|
Name |
Accession |
Description |
Interval |
E-value |
| 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 ... |
50-375 |
1.44e-111 |
|
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: 329.53 E-value: 1.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 50 KAENRELNVALLSPFTIASSRLDSVSNVAIRIELnDGFVGWGEAPILPSVTAEDQIMAMVKAREASEFLRELPEMkLGNV 129
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIEL-DGITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDPR-LEKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 130 LQEIGRFLPGhqFASVRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIV-SPAEASVLASKYRKRGFETLKLK 208
Cdd:cd03319 79 LEALQELLPG--NGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIdTPEAMAAAAKKAAKRGFPLLKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 209 VGKNLKADIEVLQAIRAVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGLSHVTRtaknRFGVS 288
Cdd:cd03319 157 LGGDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGVE--LIEQPVPAGDDDGLAYLRD----KSPLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 289 IAADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAglGCFRFI 367
Cdd:cd03319 231 IMADESCFSAADAARLAGGGAYDGINIKLMKTgGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAA--AKADFV 308
|
....*...
gi 18401824 368 DLDTPLLL 375
Cdd:cd03319 309 DLDGPLLL 316
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
54-400 |
5.44e-82 |
|
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: 255.52 E-value: 5.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 54 RELNVALLSPFTIASSRLDSVSNVAIRIELNDGFVGWGEAPilPSVTAEDQIMAMVKaREASEFLRELPEMKLGNVLQEI 133
Cdd:COG4948 9 YPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAV--PGGTGAEAVAAALE-EALAPLLIGRDPLDIEALWQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 134 GRFLPGHQFAsvRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIVSPAEASV-LASKYRKRGFETLKLKVGK- 211
Cdd:COG4948 86 YRALPGNPAA--KAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAeEAREAVARGFRALKLKVGGp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 212 NLKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGLSHVTRtaknRFGVSIA 290
Cdd:COG4948 164 DPEEDVERVRAVReAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE--WIEQPLPAEDLEGLAELRR----ATPVPIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 291 ADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGLGCFRFIDL 369
Cdd:COG4948 238 ADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIVEL 317
|
330 340 350
....*....|....*....|....*....|.
gi 18401824 370 DTPLLLADDPVQGGYKACGAVYEFKDEGGHG 400
Cdd:COG4948 318 DGPLLLADDLVEDPLRIEDGYLTVPDGPGLG 348
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
60-367 |
1.82e-42 |
|
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: 149.80 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 60 LLSPFTIASSRLDSVSNVAIRIELNDGFVGWGEAPilpsvtaedqimamvkareaseflrelpemklgnvlqeigrflpg 139
Cdd:cd03315 10 LKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEAT--------------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 140 hqfasvRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIVSPAEASVLASKYRKRGFETLKLKVGKNLKADIEV 219
Cdd:cd03315 45 ------KAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDPARDVAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 220 LQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGLSHVTRtaknRFGVSIAADESCRGL 298
Cdd:cd03315 119 VAALReAVGDDAELRVDANRGWTPKQAIRALRALEDLGLD--YVEQPLPADDLEGRAALAR----ATDTPIMADESAFTP 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 299 TDLKKIIEGNIVDVVNIKLAKTG-ILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGLGCFRFI 367
Cdd:cd03315 193 HDAFRELALGAADAVNIKTAKTGgLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLP 262
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
56-381 |
4.68e-37 |
|
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: 138.22 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 56 LNVALLSPFTIASSRLDSVSNVAIRIELNDGFVGWGEA--PILPSVTAE--DQIMAMVKAreaseFLREL----PEMKLG 127
Cdd:cd03318 10 VDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEAttPGGPAWGGEspETIKAIIDR-----YLAPLligrDATNIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 128 NVLQEIGRFLPGHQFAsvRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIVSPAEASV-LASKYRKRG-FETL 205
Cdd:cd03318 85 AAMALLDRAVAGNLFA--KAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIaEAEEMLEAGrHRRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 206 KLKVGKN-LKADIEVLQAIRAVHPT-CSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGLSHVTRtakn 283
Cdd:cd03318 163 KLKMGARpPADDLAHVEAIAKALGDrASVRVDVNQAWDESTAIRALPRLEAAGVE--LIEQPVPRENLDGLARLRS---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 284 RFGVSIAADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGL- 361
Cdd:cd03318 237 RNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSgGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLp 316
|
330 340
....*....|....*....|....
