKLKKSQCTPLFMNAY-TMRG 108
Cdd:PRK08193  15 ALPKHGLVTFTWGnvsAIDRERG-LFVIKPSGVDYDKMTAEDMVVVDLEGNVVEG-----KLKPSSDTPTHLVLYkAFPE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 109 AGAVIHTHSKAAVM---ATLLFPGqeFKITHQEMIKGIRKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLkermah 178
Cdd:PRK08193  89 IGGIVHTHSRHATAwaqAGRDIPA--LGTTHADYFYGDIPCTRkmtdeeiNGEYEWETGKV--IVE-TFEKRGI------ 157

                        170       180
                 ....*....|....*....|....*...
gi 258613873 179 amnEYPDSCAVLVRRHGVYVWGETWEKA 206
Cdd:PRK08193 158 ---DPAAVPGVLVHSHGPFTWGKDAEDA 182
PRK06755 PRK06755
hypothetical protein; Validated
 158-223 4.63e-05

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 43.10  E-value: 4.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258613873 158 LVVPIIENTPEEKDLKERMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSM 223
Cdd:PRK06755 135 MTIPIVEDEKKFADLLENNVPNFIE--GGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
21-237 8.17e-05

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 42.43  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  21 EHPRFLIPELCKQFYHLGWVTGTGGGISLKHGNEIYIA--PSGVQKERIQPEDMFVCDINEQDISGP--PASkklkKSQC 96
Cdd:PRK06833   4 QKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAitPSGIDYFEIKPEDIVIMDLDGKVVEGErkPSS----ELDM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  97 TPLFmnaYTMR-GAGAVIHTHSK-AAVMATLlfpGQEFKITHQeMI----KGIRkCTSggYYRYDdmlvvpiientpeEK 170
Cdd:PRK06833  80 HLIF---YRNReDINAIVHTHSPyATTLACL---GWELPAVHY-LIavagPNVR-CAE--YATFG-------------TK 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258613873 171 DLKERMAHAMNeypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMGlDPTQLPVGE 237
Cdd:PRK06833 137 ELAENAFEAME---DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIYYQTKSIG-EPKLLPEDE 199
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
27-206 1.52e-04

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 41.65  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  27 IPELCKQFYHLGWVTGTGGGISLKHGNEIYIAPSGVQKERIQPEDMFVCDINeqdisGPPASKKLKKSQCtpLF-MNAYT 105
Cdd:PRK08087  10 IIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGN-----GKHEEGKLPSSEW--RFhMAAYQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 106 MR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQeMIkgirkCTSGGyyryDDMLVVPIIenTPEEKDLKERMAHAMNEyp 184
Cdd:PRK08087  83 TRpDANAVVHNHAVHCTAVSIL--NRPIPAIHY-MI-----AAAGG----NSIPCAPYA--TFGTRELSEHVALALKN-- 146

                        170       180
                 ....*....|....*....|..
gi 258613873 185 dSCAVLVRRHGVYVWGETWEKA 206
Cdd:PRK08087 147 -RKATLLQHHGLIACEVNLEKA 167
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 42-206 1.29e-03

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 38.94  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873  42 GTGGGISLKHGnEIYIAPSGVQKERIQPEDMFVCDIneqdISGPPASKKLKKSQCTPLFMNAY-TMRGAGAVIHTHSK-A 119
Cdd:PRK13213  27 GNVSGIDREHG-LVVIKPSGVEYDVMSVNDMVVVDL----ATGKVVEGDKKPSSDTDTHLVLYrAFAEIGGIVHTHSRhA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258613873 120 AVMATLLFPGQEFKITHQEMIKGIRKCTS-------GGYYRYDdmlVVPIIENTPEEKDLKErmahamneyPDSCAVLVR 192
Cdd:PRK13213 102 TIWAQAGKSLSALGTTHADYFYGPIPCTRlmteaeiTGDYEHE---TGKVIVETFAEQGLRA---------ADIPAVLVN 169

                        170
                 ....*....|....
gi 258613873 193 RHGVYVWGETWEKA 206
Cdd:PRK13213 170 GHGPFAWGSNAANA 183
 
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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