|
Name |
Accession |
Description |
Interval |
E-value |
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
19-383 |
8.42e-171 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 481.60 E-value: 8.42e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 19 IDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTTIGGLAYGAESPESMKLNIDTYFTPLLLGQPAD 98
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 99 QVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLARRRHRI 178
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 179 FKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLTAQAKIA 256
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENreALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 257 IMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFHALQWG 336
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1436944753 337 TELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERVQFFNR 383
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRR 367
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-378 |
4.61e-166 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 469.49 E-value: 4.61e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 18 TIDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTTIGGLAYGAESPESMKLNIDTYFTPLLLGQPA 97
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 98 DQVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLARRRHR 177
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 178 IFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACA--DALMRLTAQAKI 255
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPREnlDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 256 AIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFHALQW 335
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1436944753 336 GTELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERV 378
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
18-378 |
1.05e-97 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 295.19 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 18 TIDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVgigegttigglAYG-----AESPESMKLNIDTYFTPLL 92
Cdd:COG4948 2 KITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGIT-----------GWGeavpgGTGAEAVAAALEEALAPLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 93 LGQPADQVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLA 172
Cdd:COG4948 71 IGRDPLDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 173 rRRHRIFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLT 250
Cdd:COG4948 151 -RGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDleGLAELR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 251 AQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATF 330
Cdd:COG4948 230 RATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAAL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1436944753 331 HALQWGtELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERV 378
Cdd:COG4948 310 PNFDIV-ELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
162-377 |
3.62e-50 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 168.13 E-value: 3.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 162 KDIDEAEEMLARRRHRIFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVA 241
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 242 CAD--ALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGaIG 319
Cdd:pfam13378 81 PDDleGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP-IG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436944753 320 TVASAHAFATFHALQWGTELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEER 377
Cdd:pfam13378 160 LAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
161-255 |
8.31e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 75.01 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 161 AKDIDEAEEMLARRRHRIFKLKIGtRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPV 240
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVG-GGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|....*..
gi 1436944753 241 ACAD--ALMRLTAQAKI 255
Cdd:smart00922 81 PPDDleGLAELRRATPI 97
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
145-293 |
3.65e-14 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 145 LRKSLPVAWTLAsgdtAKDIDEAEEMLARRRH-RIFKLKIGTR--DVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEA 221
Cdd:PRK02901 75 VRDRVPVNATVP----AVDAAQVPEVLARFPGcRTAKVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEA 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436944753 222 RYGVDGL-ADVGCELVEQPVACADALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRA 293
Cdd:PRK02901 151 VAAARALdADGPLEYVEQPCATVEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRA 223
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
19-383 |
8.42e-171 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 481.60 E-value: 8.42e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 19 IDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTTIGGLAYGAESPESMKLNIDTYFTPLLLGQPAD 98
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 99 QVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLARRRHRI 178
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 179 FKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLTAQAKIA 256
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENreALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 257 IMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFHALQWG 336
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1436944753 337 TELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERVQFFNR 383
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRR 367
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-378 |
4.61e-166 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 469.49 E-value: 4.61e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 18 TIDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTTIGGLAYGAESPESMKLNIDTYFTPLLLGQPA 97
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 98 DQVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLARRRHR 177
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 178 IFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACA--DALMRLTAQAKI 255
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPREnlDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 256 AIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFHALQW 335
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1436944753 336 GTELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERV 378
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
18-378 |
1.05e-97 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 295.19 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 18 TIDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVgigegttigglAYG-----AESPESMKLNIDTYFTPLL 92
Cdd:COG4948 2 KITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGIT-----------GWGeavpgGTGAEAVAAALEEALAPLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 93 LGQPADQVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLASGDTAKDIDEAEEMLA 172
Cdd:COG4948 71 IGRDPLDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 173 rRRHRIFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLT 250
Cdd:COG4948 151 -RGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDleGLAELR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 251 AQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATF 330