gi 18401824 362 ----GCfrfiDLDTPLLLADDPVQ 381
Cdd:cd03318 317 slpfGC----ELFGPLLLAEDLLE 336
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
51-359 |
1.59e-35 |
|
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: 133.90 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 51 AENRELNVALLSPFTIASSRLDSVSNVAIRIELNDGFVGWGEAP--ILPSVTAEDQIMAMVKAREAseFLRELPEMKLGN 128
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVafEGPFYTEETNATAWHILKDY--LLPLLLGREFSH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 129 --VLQEIGRFLPGHQFAsvRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIVSPAEASV-LASKYRKRGFETL 205
Cdd:cd03317 79 peEVSERLAPIKGNNMA--KAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQLLkQIERYLEEGYKRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 206 KLKVGKNLkaDIEVLQAIRAVHPTCSFILDANEGYQTEEA--VKVLETLHEMkvtpvLFEQPVHRDNWEGLSHVTRTAKN 283
Cdd:cd03317 157 KLKIKPGW--DVEPLKAVRERFPDIPLMADANSAYTLADIplLKRLDEYGLL-----MIEQPLAADDLIDHAELQKLLKT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18401824 284 RfgvsIAADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAA 359
Cdd:cd03317 230 P----ICLDESIQSAEDARKAIELGACKIINIKPGRVgGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALAS 302
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
79-384 |
2.13e-32 |
|
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: 125.42 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 79 IRIELNDGFVGWGEAPilpSVTAEDQIMAMVKAREASEFLRELPEM--KLGNVLQEIGRFLPGHQFASVR-AGMEMAMID 155
Cdd:cd03316 29 VRVTTDDGITGWGEAY---PGGRPSAVAAAIEDLLAPLLIGRDPLDieRLWEKLYRRLFWRGRGGVAMAAiSAVDIALWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 156 AAAKSVRVPLWKLFGG---------ASSTITTDitipivSPAEASVLASKYRKRGFETLKLKVG------KNLKADIEVL 220
Cdd:cd03316 106 IKGKAAGVPVYKLLGGkvrdrvrvyASGGGYDD------SPEELAEEAKRAVAEGFTAVKLKVGgpdsggEDLREDLARV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 221 QAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKvtPVLFEQPVHRDNWEGLSHVTRTAknrfGVSIAADESCRGLT 299
Cdd:cd03316 180 RAVReAVGPDVDLMVDANGRWDLAEAIRLARALEEYD--LFWFEEPVPPDDLEGLARLRQAT----SVPIAAGENLYTRW 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 300 DLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMvETRLAMGFSGHLAAGLGCFR-------FIDLDT 371
Cdd:cd03316 254 EFRDLLEAGAVDIIQPDVTKVgGITEAKKIAALAEAHGVRVAPHGA-GGPIGLAASLHLAAALPNFGileyhldDLPLRE 332
|
330
....*....|...
gi 18401824 372 PLLLADDPVQGGY 384
Cdd:cd03316 333 DLFKNPPEIEDGY 345
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
197-399 |
1.38e-31 |
|
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: 119.59 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 197 YRKRGFETLKLKVGKN-LKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGL 274
Cdd:pfam13378 10 VEARGFRAFKLKVGGPdPEEDVERVRAVReAVGPGVDLMVDANGAWSVAEAIRLARALEELGLL--WIEEPVPPDDLEGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 275 SHVTRtaknRFGVSIAADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIELMIGGMvETRLAMGF 353
Cdd:pfam13378 88 ARLRR----ATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVgGITEALKIAALAEAFGVPVAPHSG-GGPIGLAA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18401824 354 SGHLAAGLGCFRFIDLDTPLLLADDPVQGGykacgavyEFKDEGGH 399
Cdd:pfam13378 163 SLHLAAAVPNLLIQEYFLDPLLLEDDLLTE--------PLEVEDGR 200
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
145-369 |
8.07e-26 |
|
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: 104.33 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 145 VRAGMEMAMIDAAAKSVRVPLWKLFGGASstittditipivspaeasvlaskyrKRGFETLklkvgknlkADIEVLQAIR 224
