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Conserved domains on  [gi|1119636204|ref|WP_072557059|]
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MULTISPECIES: bifunctional 2-methylcitrate dehydratase/aconitate hydratase [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;
2-472 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


:

Pssm-ID: 181845  Cd Length: 480  Bit Score: 1015.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   2 PKTDRVIEEITDYVLEKEITSAEAYTTAGHVLLDTLGCGILALRYPECAKLLGPIVPGTTVPNGSKVPGTSYVLDPVRAA 81
Cdd:PRK09425   10 PDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQLDPVQAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  82 FNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRVRLSEGKEPLTVRDVLEMMIKAHEIQGVLALENSLNRVGL 161
Cdd:PRK09425   90 FNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALENSFNRVGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 162 DHVLFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTA 241
Cdd:PRK09425  170 DHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTGEMGYPSA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 242 LSAPGWGFQDVLFNKKEIKLARPLDAYVMENVLFKVSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRII 321
Cdd:PRK09425  250 LTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTHESAIRII 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 322 DKKGPLHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYLKPDKRSISNAVQVHFK 401
Cdd:PRK09425  330 DKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIANAVQVFFK 409

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636204 402 DGTSTEMVECEFPLGHRFRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQTMRVNEFVDMFCM 472
Cdd:PRK09425  410 DGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
2-472 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1015.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   2 PKTDRVIEEITDYVLEKEITSAEAYTTAGHVLLDTLGCGILALRYPECAKLLGPIVPGTTVPNGSKVPGTSYVLDPVRAA 81
Cdd:PRK09425   10 PDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQLDPVQAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  82 FNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRVRLSEGKEPLTVRDVLEMMIKAHEIQGVLALENSLNRVGL 161
Cdd:PRK09425   90 FNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALENSFNRVGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 162 DHVLFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTA 241
Cdd:PRK09425  170 DHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTGEMGYPSA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 242 LSAPGWGFQDVLFNKKEIKLARPLDAYVMENVLFKVSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRII 321
Cdd:PRK09425  250 LTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTHESAIRII 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 322 DKKGPLHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYLKPDKRSISNAVQVHFK 401
Cdd:PRK09425  330 DKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIANAVQVFFK 409

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636204 402 DGTSTEMVECEFPLGHRFRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQTMRVNEFVDMFCM 472
Cdd:PRK09425  410 DGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 5-470 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: 822.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   5 DRVIEEITDYVLEKEITSAEAYTTAGHVLLDTLGCGILALRYPECAKLLGPIVPGTTVPNGSKVPGTSYVLDPVRAAFNI 84
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  85 GCMIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRVRLSEGKEPLTVRDVLEMMIKAHEIQGVLALENSLNRVGLDHV 164
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 165 LFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTALSA 244
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 245 PGWGFQDVLFNKKEIKLARPLDAYVMENVLFKVSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRIIDKK 324
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKARLDEIERITITTHESAIRIIDKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 325 GPLHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYLKPDKRSISNAVQVHFKDGT 404
Cdd:TIGR02330 321 GPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFKDGT 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636204 405 STEMVECEFPLGHRFRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQTMRVNEFVDMF 470
Cdd:TIGR02330 401 RTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLF 466
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
8-469 5.38e-146

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


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 424.59  E-value: 5.38e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   8 IEEITDYVLEKEIT--SAEAYTTAGHVLLDTLGCGILALRYPECAKLLGpIVPGTTVPNGSKVPGTSYVLDPVRAAFNIG 85
Cdd:COG2079     1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  86 CMIRWLDYNDTWLAAEWgHPS-DNLGGILAAADYVsrvrlsegkePLTVRDVLEMMIKAHEIQGVLALEN--SLNRVGLD 162
Cdd:COG2079    80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEAL----------GASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 163 HV-LFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSpnTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTA 241
Cdd:COG2079   149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 242 LSAPgWGFQDVLFNKkEIKLARPLDA----YVMENVLFKvSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESA 317
Cdd:COG2079   227 LEGP-FGFFAAFAGG-EFDPEALTDGlgerWEILETSFK-PYPACRHTHAAIDAALALRAEHGLDPDDIERIEVETHPAA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 318 IRIIDKKGPlHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYlkPDkrSISNAVQ 397
Cdd:COG2079   304 LRIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARY--PA--ARPARVT 378

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636204 398 VHFKDGTSTEmVECEFPLGHRfRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQtmRVNEFVDM 469
Cdd:COG2079   379 VTLKDGRTLE-AEVDYPKGHP-ENPLSDEELEAKFRALAAPVLGAARAERLLDAVRRLEDLP--DVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 9-262 2.12e-113

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: 334.06  E-value: 2.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   9 EEITDYVLEKEITS--AEAYTTAGHVLLDTLGCGILALRYPECAKLLGpIVPGTTVPNGSKVPGTSYVLDPVRAAFNIGC 86
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  87 MIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRvrlsegkeplTVRDVLEMMIKAHEIQGVLALENSLNRVG-LDHVL 165
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGR----------SGRDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 166 FVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKsWAAGDATSRGVHLALMSLKGEMGyPTALSAP 245
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 1119636204 246 GWGFQDVLFNKKEIKLA 262
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
 
