|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-362 |
1.72e-77 |
|
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: 243.29 E-value: 1.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 2 KIDAVDLFYLSMPEVT-DAADGSQDALLVRV-AAGGHIGWGECEAAPLPSIAAfvcpksHGVCRPVSDSVLGQRLDGPDD 79
Cdd:cd03316 1 KITDVETFVLRVPLPEpGGAVTWRNLVLVRVtTDDGITGWGEAYPGGRPSAVA------AAIEDLLAPLLIGRDPLDIER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 80 IARIAALVGYNSMDLLQAPHMLSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLL-FGDTPQETLERARAARRDG 158
Cdd:cd03316 75 LWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGgYDDSPEELAEEAKRAVAEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 159 FAAVKFGWG--PIGRGTVAADADQIMAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVLWLEEPFDAGALAAH 236
Cdd:cd03316 155 FTAVKLKVGgpDSGGEDLREDLARVRAVREAVGPDVDLMVDANGRW--DLAEAIRLARALEEYDLFWFEEPVPPDDLEGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 237 AALAGRGaRVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTFTSHLALSASLQP 316
Cdd:cd03316 233 ARLRQAT-SVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 500165465 317 FAGLEADRICEYPAAPQQLALDITGDHIRPDgEGLIRAPEAPGLGL 362
Cdd:cd03316 312 AAALPNFGILEYHLDDLPLREDLFKNPPEIE-DGYVTVPDRPGLGV 356
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-372 |
4.20e-67 |
|
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: 216.61 E-value: 4.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 1 MKIDAVDLFYLSMPEVT-----DAADGSQDALLVRV-AAGGHIGWGECEAAPLPSIAAFvcpksHGVCRPVSDSVLGQrl 74
Cdd:COG4948 1 MKITDIEVYPVRLPLKRpftisRGTRTERDVVLVRVeTDDGITGWGEAVPGGTGAEAVA-----AALEEALAPLLIGR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 75 dGPDDIARIAALVgynsMDLLQAPHM-LSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLLFgDTPQETLERARA 153
Cdd:COG4948 74 -DPLDIEALWQRL----YRALPGNPAaKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGI-DTPEEMAEEARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 154 ARRDGFAAVKFGwgpIGRGTVAADADQIMAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVLWLEEPFdAGAL 233
Cdd:COG4948 148 AVARGFRALKLK---VGGPDPEEDVERVRAVREAVGPDARLRVDANGAW--TLEEAIRLLRALEDLGLEWIEQPL-PAED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 234 AAHAALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHT-FTSHLALSA 312
Cdd:COG4948 222 LEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCmLESGIGLAA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 313 SLQPFAGLEADRICEYPAAPqQLALDITGDHIRPDGeGLIRAPEAPGLGLQVAASALRRY 372
Cdd:COG4948 302 ALHLAAALPNFDIVELDGPL-LLADDLVEDPLRIED-GYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
146-364 |
7.37e-41 |
|
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: 143.86 E-value: 7.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 146 ETLERARAARRD-GFAAVKFGwgpIGRGTVAADADQIMAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVLWL 224
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLK---VGGPDPEEDVERVRAVREAVGPGVDLMVDANGAW--SVAEAIRLARALEELGLLWI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 225 EEPFDAGALAAHAALAGRGaRVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTF 304
Cdd:pfam13378 76 EEPVPPDDLEGLARLRRAT-PVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 305 TSHLALSASLQPFAGLEADRICEYPAAPQQLALDITGDHIRPDGeGLIRAPEAPGLGLQV 364
Cdd:pfam13378 155 GGPIGLAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVED-GRVAVPDGPGLGVEL 213
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
99-362 |
7.97e-28 |
|
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: 112.04 E-value: 7.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 99 HMLSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLLFGDTPQETLERARAARRDGFAAVK--FGWGPI-GRGTVA 175
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEYLKEGYRGMKmrFGYGPSdGHAGLR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 176 ADADQIMAAREGLGPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVLWLEEP-----FDagalaaHAALAGRGARVRIAG 250