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGS-------------------------RDRVPAY---------GSIERVRAVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 225 -AVHPTCSFILDANEGYQTEEAVKVLETLheMKVTPVLFEQPVHRDNWEGLSHVTRTAknrfGVSIAADESCRGLTDLKK 303
Cdd:cd00308 89 eAFGPDARLAVDANGAWTPKEAIRLIRAL--EKYGLAWIEEPCAPDDLEGYAALRRRT----GIPIAADESVTTVDDALE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18401824 304 IIEGNIVDVVNIKLAK-TGILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGLGCFRFIDL 369
Cdd:cd00308 163 ALELGAVDILQIKPTRvGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
60-378 |
4.79e-22 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 95.97 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 60 LLSPFTIASSRLDSVSNVAIRIElNDGFVGWGEAPILP-------SVTAedQIMAMVkareaseflrelPEMKLGNVLQE 132
Cdd:PRK15129 13 LHTPFVIARGSRSEARVVVVELE-EEGIKGTGECTPYPrygesdaSVMA--QIMSVV------------PQLEKGLTREA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 133 IGRFLPGhqfASVRAGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIV-SPAEASVLASKYRKRGFETLKLKVGK 211
Cdd:PRK15129 78 LQKLLPA---GAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIgTPEQMANSASALWQAGAKLLKVKLDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 212 NLKAdiEVLQAIRAVHPTCSFILDANEGYQTEEAVKVLETLHEMKVtpVLFEQPVHRDNWEGLSHVTRTaknrfgVSIAA 291
Cdd:PRK15129 155 HLIS--ERMVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGV--AMLEQPLPAQDDAALENFIHP------LPICA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 292 DESCRGLTDLKKiIEGNiVDVVNIKLAKTGIL-ESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGLgcfRFIDLD 370
Cdd:PRK15129 225 DESCHTRSSLKA-LKGR-YEMVNIKLDKTGGLtEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQV---RFADLD 299
|
....*...
gi 18401824 371 TPLLLADD 378
Cdd:PRK15129 300 GPTWLAVD 307
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
190-279 |
3.92e-20 |
|
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: 84.64 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 190 ASVLASKYRKRGFETLKLKVGKNLKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHR 268
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVReAVGPDADLMVDANGAWTAEEAIRALEALDELGLE--WIEEPVPP 82
|
90
....*....|.
gi 18401824 269 DNWEGLSHVTR 279
Cdd:smart00922 83 DDLEGLAELRR 93
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
60-362 |
2.16e-18 |
|
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: 84.23 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 60 LLSPFTIASSRLDSVSNVAIRIELNDGFVGWGE-APIlpsvtaedqimamvkareaseflrelpemklgnvlqeigrflp 138
Cdd:cd03320 10 LSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGEiAPL------------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 139 ghqfaSVRAGMEMAMIDAAAKSVRVPLWK--------LFGGasstittditipivsPAEASVLASKYRKRGFETLKLKVG 210
Cdd:cd03320 47 -----PLAFGIESALANLEALLVGFTRPRnripvnalLPAG---------------DAAALGEAKAAYGGGYRTVKLKVG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 211 K-NLKADIEVLQAIRAVHPT-CSFILDANEGYQTEEAVKVLETLHEMKVTPVlfEQPVHRDNWEGLshvtrtAKNRFGVS 288
Cdd:cd03320 107 AtSFEEDLARLRALREALPAdAKLRLDANGGWSLEEALAFLEALAAGRIEYI--EQPLPPDDLAEL------RRLAAGVP 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401824 289 IAADESCRGLTDLKKIIEGNIVDVVNIKLAKTG-ILESLEVIELARSSGIELMIGGMVETRLAMGFSGHLAAGLG 362
Cdd:cd03320 179 IALDESLRRLDDPLALAAAGALGALVLKPALLGgPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALP 253
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
77-339 |
4.75e-13 |
|
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: 69.66 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 77 VAIRIELNDGFVGWGEaPILPSVTAedQIMAMVKarEASEFL---RELPEMKLGNVLQEIGRFLPGHQFASVRAGMEMAM 153
