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Conserved domains on  [gi|446520785|ref|WP_000598131|]
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MULTISPECIES: 2-methylcitrate dehydratase [Bacillus]

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;
1-478 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


:

Pssm-ID: 181845  Cd Length: 480  Bit Score: 1030.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   1 MIKTNEIKQKDALLEEITDYVLNKEVTSAEAFSTARYVLLDTLGCGILALQYPECTKLLGPVVPGTIVPNGTRVPGTSYV 80
Cdd:PRK09425   3 AVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  81 LDPVKGAFNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRISEGKEPLKVREVLEMMIKAHEIQGVLALEN 160
Cdd:PRK09425  83 LDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 161 SLNRVGLDHVLYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKSWAAGDATSRGVHLAMTALKG 240
Cdd:PRK09425 163 SFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 241 EMGYPTALSAPGWGFQDVLFNKQELKLARPLDSYVMENVLFKVSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTH 320
Cdd:PRK09425 243 EMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTH 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 321 ESAIRIIDKEGPLNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDPNKRSIAN 400
Cdd:PRK09425 323 ESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIAN 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446520785 401 AVQVHFKDGTVTENVECEYPLGHRFRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNEEKLENMNVNEFVDLFLI 478
Cdd:PRK09425 403 AVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
1-478 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1030.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   1 MIKTNEIKQKDALLEEITDYVLNKEVTSAEAFSTARYVLLDTLGCGILALQYPECTKLLGPVVPGTIVPNGTRVPGTSYV 80
Cdd:PRK09425   3 AVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  81 LDPVKGAFNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRISEGKEPLKVREVLEMMIKAHEIQGVLALEN 160
Cdd:PRK09425  83 LDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 161 SLNRVGLDHVLYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKSWAAGDATSRGVHLAMTALKG 240
Cdd:PRK09425 163 SFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 241 EMGYPTALSAPGWGFQDVLFNKQELKLARPLDSYVMENVLFKVSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTH 320
Cdd:PRK09425 243 EMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTH 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 321 ESAIRIIDKEGPLNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDPNKRSIAN 400
Cdd:PRK09425 323 ESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIAN 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446520785 401 AVQVHFKDGTVTENVECEYPLGHRFRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNEEKLENMNVNEFVDLFLI 478
Cdd:PRK09425 403 AVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 11-478 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: 916.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   11 DALLEEITDYVLNKEVTSAEAFSTARYVLLDTLGCGILALQYPECTKLLGPVVPGTIVPNGTRVPGTSYVLDPVKGAFNI 90
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   91 GCMIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRISEGKEPLKVREVLEMMIKAHEIQGVLALENSLNRVGLDHV 170
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  171 LYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKSWAAGDATSRGVHLAMTALKGEMGYPTALSA 250
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  251 PGWGFQDVLFNKQELKLARPLDSYVMENVLFKVSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTHESAIRIIDKE 330
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKARLDEIERITITTHESAIRIIDKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  331 GPLNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDPNKRSIANAVQVHFKDGT 410
Cdd:TIGR02330 321 GPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFKDGT 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446520785  411 VTENVECEYPLGHRFRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNEEKLENMNVNEFVDLFLI 478
Cdd:TIGR02330 401 RTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLFAI 468
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
14-475 3.25e-152

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


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 440.77  E-value: 3.25e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  14 LEEITDYVLNKEVT--SAEAFSTARYVLLDTLGCGILALQYPECTKLLGpVVPGTIVPNGTRVPGTSYVLDPVKGAFNIG 91
Cdd:COG2079    1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  92 CMIRWLDYNDTWLAAEWgHPS-DNLGGILAVADYisrvrisegkEPLKVREVLEMMIKAHEIQGVLALEN--SLNRVGLD 168
Cdd:COG2079   80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEA----------LGASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 169 HV-LYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHApnTGSRKSWAAGDATSRGVHLAMTALKGEMGYPTA 247
Cdd:COG2079  149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 248 LSAPgWGFQDVLFNKQ--ELKLARPL-DSYVMENVLFKvSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTHESAI 324
Cdd:COG2079  227 LEGP-FGFFAAFAGGEfdPEALTDGLgERWEILETSFK-PYPACRHTHAAIDAALALRAEHGLDPDDIERIEVETHPAAL 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 325 RIIDKEGPlNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDpnkrSIANAVQV 404
Cdd:COG2079  305 RIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARYPA----ARPARVTV 379

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446520785 405 HFKDGTVTEnVECEYPLGHRfRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNeekLENM-NVNEFVDL 475
Cdd:COG2079  380 TLKDGRTLE-AEVDYPKGHP-ENPLSDEELEAKFRALAAPVLGAARAERLLDAVRR---LEDLpDVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 15-268 1.25e-114

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: 337.14  E-value: 1.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   15 EEITDYVLNKEVTS--AEAFSTARYVLLDTLGCGILALQYPECTKLLGpVVPGTIVPNGTRVPGTSYVLDPVKGAFNIGC 92
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   93 MIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRisegkeplkvREVLEMMIKAHEIQGVLALENSLNRVG-LDHVL 171
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGRSG----------RDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  172 YVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKsWAAGDATSRGVHLAMTALKGEMGyPTALSAP 251
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 446520785  252 GWGFQDVLFNKQELKLA 268
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
1-478 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1030.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   1 MIKTNEIKQKDALLEEITDYVLNKEVTSAEAFSTARYVLLDTLGCGILALQYPECTKLLGPVVPGTIVPNGTRVPGTSYV 80
Cdd:PRK09425   3 AVISNVRPDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  81 LDPVKGAFNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRISEGKEPLKVREVLEMMIKAHEIQGVLALEN 160
Cdd:PRK09425  83 LDPVQAAFNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALEN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 161 SLNRVGLDHVLYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKSWAAGDATSRGVHLAMTALKG 240
Cdd:PRK09425 163 SFNRVGLDHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 241 EMGYPTALSAPGWGFQDVLFNKQELKLARPLDSYVMENVLFKVSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTH 320
Cdd:PRK09425 243 EMGYPSALTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTH 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 321 ESAIRIIDKEGPLNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDPNKRSIAN 400
Cdd:PRK09425 323 ESAIRIIDKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIAN 402

