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Conserved domains on  [gi|447198629|ref|WP_001275885|]
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MULTISPECIES: 2-methylcitrate dehydratase [Escherichia]

Protein Classification

MmgE/PrpD family protein( domain architecture ID 10013227)

MmgE/PrpD family protein such as 2-methylcitrate dehydratase (PrpD), which catalyzes the stereospecific dehydration of (2S,3S)-2-methylcitrate to yield the cis isomer of 2-methyl-aconitate and could also catalyze the dehydration of citrate and the hydration of cis-aconitate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
1-483 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


:

Pssm-ID: 181845  Cd Length: 480  Bit Score: 1064.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   1 MSAQINNIRPEFDREIVDIVDYVMNYEISSRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQ 80
Cdd:PRK09425   1 MSAVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAIASGKAPLTMKQVLTGMIKAHEIQGCIAL 160
Cdd:PRK09425  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 161 ENSFNRVGLDHVLLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAK 240
Cdd:PRK09425 161 ENSFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 241 TGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAgktAADIEKV 320
Cdd:PRK09425 241 TGEMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKAR---LDDIERI 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 321 TIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEK 400
Cdd:PRK09425 318 TIRTHESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 401 RAIANAITLEFTDGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRTRLEQMPVNEYLDL 480
Cdd:PRK09425 398 RSIANAVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDL 477


                 ...
gi 447198629 481 YVI 483
Cdd:PRK09425 478 FVI 480
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
1-483 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1064.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   1 MSAQINNIRPEFDREIVDIVDYVMNYEISSRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQ 80
Cdd:PRK09425   1 MSAVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAIASGKAPLTMKQVLTGMIKAHEIQGCIAL 160
Cdd:PRK09425  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 161 ENSFNRVGLDHVLLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAK 240
Cdd:PRK09425 161 ENSFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 241 TGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAgktAADIEKV 320
Cdd:PRK09425 241 TGEMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKAR---LDDIERI 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 321 TIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEK 400
Cdd:PRK09425 318 TIRTHESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 401 RAIANAITLEFTDGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRTRLEQMPVNEYLDL 480
Cdd:PRK09425 398 RSIANAVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDL 477


                 ...
gi 447198629 481 YVI 483
Cdd:PRK09425 478 FVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 13-483 0e+00

2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted to act as 2-methylcitrate dehydratase, an enzyme involved in the methylcitrate cycle of propionate catabolism. A related clade of archaeal proteins that may or may not be functionally equivalent is reserved for a future model and is excluded from this family. The PrpD enzyme of E. coli is responsible for the minor aconitase activity (AcnC) not accounted for by AcnA and AcnB.


Pssm-ID: 131383  Cd Length: 468  Bit Score: 900.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   13 DREIVDIVDYVMNYEISSRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQFQLDPVQAAFNI 92
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   93 GAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAIASGKAPLTMKQVLTGMIKAHEIQGCIALENSFNRVGLDHV 172
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  173 LLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSALTA 252
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  253 PVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAgktAADIEKVTIRTHEACIRII 332
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKAR---LDEIERITITTHESAIRII 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  333 DKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEKRAIANAITLEFT 412
Cdd:TIGR02330 318 DKVGPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFK 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447198629  413 DGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRTRLEQMPVNEYLDLYVI 483
Cdd:TIGR02330 398 DGTRTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLFAI 468
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
16-480 4.45e-151

2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 438.07  E-value: 4.45e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  16 IVDIVDYVMNYEIS--SRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGpIVPGTVVPNGVRVPGTQFQLDPVQAAFNIG 93
Cdd:COG2079    1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  94 AMIRWLDFNDTWLAAEWgHPS-DNLGGILATADWLsrnaiasgkaPLTMKQVLTGMIKAHEIQGCIALEN--SFNRVGLD 170
Cdd:COG2079   80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEAL----------GASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 171 HV-LLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHApnTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSA 249
Cdd:COG2079  149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 250 LTAPvWGFYDVSFKGE--SFRFQRPYG-SYVMENVLFKiSFPAEFHSQTAVEAAMTLyeqMQAAGKTAADIEKVTIRTHE 326
Cdd:COG2079  227 LEGP-FGFFAAFAGGEfdPEALTDGLGeRWEILETSFK-PYPACRHTHAAIDAALAL---RAEHGLDPDDIERIEVETHP 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 327 ACIRIIDKKGPlNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDpekrAIANA 406
Cdd:COG2079  302 AALRIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARYPA----ARPAR 376