Name Accession Description Interval E-value
prpD PRK09425
bifunctional 2-methylcitrate dehydratase/aconitate hydratase;
2-472 0e+00

bifunctional 2-methylcitrate dehydratase/aconitate hydratase;


Pssm-ID: 181845  Cd Length: 480  Bit Score: 1015.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   2 PKTDRVIEEITDYVLEKEITSAEAYTTAGHVLLDTLGCGILALRYPECAKLLGPIVPGTTVPNGSKVPGTSYVLDPVRAA 81
Cdd:PRK09425   10 PDPDQVLVDIADYVLNYEIDSAEAYDTARYCLMDTLGCGLLALRYPECTKLLGPIVPGTVVPNGARVPGTSFQLDPVQAA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  82 FNIGCMIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRVRLSEGKEPLTVRDVLEMMIKAHEIQGVLALENSLNRVGL 161
Cdd:PRK09425   90 FNIGAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKAVAEGKEPLTMRDVLTAMIKAHEIQGVLALENSFNRVGL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 162 DHVLFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTA 241
Cdd:PRK09425  170 DHVLLVKVASTAVVAKLLGGTREEILNALSLAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIALTGEMGYPSA 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 242 LSAPGWGFQDVLFNKKEIKLARPLDAYVMENVLFKVSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRII 321
Cdd:PRK09425  250 LTAPTWGFYDVLFKGKPFRFQRPYGSYVMENVLFKISFPAEFHAQTAVEAAVTLHPQVKARLDDIERITIRTHESAIRII 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 322 DKKGPLHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYLKPDKRSISNAVQVHFK 401
Cdd:PRK09425  330 DKKGPLNNPADRDHCLQYMVAVPLLFGRLTAEDYEDAVAADPRIDALREKMVVVEDPQFTRDYLDPEKRSIANAVQVFFK 409

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119636204 402 DGTSTEMVECEFPLGHRFRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQTMRVNEFVDMFCM 472
Cdd:PRK09425  410 DGSSTEEVEVEYPIGHRRRRAEGIPLLVEKFKANLATRFPAKQQQRILDLCLDQERLEAMPVNEFVDLFVI 480
prpD TIGR02330
2-methylcitrate dehydratase; Members of this family are bacterial proteins known or predicted ...
 5-470 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: 822.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   5 DRVIEEITDYVLEKEITSAEAYTTAGHVLLDTLGCGILALRYPECAKLLGPIVPGTTVPNGSKVPGTSYVLDPVRAAFNI 84
Cdd:TIGR02330   1 DAELVDIADYVLNYEISSKEAYDTARYCLMDTLGCGLLALEYPACTKLLGPVVPGTVVPNGARVPGTSFQLDPVKAAFNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  85 GCMIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRVRLSEGKEPLTVRDVLEMMIKAHEIQGVLALENSLNRVGLDHV 164
Cdd:TIGR02330  81 GAMIRWLDFNDTWLAAEWGHPSDNLGGILAVADYLSRKRIASGKAPLTVKQVLEAMIKAHEIQGVIALENSFNRVGLDHV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 165 LFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTALSA 244
Cdd:TIGR02330 161 LLVKVASTAVVAKMLGGTREEILNALSHAWVDGQSLRTYRHAPNTGSRKSWAAGDATSRGVRLALKALTGEMGYPSALSA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 245 PGWGFQDVLFNKKEIKLARPLDAYVMENVLFKVSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRIIDKK 324
Cdd:TIGR02330 241 PVWGFYDVLFKGQSFRFPRPYGSYVMENVLFKISFPAEFHAQTAVEAAVKLHPEVKARLDEIERITITTHESAIRIIDKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 325 GPLHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYLKPDKRSISNAVQVHFKDGT 404
Cdd:TIGR02330 321 GPLNNPADRDHCIQYMVAIPLLFGRLTAEDYEDAVAQDPRIDALREKMNVVEDPRYTRDYLDPDKRSIANAVQVFFKDGT 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119636204 405 STEMVECEFPLGHRFRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQTMRVNEFVDMF 470
Cdd:TIGR02330 401 RTEEVEVEYPIGHRRRRDEGIPKLVDKFKANLARQFPSKQQQRILEVCLDQARLEQTPVNEFLDLF 466
PrpD COG2079
2-methylcitrate dehydratase PrpD [Carbohydrate transport and metabolism];
8-469 5.38e-146