Cdd:cd03327 156 KNVELVRAIREAVGYDVDLMLDCYM--SWNLNYAIKMARALEKYELRWIEEPlipddIE------GYAELKKATGIPIST 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 251 GEaaHNFHM--AQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHT---FTSHLALSASLQPFAgleadri 325
Cdd:cd03327 228 GE--HEYTVygFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHAsqiYNYHFIMSEPNSPFA------- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 500165465 326 cEY-PAAPQQLALDITGDHIrpDGE-----GLIRAPEAPGLGL 362
Cdd:cd03327 299 -EYlPNSPDEVGNPLFYYIF--LNEpvpvnGYFDLSDKPGFGL 338
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
101-364 |
1.86e-23 |
|
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: 100.09 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 101 LSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYaSLLFGDTPQETLERARAARRDGFAAVKFGW-GPIGR----GTVA 175
Cdd:cd03325 82 ISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVY-SWIGGDRPSDVAEAARARREAGFTAVKMNAtEELQWidtsKKVD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 176 ADADQIMAAREGLGPDGDLMVDvgqIFGEDVEAAAARLPT-LDAAGVLWLEEPFdAGALAAHAALAGRGARVRIAGGEAA 254
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVD---FHGRVSKPMAKDLAKeLEPYRLLFIEEPV-LPENVEALAEIAARTTIPIATGERL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 255 HNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTFTSHLALSASLQPFAgleadriCEYPAAPQQ 334
Cdd:cd03325 237 FSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDA-------STPNFLIQE 309
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500165465 335 LALDIT---GDHIRPDG---------EGLIRAPEAPGLGLQV 364
Cdd:cd03325 310 QSLGIHyneGDDLLDYLvdpevfdmeNGYVKLPTGPGLGIEI 351
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-371 |
9.41e-20 |
|
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: 89.68 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 2 KIDAVDLFYLSMPEV-----TDAADGSQDALLVRV-AAGGHIGWGECeaapLPSIAAFVCPKSHGVCRPVSDSVLGQRLD 75
Cdd:cd03318 1 KIEAIETTIVDLPTRrphqfAGTTMHTQSLVLVRLtTSDGVVGIGEA----TTPGGPAWGGESPETIKAIIDRYLAPLLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 76 G--PDDIARIAALvgynsMDLLQAPHML--SGIEMALWDLLGRRLSAPAWALLGysanhGKR----PYA-SLLFGDTPQ- 145
Cdd:cd03318 77 GrdATNIGAAMAL-----LDRAVAGNLFakAAIEMALLDAQGRRLGLPVSELLG-----GRVrdslPVAwTLASGDTERd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 146 -ETLERARAARRDGFAAVKfgwgpIGRGTVAADADQIMAAREGLGPDGDLMVDVGQIFGEDVeaAAARLPTLDAAGVLWL 224
Cdd:cd03318 147 iAEAEEMLEAGRHRRFKLK-----MGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDEST--AIRALPRLEAAGVELI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 225 EEPFdAGALAAHAALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGI-TYVNHT 303
Cdd:cd03318 220 EQPV-PRENLDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIaLYGGTM 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500165465 304 FTSHLALSASLQPFAGLEA-DRICEYpAAPQQLALDITGDHIRPDgEGLIRAPEAPGLGLQVAASALRR 371
Cdd:cd03318 299 LESSIGTAASAHLFATLPSlPFGCEL-FGPLLLAEDLLEEPLAYR-DGELHVPTGPGLGVRLDEDKVRR 365
|
|
| 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 ... |
25-325 |
7.50e-19 |
|
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: 86.47 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 25 DALLVRVAAGGHIGWGECeaAPLPSIAAfvcpKSHGVCRPVSDSVLGQRLDGPDDIARIAALVGyNSMDLLQAPhmLSGI 104
Cdd:cd03319 26 ENVIVEIELDGITGYGEA--APTPRVTG----ETVESVLAALKSVRPALIGGDPRLEKLLEALQ-ELLPGNGAA--RAAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 105 EMALWDLLGRRLSAPAWALLGySANHGKRPYASLLFGDTPQETLERARAARRDGFAAVKFGWGpigrGTVAADADQIMAA 184
Cdd:cd03319 97 DIALWDLEAKLLGLPLYQLWG-GGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLG----GDLEDDIERIRAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 185 REGLgPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVLWLEEPFdAGALAAHAALAGRGARVRIAGGEAAHNFHMAQHLM 264