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447198629 407 ITLEFTDGTRFeEVVVEYPIGHARRRqDGIPKLVDKFKINLARQFPTRQQQRILEVSLdrtRLEQMP-VNEYLDL 480
Cdd:COG2079  377 VTVTLKDGRTL-EAEVDYPKGHPENP-LSDEELEAKFRALAAPVLGAARAERLLDAVR---RLEDLPdVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 17-270 8.71e-117

MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate dehydratase EC:4.2.1.79 (PrpD) that is required for propionate catabolism. It catalyzes the third step of the 2-methylcitric acid cycle.


Pssm-ID: 461115  Cd Length: 244  Bit Score: 342.92  E-value: 8.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   17 VDIVDYVMNYEISS--RVAYDTAHYCLLDTLGCGLEALEYPACKKLLGpIVPGTVVPNGVRVPGTQFQLDPVQAAFNIGA 94
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   95 MIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRnaiaSGkapltmKQVLTGMIKAHEIQGCIALENSFNRVG-LDHVL 173
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGR----SG------RDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  174 LVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKsWAAGDATSRAVRLALMAKTGEMGyPSALTAP 253
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 447198629  254 VWGFYDVSFKGESFRFQ 270
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
1-483 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1064.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   1 MSAQINNIRPEFDREIVDIVDYVMNYEISSRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQ 80
Cdd:PRK09425   1 MSAVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAIASGKAPLTMKQVLTGMIKAHEIQGCIAL 160
Cdd:PRK09425  81 FQLDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 161 ENSFNRVGLDHVLLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAK 240
Cdd:PRK09425 161 ENSFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIAL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 241 TGEMGYPSALTAPVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAgktAADIEKV 320
Cdd:PRK09425 241 TGEMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKAR---LDDIERI 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 321 TIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEK 400
Cdd:PRK09425 318 TIRTHESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEK 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 401 RAIANAITLEFTDGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRTRLEQMPVNEYLDL 480
Cdd:PRK09425 398 RSIANAVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDL 477


                 ...
gi 447198629 481 YVI 483
Cdd:PRK09425 478 FVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 13-483 0e+00

2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted to act as 2-methylcitrate dehydratase, an enzyme involved in the methylcitrate cycle of propionate catabolism. A related clade of archaeal proteins that may or may not be functionally equivalent is reserved for a future model and is excluded from this family. The PrpD enzyme of E. coli is responsible for the minor aconitase activity (AcnC) not accounted for by AcnA and AcnB.


Pssm-ID: 131383  Cd Length: 468  Bit Score: 900.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   13 DREIVDIVDYVMNYEISSRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGPIVPGTVVPNGVRVPGTQFQLDPVQAAFNI 92
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   93 GAMIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRNAIASGKAPLTMKQVLTGMIKAHEIQGCIALENSFNRVGLDHV 172
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  173 LLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSALTA 252
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  253 PVWGFYDVSFKGESFRFQRPYGSYVMENVLFKISFPAEFHSQTAVEAAMTLYEQMQAAgktAADIEKVTIRTHEACIRII 332
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKAR---LDEIERITITTHESAIRII 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  333 DKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDPEKRAIANAITLEFT 412
Cdd:TIGR02330 318 DKVGPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFK 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447198629  413 DGTRFEEVVVEYPIGHARRRQDGIPKLVDKFKINLARQFPTRQQQRILEVSLDRTRLEQMPVNEYLDLYVI 483
Cdd:TIGR02330 398 DGTRTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLFAI 468
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
16-480 4.45e-151