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


Pssm-ID: 441682 [Multi-domain]  Cd Length: 446  Bit Score: 424.59  E-value: 5.38e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   8 IEEITDYVLEKEIT--SAEAYTTAGHVLLDTLGCGILALRYPECAKLLGpIVPGTTVPNGSKVPGTSYVLDPVRAAFNIG 85
Cdd:COG2079     1 TERLAEFAAGLRYEdlPAEVVERAKRRLLDTLGVALAGLREPPVRALRA-AAAALGGPGGATVLGTGGRLSPEDAALANG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  86 CMIRWLDYNDTWLAAEWgHPS-DNLGGILAAADYVsrvrlsegkePLTVRDVLEMMIKAHEIQGVLALEN--SLNRVGLD 162
Cdd:COG2079    80 TAAHALDFDDTHLAAIG-HPSaDVIPAALAVAEAL----------GASGRDLLTAIVAGYEVQGRLGLAVgpSHYRRGWH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 163 HV-LFVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSpnTGSRKSWAAGDATSRGVHLALMSLKGEMGYPTA 241
Cdd:COG2079   149 HTgTLGTFGAAAAAARLLGLDAEQTAHALGIAASQAAGLRQYLRF--GTMTKPLHAGFAARNGVLAALLARAGFTGPPDI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 242 LSAPgWGFQDVLFNKkEIKLARPLDA----YVMENVLFKvSYPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESA 317
Cdd:COG2079   227 LEGP-FGFFAAFAGG-EFDPEALTDGlgerWEILETSFK-PYPACRHTHAAIDAALALRAEHGLDPDDIERIEVETHPAA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 318 IRIIDKKGPlHNPADRDHCLQYITAIGLLFGDITAQHYEAETASDPRIDKLRDKMEVTENKTYTEDYlkPDkrSISNAVQ 397
Cdd:COG2079   304 LRIIGDPDP-ATPEDAKFSLPYCVAVALLDGRLGLDDFEDERLADPDVRALAAKVTVVEDPELDARY--PA--ARPARVT 378

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119636204 398 VHFKDGTSTEmVECEFPLGHRfRREEAVPKLLEKFSDNLKTHFPDKQHKHIYERCTSYETLQtmRVNEFVDM 469
Cdd:COG2079   379 VTLKDGRTLE-AEVDYPKGHP-ENPLSDEELEAKFRALAAPVLGAARAERLLDAVRRLEDLP--DVAELLAL 446
MmgE_PrpD pfam03972
MmgE/PrpD N-terminal domain; This entry represents the N-terminal domain of 2-methylcitrate ...
 9-262 2.12e-113

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: 334.06  E-value: 2.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204   9 EEITDYVLEKEITS--AEAYTTAGHVLLDTLGCGILALRYPECAKLLGpIVPGTTVPNGSKVPGTSYVLDPVRAAFNIGC 86
Cdd:pfam03972   1 EQLADYVAGLRYDDlpDEVVERAKRCLLDTLGCALAGLRHPPVTKALG-AVPGTGGPGGATVIGTGYRLDPVNAAFANGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204  87 MIRWLDYNDTWLAAEWGHPSDNLGGILAAADYVSRvrlsegkeplTVRDVLEMMIKAHEIQGVLALENSLNRVG-LDHVL 165
Cdd:pfam03972  80 AIHALDFDDTHLAAEWHHPSDNLPAILAVAEHLGR----------SGRDLLTALVVGYEIQGRLALANSFNHYGrHDHVT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 166 FVKVATTAVAAKLLGGGREEIKNALSNAWIDNAALRTYRHSPNTGSRKsWAAGDATSRGVHLALMSLKGEMGyPTALSAP 245
Cdd:pfam03972 150 LGTFGAAAAAAKLLGLDAEQIANALGIAATQAAGLRQYRHAPNTSKRK-WAAGDAARNGVFAALLAKRGFTG-PSDLLEG 227

                         250
                  ....*....|....*..
gi 1119636204 246 GWGFQDVLFNKKEIKLA 262
Cdd:pfam03972 228 EWGFYDVLSGGKDFELQ 244
MmgE_PrpD_C pfam19305
MmgE/PrpD C-terminal domain; This entry represents the C-terminal domain of 2-methylcitrate ...
 279-452 3.14e-66

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: 210.47  E-value: 3.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 279 YPAEFHAQTAAESAVILHPQVKNRIDEIDRVVIRTHESAIRIIDKKGPLHNPADRDHCLQYITAIGLLFGDITAQHYEAE 358
Cdd:pfam19305   1 YPAERHTHTAIDAALQLHREHGLRPDDIESIVIRTHEAALRIIGKKGPPATRADADHSLQYVVAVALLDGRLTLEDFEDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119636204 359 TASDPRIDKLRDKMEVTENKTYTEDYlkPDKRSIsnaVQVHFKDGTSTEMVECEFPLGHRfRREEAVPKLLEKFSDNLKT 438
Cdd:pfam19305  81 RAADPRIDALRDKVEVVEDPEFTADY--PEKRSI---VVIVLLDGGRTLEVRVEYPKGHP-RRPLSREELEEKFRRLAAG 154

                         170
                  ....*....|....*.
gi 1119636204 439 HFP--DKQHKHIYERC 452
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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