Cdd:cd03325 15 LFVKIETDEGVVGWGE-PTVEGKAR--TVEAAVQ--ELEDYLigkDPMNIEHHWQVMYRGGFYRGGPVLMSAISGIDQAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 154 IDAAAKSVRVPLWKLFGGAS-STITTDITIPIVSPAEASVLASKYRKRGFETLK---------LKVGKNLKADIEVLQAI 223
Cdd:cd03325 90 WDIKGKVLGVPVHQLLGGQVrDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 224 R-AVHPTCSFILDANeGYQTEEAVKVL-ETLHEMKvtPVLFEQPVHRDNWEGLSHVTrtakNRFGVSIAADESCRGLTDL 301
Cdd:cd03325 170 ReAVGPDIDIGVDFH-GRVSKPMAKDLaKELEPYR--LLFIEEPVLPENVEALAEIA----ARTTIPIATGERLFSRWDF 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 18401824 302 KKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIEL 339
Cdd:cd03325 243 KELLEDGAVDIIQPDISHAgGITELKKIAAMAEAYDVAL 281
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
193-337 |
5.84e-12 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta 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: 239440 [Multi-domain] Cd Length: 415 Bit Score: 66.98 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 193 LASKYRKRGFETLKLKVGKNLKADIEVLQAIRAV-HPTCSFILDANEGYQTEEAVKVLETLHEMKvtPVLFEQPVHRDNW 271
Cdd:cd03324 203 LCKEALAQGFTHFKLKVGADLEDDIRRCRLAREViGPDNKLMIDANQRWDVPEAIEWVKQLAEFK--PWWIEEPTSPDDI 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401824 272 EGlsHVT-RTAKNRFGVSIAADESCRGLTDLKKIIEGNIVDVVNIKLAKTG-ILESLEVIELARSSGI 337
Cdd:cd03324 281 LG--HAAiRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGgVNENLAVLLMAAKFGV 346
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
46-409 |
1.79e-11 |
|
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: 65.20 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 46 VRVLKAENRELNVALLSPFTIASSRLDSVSNVAIRIELNDGFVG------WGEAPILPSVTAEDQIMAMVKAREASEFLR 119
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGhsylftYTPAALKSLKQLLDDMAALLVGEPLAPAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 120 ElpeMKLGnvlqeiGRF-LPGHQfASVR---AGMEMAMIDAAAKSVRVPLWKLFGGASSTITTDITIPIVSPAEASVLAS 195
Cdd:cd03321 81 E---RALA------KRFrLLGYT-GLVRmaaAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATERAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 196 KYRKRGFETLKLKVGK-NLKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTPVlfEQPVHRDNWEG 273
Cdd:cd03321 151 TAAEEGFHAVKTKIGYpTADEDLAVVRSIRqAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWI--EEPTLQHDYEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 274 lsHVTRTAKNRFGVSIAadESCRGLTDLKKIIEGNIVDVVNIKLAKTGILES-LEVIELARSSGIELmiggmvETRLAMG 352
Cdd:cd03321 229 --HARIASALRTPVQMG--ENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGwLRASALAEQAGIPM------SSHLFQE 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 353 FSGHLAAGLGC---FRFIDLDTPLLLADDPVQGGYKACGavyefkDEGGHGgyLQWNDVA 409
Cdd:cd03321 299 ISAHLLAVTPTahwLEYVDWAGAILEPPLKFEDGNAVIP------DEPGNG--IIWREKA 350
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
28-247 |
2.35e-11 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 66.03 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 28 ITVMSKTSKFKTLTENFTV-RVLKAENRELNVALLSPFTIASSRLDSV--SNVAIRIELNDGFVGWGE-APILPSVT--- 100
Cdd:PLN02980 912 LGILSESSCLHSIIDGVFLcKISGMEYSLYRIQLCAPPTSASVDFSQFhrEGFILSLSLEDGSVGFGEvAPLEIHEEdll 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 101 -AEDQIMAMVKAREASEFLRELPEMKlGNVLQEIGRFL---PGHQFASVRAGMEMAMIDAAAKSVRVPLWKLFGGASSTI 176
Cdd:PLN02980 992 dVEEQLRFLLHVIKGAKISFMLPLLK-GSFSSWIWSELgipPSSIFPSVRCGLEMAILNAIAVRHGSSLLNILDPYQKDE 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 177 TTDITIPIV----------SPAEASVLASKYRKRGFETLKLKVGKNLKA--DIEVLQAIR-AVHPTCSFILDANEGYQTE 243
Cdd:PLN02980 1071 NGSEQSHSVqicalldsngSPLEVAYVARKLVEEGFSAIKLKVGRRVSPiqDAAVIQEVRkAVGYQIELRADANRNWTYE 1150
|
....