Cdd:COG4948 230 RATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAAL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1436944753 331 HALQWGtELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERV 378
Cdd:COG4948 310 PNFDIV-ELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
22-339 |
4.55e-58 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 190.25 E-value: 4.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 22 IQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIgegttigglaygAESPesmklnidtyftplllgqpadqvp 101
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGW------------AEAT------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 102 flmqqletairgnrfaKSAIETALYDALGQRLNLSVAELLGGsLRKSLPVAWTLASGDTAKDIDEAEeMLARRRHRIFKL 181
Cdd:cd03315 45 ----------------KAAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEAR-RALEAGFRTFKL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 182 KIGtRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLTAQAKIAIMA 259
Cdd:cd03315 107 KVG-RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDleGRAALARATDTPIMA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 260 DELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFHALQWGTEL 339
Cdd:cd03315 186 DESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGEL 265
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
162-377 |
3.62e-50 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 168.13 E-value: 3.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 162 KDIDEAEEMLARRRHRIFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVA 241
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 242 CAD--ALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGaIG 319
Cdd:pfam13378 81 PDDleGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP-IG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436944753 320 TVASAHAFATFHALQWGTELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEER 377
Cdd:pfam13378 160 LAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
72-345 |
5.42e-44 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 155.04 E-value: 5.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 72 YGaESPESMKLNIdTYFTPLLLGQPAdQVPFLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPV 151
Cdd:cd03319 50 TG-ETVESVLAAL-KSVRPALIGGDP-RLEKLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLET 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 152 AWTLAsgdtakdIDEAEEMLAR------RRHRIFKLKIGTrDVAKDIAHVAAIKKALGDrGAVRVDVNMAWSELEARYGV 225
Cdd:cd03319 127 DYTIS-------IDTPEAMAAAakkaakRGFPLLKIKLGG-DLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 226 DGLADVGCELVEQPVA--CADALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEA 303
Cdd:cd03319 198 RELAELGVELIEQPVPagDDDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARA 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1436944753 304 ANIELYGGTMLEGAIGTVASAH---AFATFHalqwgtELFGPLLI 345
Cdd:cd03319 278 AGLKVMVGCMVESSLSIAAAAHlaaAKADFV------DLDGPLLL 316
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
18-371 |
1.64e-36 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 136.20 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 18 TIDSIQTLLVDLPTIRPHQlsmtTMKGQTLMLVRIHCSDGSVGIGEgttigglAYGAESPESMKLNIDTYFTPLLLGQPA 97
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGE-------AYPGGRPSAVAAAIEDLLAPLLIGRDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 98 DQVPFLMQQLE--TAIRGNR----FAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTlaSGDTAKDIDEAEEML 171
Cdd:cd03316 70 LDIERLWEKLYrrLFWRGRGgvamAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYAS--GGGYDDSPEELAEEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 172 ARRR---HRIFKLKIG-----TRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACA 243
Cdd:cd03316 148 KRAVaegFTAVKLKVGgpdsgGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 244 D--ALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAanielYGGTM----LEGA 317
Cdd:cd03316 228 DleGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEA-----HGVRVaphgAGGP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1436944753 318 IGTVASAHAFATFHALQWgTELFGPLLITEEILAT-PLVYENFELQIPQGPGLGI 371
Cdd:cd03316 303 IGLAASLHLAAALPNFGI-LEYHLDDLPLREDLFKnPPEIEDGYVTVPDRPGLGV 356
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
22-329 |
2.00e-32 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 122.05 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 22 IQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGsvgigegttigglaygaespesmklnidtyftplllgqpadqvp 101
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSG-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 102 flmqqletaIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTlasgdtakdideaeemlarrrhrifkl 181
Cdd:cd00308 37 ---------VVGWGEVISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS--------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 182 kigtrdvakdIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVA--CADALMRLTAQAKIAIMA 259
Cdd:cd00308 81 ----------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCApdDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 260 DELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFAT 329
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAA 220
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
22-378 |
1.77e-27 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 111.56 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 22 IQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTTIGGLAYGAESPESMKLNIDTYFTPLLLGQPaDQVP 101
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGRE-FSHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 102 FLMQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLGGSlRKSLPVAWTL----ASGDTAKDIDEAEEMLARRrhr 177
Cdd:cd03317 80 EEVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVGVSIgiqdDVEQLLKQIERYLEEGYKR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 178 iFKLKIgtrDVAKDIAHVAAIKKALGDRGaVRVDVNMA-----WSELEArygvdgLADVGCELVEQPVACADAL--MRLT 250
Cdd:cd03317 156 -IKLKI---KPGWDVEPLKAVRERFPDIP-LMADANSAytladIPLLKR------LDEYGLLMIEQPLAADDLIdhAELQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 251 AQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGtvaSAH--AFA 328
Cdd:cd03317 225 KLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIG---RAHnvALA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436944753 329 T----------------FHalqwgtelfgpllitEEILATPLVYENFELQIPQGPGLGIALDEERV 378
Cdd:cd03317 302 SlpnftypgdisassryFE---------------EDIITPPFELENGIISVPTGPGIGVTVDREAL 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
117-331 |
3.22e-24 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 100.41 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 117 AKSAIETALydalgqrLNLSVAELLGGSLRKSLPVAWTLASGDTAkDIDEAEEMLARRrHRIFKLKIGTRDVAKDIAHVA 196
Cdd:cd03320 48 LAFGIESAL-------ANLEALLVGFTRPRNRIPVNALLPAGDAA-ALGEAKAAYGGG-YRTVKLKVGATSFEEDLARLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 197 AIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLTAQAKIAimADELLVGPASAFELAK 274
Cdd:cd03320 119 ALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDlaELRRLAAGVPIA--LDESLRRLDDPLALAA 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436944753 275 NNAAHVFAIKVEQSGGLRASQKVAAIAEAANIELYGGTMLEGAIGTVASAHAFATFH 331
Cdd:cd03320 197 AGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALP 253
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
24-142 |
9.61e-23 |
|
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold similarity with enolase N-terminal domain.