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446520785 401 AVQVHFKDGTVTENVECEYPLGHRFRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNEEKLENMNVNEFVDLFLI 478
Cdd:PRK09425 403 AVQVFFKDGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 11-478 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: 916.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   11 DALLEEITDYVLNKEVTSAEAFSTARYVLLDTLGCGILALQYPECTKLLGPVVPGTIVPNGTRVPGTSYVLDPVKGAFNI 90
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   91 GCMIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRISEGKEPLKVREVLEMMIKAHEIQGVLALENSLNRVGLDHV 170
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  171 LYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKSWAAGDATSRGVHLAMTALKGEMGYPTALSA 250
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  251 PGWGFQDVLFNKQELKLARPLDSYVMENVLFKVSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTHESAIRIIDKE 330
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKARLDEIERITITTHESAIRIIDKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  331 GPLNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDPNKRSIANAVQVHFKDGT 410
Cdd:TIGR02330 321 GPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFKDGT 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446520785  411 VTENVECEYPLGHRFRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNEEKLENMNVNEFVDLFLI 478
Cdd:TIGR02330 401 RTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLFAI 468
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
14-475 3.25e-152

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


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 440.77  E-value: 3.25e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  14 LEEITDYVLNKEVT--SAEAFSTARYVLLDTLGCGILALQYPECTKLLGpVVPGTIVPNGTRVPGTSYVLDPVKGAFNIG 91
Cdd:COG2079    1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  92 CMIRWLDYNDTWLAAEWgHPS-DNLGGILAVADYisrvrisegkEPLKVREVLEMMIKAHEIQGVLALEN--SLNRVGLD 168
Cdd:COG2079   80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEA----------LGASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 169 HV-LYVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHApnTGSRKSWAAGDATSRGVHLAMTALKGEMGYPTA 247
Cdd:COG2079  149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 248 LSAPgWGFQDVLFNKQ--ELKLARPL-DSYVMENVLFKvSYPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTHESAI 324
Cdd:COG2079  227 LEGP-FGFFAAFAGGEfdPEALTDGLgERWEILETSFK-PYPACRHTHAAIDAALALRAEHGLDPDDIERIEVETHPAAL 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785 325 RIIDKEGPlNNPADRDHCLQYITAIGLLKGDIVADDYEDAVANDPRVDELRNKMVVVENKQYSLDYLDpnkrSIANAVQV 404
Cdd:COG2079  305 RIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARYPA----ARPARVTV 379

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446520785 405 HFKDGTVTEnVECEYPLGHRfRRDEAIPKVVQKFTANMAGHYSSKQQEQIHEACLNeekLENM-NVNEFVDL 475
Cdd:COG2079  380 TLKDGRTLE-AEVDYPKGHP-ENPLSDEELEAKFRALAAPVLGAARAERLLDAVRR---LEDLpDVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 15-268 1.25e-114

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: 337.14  E-value: 1.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   15 EEITDYVLNKEVTS--AEAFSTARYVLLDTLGCGILALQYPECTKLLGpVVPGTIVPNGTRVPGTSYVLDPVKGAFNIGC 92
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785   93 MIRWLDYNDTWLAAEWGHPSDNLGGILAVADYISRVRisegkeplkvREVLEMMIKAHEIQGVLALENSLNRVG-LDHVL 171
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGRSG----------RDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  172 YVKVATTAVVAKMLGGTREEIFNALSHAWIDNSSLRTYRHAPNTGSRKsWAAGDATSRGVHLAMTALKGEMGyPTALSAP 251
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 446520785  252 GWGFQDVLFNKQELKLA 268
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
MmgE_PrpD_C pfam19305
MmgE/PrpD C-terminal domain; This entry represents the C-terminal domain of 2-methylcitrate ...
 285-460 3.39e-69

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: 218.18  E-value: 3.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  285 YPAEFHAQTAAECAVKLHPEIKGKLDEIDRITITTHESAIRIIDKEGPLNNPADRDHCLQYITAIGLLKGDIVADDYEDA 364
Cdd:pfam19305   1 YPAERHTHTAIDAALQLHREHGLRPDDIESIVIRTHEAALRIIGKKGPPATRADADHSLQYVVAVALLDGRLTLEDFEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446520785  365 VANDPRVDELRNKMVVVENKQYSLDYldPNKRSIanaVQVHFKDGTVTENVECEYPLGHRfRRDEAIPKVVQKFTANMAG 444
Cdd:pfam19305  81 RAADPRIDALRDKVEVVEDPEFTADY--PEKRSI---VVIVLLDGGRTLEVRVEYPKGHP-RRPLSREELEEKFRRLAAG 154

                         170
                  ....*....|....*.
gi 446520785  445 HYSSKQQEQIHEACLN 460
Cdd:pfam19305 155 VLPESEAERIIIIVLV 170
 
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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