gi 18401824 244 EAVK 247
Cdd:PLN02980 1151 EAIE 1154
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
201-339 |
4.04e-10 |
|
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: 60.89 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 201 GFETLKLKVGKNLKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQPVHRDNWEGLSHVTr 279
Cdd:cd03328 153 GIPRVKMKIGRDPRRDPDRVAAARrAIGPDAELFVDANGAYSRKQALALARAFADEGVT--WFEEPVSSDDLAGLRLVR- 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401824 280 tAKNRFGVSIAADESCRGLTDLKKIIEGNIVDVVNIKLAKT-GILESLEVIELARSSGIEL 339
Cdd:cd03328 230 -ERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCgGVTGFLQAAALAAAHHVDL 289
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
185-377 |
8.22e-10 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 59.60 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 185 VSPAEASVLASKYRkrGFETLKLKV---GKNLKADIEVLQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTPV 260
Cdd:PRK02901 88 VDAAQVPEVLARFP--GCRTAKVKVaepGQTLADDVARVNAVRdALGPDGRVRVDANGGWSVDEAVAAARALDADGPLEY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 261 LfEQP---VhrdnwEGLSHVTRtaknRFGVSIAADESCRGLTDLKKIIEGNIVDVVNIKLAKTGILESleVIELARSSGI 337
Cdd:PRK02901 166 V-EQPcatV-----EELAELRR----RVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRA--ALDIAEQIGL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18401824 338 ELMIGGMVETRLAMGFSGHLAA---------GLGCFRFI--DLDTPLLLAD 377
Cdd:PRK02901 234 PVVVSSALDTSVGIAAGLALAAalpeldhacGLATGGLFeeDVADPLLPVD 284
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
79-362 |
1.08e-09 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 59.26 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 79 IRIELNDGFVGWGE-APIlPSVTAEDqimamvkAREASEFLRELPEMKLGNVLQEIGRFLPGHQFasvraGMEMAMIDAA 157
Cdd:PRK02714 33 LRLTDETGKIGWGEiAPL-PWFGSET-------LEEALAFCQQLPGEITPEQIFSIPDALPACQF-----GFESALENES 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 158 aksvrvplwklfGGASSTITTDITIPIVSPAEASVLA--SKYRKRGFETLKLKVG-KNLKADIEVLQA-IRAVHPTCSFI 233
Cdd:PRK02714 100 ------------GSRSNVTLNPLSYSALLPAGEAALQqwQTLWQQGYRTFKWKIGvDPLEQELKIFEQlLERLPAGAKLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 234 LDANEGYQTEEAVKVLETLHEMKVTPVLF-EQPVHRDNWEGLSHVTRTaknrFGVSIAADESCRGLTDLKKIIEGNIVDV 312
Cdd:PRK02714 168 LDANGGLSLEEAKRWLQLCDRRLSGKIEFiEQPLPPDQFDEMLQLSQD----YQTPIALDESVANLAQLQQCYQQGWRGI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18401824 313 VNIKLAKTGILESLEviELARSSGIELMIGGMVETRLAMGFSGHLAAGLG 362
Cdd:PRK02714 244 FVIKPAIAGSPSRLR--QFCQQHPLDAVFSSVFETAIGRKAALALAAELS 291
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
61-170 |
1.59e-07 |
|
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: 49.39 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 61 LSPFTIASSRLDSVSNVAIRIELNDGFVGWGEAPILPSVT------AEDQIMAMVKAREASeflrelpemKLGNVLQEIG 134
Cdd:pfam02746 13 LRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGGRAetikaiLDDHLAPLLIGRDAA---------NISDLWQLMY 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 18401824 135 RFLPGHQFAsvRAGMEMAMIDAAAKSVRVPLWKLFG 170
Cdd:pfam02746 84 RAALGNMSA--KAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
150-265 |
4.04e-04 |
|
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: 42.38 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401824 150 EMAMIDAAAKSVRVPLWKLFGG--------ASSTITTDITIPIvSPAEASVLASKYRKRGFETLKLK--VGKNLKADIEV 219
Cdd:cd03329 100 DIALWDLAGKYLGLPVHRLLGGyrekipayASTMVGDDLEGLE-SPEAYADFAEECKALGYRAIKLHpwGPGVVRRDLKA 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18401824 220 LQAIR-AVHPTCSFILDANEGYQTEEAVKVLETLHEMKVTpvLFEQP 265
Cdd:cd03329 179 CLAVReAVGPDMRLMHDGAHWYSRADALRLGRALEELGFF--WYEDP 223
|
|
| |