Pssm-ID: 397046 [Multi-domain] Cd Length: 117 Bit Score: 92.15 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 24 TLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGTtigglAYGAeSPESMKLNIDTYFTPLLLGQPADQVPFL 103
Cdd:pfam02746 5 FVVDVGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEAT-----SYGG-RAETIKAILDDHLAPLLIGRDAANISDL 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1436944753 104 MQQLETAIRGNRFAKSAIETALYDALGQRLNLSVAELLG 142
Cdd:pfam02746 79 WQLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
17-381 |
1.13e-18 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 86.38 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 17 VTIDSIQTLLVDLPTIRPHQLSMTTMKGQTLMLVRIHCSDGSVGIGEGttiggLAYGAESPESMKLNIDTyFTPLLLGQP 96
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYL-----FTYTPAALKSLKQLLDD-MAALLVGEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 97 AdqVPFLMQQ-LETAIR--GN----RFAKSAIETALYDALGQRLNLSVAELLGGSLRkslPV-AWTLASGDTAKD-IDEA 167
Cdd:cd03321 75 L--APAELERaLAKRFRllGYtglvRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR---PVqAYDSHGLDGAKLaTERA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 168 EEMLARRRHRIfKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--A 245
Cdd:cd03321 150 VTAAEEGFHAV-KTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDyeG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 246 LMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGG----LRASQKVAAIaeaanielygGTMLEGAIGTV 321
Cdd:cd03321 229 HARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGvtgwLRASALAEQA----------GIPMSSHLFQE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436944753 322 ASAHAFA---TFHALQWgTELFGPlliteeILATPLVYENFELQIPQGPGLGIALDEERVQFF 381
Cdd:cd03321 299 ISAHLLAvtpTAHWLEY-VDWAGA------ILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
161-255 |
8.31e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 75.01 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 161 AKDIDEAEEMLARRRHRIFKLKIGtRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPV 240
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVG-GGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|....*..
gi 1436944753 241 ACAD--ALMRLTAQAKI 255
Cdd:smart00922 81 PPDDleGLAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
119-383 |
4.35e-16 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 79.29 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 119 SAIETALYDALGQRLNLSVAELLGGSLRKSLPVA------------------WTLASGDtAKDID----EAEEMLARRRH 176
Cdd:cd03323 107 TAFEVALLDLLGQALGVPVADLLGGGQRDSVPFLaylfykgdrhktdlpypwFRDRWGE-ALTPEgvvrLARAAIDRYGF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 177 RIFKLKIGTRDVAKDIAHVAAIKKAL-GDRgaVRVDVNMAWSELEARYGVDGLADVgCELVEQPVACADALMRL------ 249
Cdd:cd03323 186 KSFKLKGGVLPGEEEIEAVKALAEAFpGAR--LRLDPNGAWSLETAIRLAKELEGV-LAYLEDPCGGREGMAEFrratgl 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 250 -TAQAKIAIMADELlvgpASAFELAknnaahvfAIKVEQS-----GGLRASQKVAAIAEAANIELYGGTMLEGAIGTVAS 323
Cdd:cd03323 263 pLATNMIVTDFRQL----GHAIQLN--------AVDIPLAdhhfwGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMM 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 324 AHAFATFHALQWGTELFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEERVQFFNR 383
Cdd:cd03323 331 THVAAAAPGLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHE 390
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
50-374 |
4.51e-16 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239443 [Multi-domain] Cd Length: 341 Bit Score: 78.53 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 50 VRIHCSDGSVGigegttiggLAYGAESPESMKLnIDTYFTPLLLGQPADQVPFLMQQLetaIRGNRF---------AKSA 120
Cdd:cd03327 14 VEIETDDGTVG---------YANTTGGPVACWI-VDQHLARFLIGKDPSDIEKLWDQM---YRATLAygrkgiamaAISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 121 IETALYDALGQRLNLSVAELLGGSLRKSLPVAWT-LASGDTAKDIDEAEEMLaRRRHRIFKLKI------GTRDVAKDIA 193
Cdd:cd03327 81 VDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYL-KEGYRGMKMRFgygpsdGHAGLRKNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 194 HVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCELVEQPVACAD--ALMRLTAQAKIAIMADELLVGPASAFE 271
Cdd:cd03327 160 LVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDieGYAELKKATGIPISTGEHEYTVYGFKR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 272 LAKNNAAHVFAIKVEQSGGLRASQKVAAIAEAanielYGGTMLEGAiGTVASAHAFATFHA-----------LQWGTELF 340
Cdd:cd03327 240 LLEGRAVDILQPDVNWVGGITELKKIAALAEA-----YGVPVVPHA-SQIYNYHFIMSEPNspfaeylpnspDEVGNPLF 313
|
330 340 350
....*....|....*....|....*....|....