Cdd:cd03319 172 REAA-PDARLRVDANQ--GWTPEEAVELLRELAELGVELIEQPV-PAGDDDGLAYLRDKSPLPIMADESCFSAADAARLA 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500165465 265 DYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITY-VNHTFTSHLALSASLQpFAGLEADRI 325
Cdd:cd03319 248 GGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVmVGCMVESSLSIAAAAH-LAAAKADFV 308
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
100-364 |
4.30e-18 |
|
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: 84.76 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 100 MLSGIEMALWDLLGRRLSAPAWALLGysANHGKRP-YASLLFGD------TPQETLERARAARRDGFAAVKF-GWGPigr 171
Cdd:cd03329 95 GLGLVDIALWDLAGKYLGLPVHRLLG--GYREKIPaYASTMVGDdlegleSPEAYADFAEECKALGYRAIKLhPWGP--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 172 GTVAADADQIMAAREGLGPDGDLMVDVgqiFGEDVEAAAARL-PTLDAAGVLWLEEPFDaGALAAHAALAGRGARVRIAG 250
Cdd:cd03329 170 GVVRRDLKACLAVREAVGPDMRLMHDG---AHWYSRADALRLgRALEELGFFWYEDPLR-EASISSYRWLAEKLDIPILG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 251 GEAAHNFHMaqHLMDYGRIG---FIQIDCGRIGGLGPAKRVADAAQARGITY-VNHTFTSHLALSASLQP---FAGLEAD 323
Cdd:cd03329 246 TEHSRGALE--SRADWVLAGatdFLRADVNLVGGITGAMKTAHLAEAFGLDVeLHGNGAANLHVIAAIRNtryYERGLLH 323
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500165465 324 RICEYPA-APQQLALDitgDHIrpDGEGLIRAPEAPGLGLQV 364
Cdd:cd03329 324 PSQKYDVyAGYLSVLD---DPV--DSDGFVHVPKGPGLGVEI 360
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
101-371 |
8.65e-18 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 84.18 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 101 LSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYaSLLFGDTPQETLERARAARRDGFAAVKF-GWGPIGR----GTVA 175
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVY-SWIGGDRPADVAEAARARVERGFTAVKMnGTEELQYidspRKVD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 176 ADADQIMAAREGLGPDGDLMVDvgqiFGEDVEAAAAR--LPTLDAAGVLWLEEPFdAGALAAHAALAGRGARVRIAGGEA 253
Cdd:PRK14017 162 AAVARVAAVREAVGPEIGIGVD----FHGRVHKPMAKvlAKELEPYRPMFIEEPV-LPENAEALPEIAAQTSIPIATGER 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 254 AHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTFTSHLALSASLQPFAgleadriCEYPAAPQ 333
Cdd:PRK14017 237 LFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDA-------VSPNAFIQ 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 500165465 334 QLALDItgdHIRPDGE---------------GLIRAPEAPGLGLQVAASALRR 371
Cdd:PRK14017 310 EQSLGI---HYNQGADlldyvknkevfayedGFVAIPTGPGLGIEIDEAKVRE 359
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-371 |
3.32e-17 |
|
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: 81.90 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 6 VDLFYLSMPEVT--DAADGSQ---DALLVRV-AAGGHIGWGECEAAPLPS------------IAAFVCPKshgvcrpvsd 67
Cdd:cd03317 1 IELFHVRMPLKFpfETSFGTLnerEFLIVELtDEEGITGYGEVVAFEGPFyteetnatawhiLKDYLLPL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 68 sVLGQRLDGPDDIARIAALVGYNSMdllqaphMLSGIEMALWDLLGRRLSAPAWALLGysanhGKRPYA----SLLFGDT 143
Cdd:cd03317 71 -LLGREFSHPEEVSERLAPIKGNNM-------AKAGLEMAVWDLYAKAQGQSLAQYLG-----GTRDSIpvgvSIGIQDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 144 PQETLERARAARRDGFAAVKF----GWgpigrgtvaaDADQIMAAREGLgPDGDLMVDVGQIFgedVEAAAARLPTLDAA 219
Cdd:cd03317 138 VEQLLKQIERYLEEGYKRIKLkikpGW----------DVEPLKAVRERF-PDIPLMADANSAY---TLADIPLLKRLDEY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 220 GVLWLEEPFDaGALAAHAALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITY 299
Cdd:cd03317 204 GLLMIEQPLA-ADDLIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 300 -VNHTFTS------HLALsASLQPFAgleadriceYPAapqqlalDITG-------DHIRPDGE---GLIRAPEAPGLGL 362
Cdd:cd03317 283 wCGGMLESgigrahNVAL-ASLPNFT---------YPG-------DISAssryfeeDIITPPFElenGIISVPTGPGIGV 345
|
....*....