2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 438.07  E-value: 4.45e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  16 IVDIVDYVMNYEIS--SRVAYDTAHYCLLDTLGCGLEALEYPACKKLLGpIVPGTVVPNGVRVPGTQFQLDPVQAAFNIG 93
Cdd:COG2079    1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  94 AMIRWLDFNDTWLAAEWgHPS-DNLGGILATADWLsrnaiasgkaPLTMKQVLTGMIKAHEIQGCIALEN--SFNRVGLD 170
Cdd:COG2079   80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEAL----------GASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 171 HV-LLVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHApnTGTRKSWAAGDATSRAVRLALMAKTGEMGYPSA 249
Cdd:COG2079  149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 250 LTAPvWGFYDVSFKGE--SFRFQRPYG-SYVMENVLFKiSFPAEFHSQTAVEAAMTLyeqMQAAGKTAADIEKVTIRTHE 326
Cdd:COG2079  227 LEGP-FGFFAAFAGGEfdPEALTDGLGeRWEILETSFK-PYPACRHTHAAIDAALAL---RAEHGLDPDDIERIEVETHP 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629 327 ACIRIIDKKGPlNNPADRDHCIQYMVAIPLLFGRLTAADYEDNVAQDKRIDALREKINCFEDPAFTADYHDpekrAIANA 406
Cdd:COG2079  302 AALRIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARYPA----ARPAR 376

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447198629 407 ITLEFTDGTRFeEVVVEYPIGHARRRqDGIPKLVDKFKINLARQFPTRQQQRILEVSLdrtRLEQMP-VNEYLDL 480
Cdd:COG2079  377 VTVTLKDGRTL-EAEVDYPKGHPENP-LSDEELEAKFRALAAPVLGAARAERLLDAVR---RLEDLPdVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 17-270 8.71e-117

MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate dehydratase EC:4.2.1.79 (PrpD) that is required for propionate catabolism. It catalyzes the third step of the 2-methylcitric acid cycle.


Pssm-ID: 461115  Cd Length: 244  Bit Score: 342.92  E-value: 8.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   17 VDIVDYVMNYEISS--RVAYDTAHYCLLDTLGCGLEALEYPACKKLLGpIVPGTVVPNGVRVPGTQFQLDPVQAAFNIGA 94
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629   95 MIRWLDFNDTWLAAEWGHPSDNLGGILATADWLSRnaiaSGkapltmKQVLTGMIKAHEIQGCIALENSFNRVG-LDHVL 173
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGR----SG------RDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  174 LVKVASTAVVAEMLGLTREEILNAVSLAWVDGQSLRTYRHAPNTGTRKsWAAGDATSRAVRLALMAKTGEMGyPSALTAP 253
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 447198629  254 VWGFYDVSFKGESFRFQ 270
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
MmgE_PrpD_C pfam19305
MmgE/PrpD C-terminal domain; This entry represents the C-terminal domain of 2-methylcitrate ...
 287-462 2.34e-68

MmgE/PrpD C-terminal domain; This entry represents the C-terminal domain of 2-methylcitrate dehydratase EC:4.2.1.79 (PrpD) that is required for propionate catabolism. It catalyzes the third step of the 2-methylcitric acid cycle. This domain is related to the serine dehydratase beta chain.


Pssm-ID: 466033 [Multi-domain]  Cd Length: 173  Bit Score: 216.25  E-value: 2.34e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  287 FPAEFHSQTAVEAAMTLYEQMqaaGKTAADIEKVTIRTHEACIRIIDKKGPLNNPADRDHCIQYMVAIPLLFGRLTAADY 366
Cdd:pfam19305   1 YPAERHTHTAIDAALQLHREH---GLRPDDIESIVIRTHEAALRIIGKKGPPATRADADHSLQYVVAVALLDGRLTLEDF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447198629  367 EDNVAQDKRIDALREKINCFEDPAFTADYhdPEKRAIanaITLEFTDGTRFEEVVVEYPIGHaRRRQDGIPKLVDKFKIN 446
Cdd:pfam19305  78 EDERAADPRIDALRDKVEVVEDPEFTADY--PEKRSI---VVIVLLDGGRTLEVRVEYPKGH-PRRPLSREELEEKFRRL 151

                         170
                  ....*....|....*.
gi 447198629  447 LARQFPTRQQQRILEV 462
Cdd:pfam19305 152 AAGVLPESEAERIIII 167
 
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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