gi 1436944753 341 GPLLITEeilatpLVYENFELQIPQGPGLGIALD 374
Cdd:cd03327 314 YYIFLNE------PVPVNGYFDLSDKPGFGLELN 341
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
91-374 |
1.61e-15 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 76.98 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 91 LLLGQPADQVPFLMQQLetaIRGNRF--------AKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVaWTLASGDTAK 162
Cdd:cd03325 50 YLIGKDPMNIEHHWQVM---YRGGFYrggpvlmsAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRV-YSWIGGDRPS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 163 DIDEAEEMLARRRHRIFKLK-------IGTRD-VAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCE 234
Cdd:cd03325 126 DVAEAARARREAGFTAVKMNateelqwIDTSKkVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 235 LVEQPVAC--ADALMRLTAQAKIAIMADELLVgpaSAFELAKNNAAHVFAI---KVEQSGGLRASQKVaaiaeAANIELY 309
Cdd:cd03325 206 FIEEPVLPenVEALAEIAARTTIPIATGERLF---SRWDFKELLEDGAVDIiqpDISHAGGITELKKI-----AAMAEAY 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436944753 310 GGTML----EGAIGTVASAH-AFATFHALQWGTELF-----GPLLITEEILATPLVYENFELQIPQGPGLGIALD 374
Cdd:cd03325 278 DVALAphcpLGPIALAASLHvDASTPNFLIQEQSLGihyneGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
84-290 |
1.74e-14 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 73.99 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 84 IDTYFTPLLLGQPADQVPFLMQQLETAIRGN------RFAKSAIETALYDALGQRLNLSVAELLGgSLRKSLPVAWTlaS 157
Cdd:cd03328 56 VDGLLAPVVEGRDALDPPAAWEAMQRAVRNAgrpgvaAMAISAVDIALWDLKARLLGLPLARLLG-RAHDSVPVYGS--G 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 158 GDTAKDIDEAEEMLARRRH---RIFKLKIGtRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCE 234
Cdd:cd03328 133 GFTSYDDDRLREQLSGWVAqgiPRVKMKIG-RDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVT 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 235 LVEQPVACAD----ALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGG 290
Cdd:cd03328 212 WFEEPVSSDDlaglRLVRERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGG 271
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
145-293 |
3.65e-14 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 145 LRKSLPVAWTLAsgdtAKDIDEAEEMLARRRH-RIFKLKIGTR--DVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEA 221
Cdd:PRK02901 75 VRDRVPVNATVP----AVDAAQVPEVLARFPGcRTAKVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEA 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436944753 222 RYGVDGL-ADVGCELVEQPVACADALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLRA 293
Cdd:PRK02901 151 VAAARALdADGPLEYVEQPCATVEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRA 223
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
84-265 |
6.35e-09 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 57.02 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 84 IDTYFTPLLLGQPADQVPFLMQQLETAIRG-NRFAKSAIETALYDALGQRLNLSVAELLGGsLRKSLPVAWTLASGDTAK 162
Cdd:cd03329 61 VDRFLKKVLIGQDPLDRERLWQDLWRLQRGlTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 163 DI-------DEAEEMLArRRHRIFKLKI-GTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARYGVDGLADVGCE 234
Cdd:cd03329 140 GLespeayaDFAEECKA-LGYRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFF 218
|
170 180 190
....*....|....*....|....*....|...