gi 500165465 363 QVAASALRR 371
Cdd:cd03317 346 TVDREALKK 354
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
102-327 |
8.40e-17 |
|
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: 79.69 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 102 SGIEMALWDLLGRRLSAPAWALLGysANHGKRPYASLLFGDTPQETLERARAARRDGFAAVKFgwgPIGRGTvAADADQI 181
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLG--GYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKL---KVGRDP-ARDVAVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 182 MAAREGLGPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVLWLEEPFDaGALAAHAALAGRGARVRIAGGEAAHNFHMAQ 261
Cdd:cd03315 120 AALREAVGDDAELRVDANR--GWTPKQAIRALRALEDLGLDYVEQPLP-ADDLEGRAALARATDTPIMADESAFTPHDAF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500165465 262 HLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGIT-YVNHTFTSHLALSASLQPFAGLEA-DRICE 327
Cdd:cd03315 197 RELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPvMVGSMIESGLGTLANAHLAAALRAvTLPGE 264
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
100-328 |
2.35e-15 |
|
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: 74.67 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 100 MLSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLlfgdtpqetleraraarrdgfAAVKfgwgpigrgtvaadad 179
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI---------------------ERVR---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 180 qimAAREGLGPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVLWLEEPFDaGALAAHAALAGRGARVRIAGGEAAHNFHM 259
Cdd:cd00308 86 ---AVREAFGPDARLAVDANG--AWTPKEAIRLIRALEKYGLAWIEEPCA-PDDLEGYAALRRRTGIPIAADESVTTVDD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 260 AQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGIT-YVNHTFTSHLALSASLQPFAGLEADRICEY 328
Cdd:cd00308 160 ALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRvMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
101-373 |
3.54e-15 |
|
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: 75.98 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 101 LSGIEMALWDLLGRRLSAPAWALLGYSAnhgkRP---YASLLFGDTPQETlERARAARRDGFAAVKFgwgPIGRGTVAAD 177
Cdd:cd03321 101 AAGIDMAAWDALAKVHGLPLAKLLGGNP----RPvqaYDSHGLDGAKLAT-ERAVTAAEEGFHAVKT---KIGYPTADED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 178 ADQIMAAREGLGPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVLWLEEPFdAGALAAHAALAGRGARVRIAGGEAAHNF 257
Cdd:cd03321 173 LAVVRSIRQAVGDGVGLMVDYNQ--SLTVPEAIERGQALDQEGLTWIEEPT-LQHDYEGHARIASALRTPVQMGENWLGP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 258 HMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTFTShlaLSASLqpfagleadrICEYPAAPQQLAL 337
Cdd:cd03321 250 EEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQE---ISAHL----------LAVTPTAHWLEYV 316
|
250 260 270
....*....|....*....|....*....|....*....