gi 1436944753 235 LVEQPVACAD--ALMRLTAQAKIAIMADELLVG 265
Cdd:cd03329 219 WYEDPLREASisSYRWLAEKLDIPILGTEHSRG 251
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
155-292 |
1.55e-07 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 52.50 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 155 LASGDTAKDIDEAEEMLArrrHRIFKLKIGTRDVAKDIAHVAAIKKALGDRGAVRVDVNMAWSELEARY---GVDGLADV 231
Cdd:TIGR01927 107 LPAGDPALLLLRSAKAEG---FRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQflkALDPNLRG 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436944753 232 GCELVEQPVACADALMRLTAQAKIAIMADELLVGPASAFELAKNNAAHVFAIKVEQSGGLR 292
Cdd:TIGR01927 184 RIAFLEEPLPDADEMSAFSEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPA 244
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
41-376 |
7.18e-07 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 50.90 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 41 TMKGQTLMLVRIHCSDGsvgigegttigGLAYGAES----PESMKLNIDTYFTPLLLGQPADQVPFLMQQLETAI---RG 113
Cdd:cd03322 10 TCPGRNFVTLKITTDQG-----------VTGLGDATlngrELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAywrRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 114 ---NRfAKSAIETALYDALGQRLNLSVAELLGGSLRKSLpVAWTLASGDtakDIDEAEEmlARRRHrifkLKIGTRDV-A 189
Cdd:cd03322 79 pvtMN-AIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGI-MVYSHASGR---DIPELLE--AVERH----LAQGYRAIrV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 190 KDIAHVAAIKKALGDRGAVRVDVNMAWSELEA-RYGVDgLADVGCELVEQPVACAD--ALMRLTAQAKIAIMADELLVGP 266
Cdd:cd03322 148 QLPKLFEAVREKFGFEFHLLHDVHHRLTPNQAaRFGKD-VEPYRLFWMEDPTPAENqeAFRLIRQHTATPLAVGEVFNSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 267 ASAFELAKNNAAHVFAIKVEQSGGLRASQKVaaiaeAANIELYG-GTMLEGA-----IGTVASAHAFATFH--ALQwgtE 338
Cdd:cd03322 227 WDWQNLIQERLIDYIRTTVSHAGGITPARKI-----ADLASLYGvRTGWHGPtdlspVGMAAALHLDLWVPnfGIQ---E 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 1436944753 339 LFGPLLITEEILATPLVYENFELQIPQGPGLGIALDEE 376
Cdd:cd03322 299 YMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEK 336
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
117-180 |
2.80e-03 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 39.51 E-value: 2.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436944753 117 AKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVaWTLASGdtaKDIDEAEEMLARRRHRIFK 180
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMV-YGHANG---RDIDELLDDVARHLELGYK 144
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
117-314 |
3.45e-03 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 38.96 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 117 AKSAIETALYDALGQRLNLSVAELLGGSLRKSLPVAWTLAsgdtakdIDEAEEM------LARRRHRIFKLKIGTRDVAK 190
Cdd:PRK15129 87 ARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVV-------IGTPEQMansasaLWQAGAKLLKVKLDNHLISE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 191 diaHVAAIKKALGDRGAVrVDVNMAW-SE-LEARYGVdgLADVGCELVEQPVACADALMRLTAQAKIAIMADEL------ 262
Cdd:PRK15129 160 ---RMVAIRSAVPDATLI-VDANESWrAEgLAARCQL--LADLGVAMLEQPLPAQDDAALENFIHPLPICADESchtrss 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436944753 263 LVGPASAFELAKnnaahvfaIKVEQSGGLRASQKVAAIAEAANIELYGGTML 314
Cdd:PRK15129 234 LKALKGRYEMVN--------IKLDKTGGLTEALALATEARAQGFALMLGCML 277
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
120-261 |
4.01e-03 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 38.84 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436944753 120 AIETALYDALGQRLNLSVaellggslrKSLPVAWTLASGDTAKDideAEEMLARRRHRIFKLKIGTRDVAKDIAHVAAIK 199
Cdd:PRK02714 90 GFESALENESGSRSNVTL---------NPLSYSALLPAGEAALQ---QWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436944753 200 KALGDRGAVRVDVNMAWSELEARYGV---DGLADVGCELVEQPVACA--DALMRLTAQAKIAIMADE 261
Cdd:PRK02714 158 ERLPAGAKLRLDANGGLSLEEAKRWLqlcDRRLSGKIEFIEQPLPPDqfDEMLQLSQDYQTPIALDE 224
|
|
| |