gi 500165465 338 DITGDHIRPDGE---GLIRAPEAPGLGLQVAASALRRYL 373
Cdd:cd03321 317 DWAGAILEPPLKfedGNAVIPDEPGNGIIWREKAVRKYL 355
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
2-367 |
5.83e-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: 72.44 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 2 KIDAVDLFYLSMPEVTDAADG-----SQDALLVRVAAGGH--IGWGECEAaplpSIAAFVcpksHGVcrpVSDSVLGQR- 73
Cdd:cd03328 1 AVERVEARAYTVPTDAPEADGtlawdATTLVLVEVRAGGRtgLGYTYADA----AAAALV----DGL---LAPVVEGRDa 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 74 LDGPDDIARIAALVGYNSMDLLQApHMLSGIEMALWDLLGRRLSAPAWALLGysANHGKRP-YASLLFGDTPQETL-ERA 151
Cdd:cd03328 70 LDPPAAWEAMQRAVRNAGRPGVAA-MAISAVDIALWDLKARLLGLPLARLLG--RAHDSVPvYGSGGFTSYDDDRLrEQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 152 RAARRDGFAAVKFgwgPIGRGTvAADADQIMAAREGLGPDGDLMVDVGQIFGedVEAAAARLPTLDAAGVLWLEEPFDAG 231
Cdd:cd03328 147 SGWVAQGIPRVKM---KIGRDP-RRDPDRVAAARRAIGPDAELFVDANGAYS--RKQALALARAFADEGVTWFEEPVSSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 232 -ALAAHAALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGItyvnhTFTSHLAL 310
Cdd:cd03328 221 dLAGLRLVRERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHV-----DLSAHCAP 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500165465 311 SASLQPFAGLEADRICEY---PAAPQQL----ALDITGDHIRPDgegliraPEAPGLGLQVAAS 367
Cdd:cd03328 296 ALHAHVACAVPRLRHLEWfhdHVRIERMlfdgAPDPSGGALRPD-------LSRPGLGLELRAR 352
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
107-328 |
2.43e-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: 67.75 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 107 ALWDLLGRRLSAPAWALLgysANHGKRPYASLL----FGD--TPQETLE-----------RARAARRDGFA--------- 160
Cdd:cd03324 117 AVWDLWAKAEGKPLWKLL---VDMTPEELVSCIdfryITDalTPEEALEilrrgqpgkaaREADLLAEGYPayttsagwl 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 161 -------------AVKFGWGPIgRGTVAAD-ADQI---MAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVLW 223
Cdd:cd03324 194 gysdeklrrlckeALAQGFTHF-KLKVGADlEDDIrrcRLAREVIGPDNKLMIDANQRW--DVPEAIEWVKQLAEFKPWW 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 224 LEEPF--DAGALAAHAALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGG--------LGPAK---RVAD 290
Cdd:cd03324 271 IEEPTspDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGvnenlavlLMAAKfgvPVCP 350
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 500165465 291 AAQARGI-TYVNH-TFTSHLALSASLqpfagleADRICEY 328
Cdd:cd03324 351 HAGGVGLcELVQHlSMIDYICVSGSK-------EGRVIEY 383
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
101-318 |
2.95e-10 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 61.28 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 101 LSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYAsllfgdtpqeTLERARAARRDGFAAVKFG--WGPI-GRGTVAAD 177
Cdd:PRK15440 125 ISCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFYA----------TGARPDLAKEMGFIGGKMPlhHGPAdGDAGLRKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 178 ADQIMAAREGLGPDGDLMVDVGqiFGEDVEAAAARLPTLDAAGVLWLEEPFDAGALAAHAALAGRGAR-VRIAGGEAAHN 256
Cdd:PRK15440 195 AAMVADMREKVGDDFWLMLDCW--MSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAgMMVTSGEHEAT 272
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500165465 257 FHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNH---TFTSHLALSASLQPFA 318
Cdd:PRK15440 273 LQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHgssVYSHHFVITRTNSPFS 337
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
101-372 |
4.94e-10 |
|
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: 60.53 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 101 LSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLLfGDTPQETLERARAARRDGFAAVKfgwgpigrgtvAADADQ 180
Cdd:cd03322 85 IAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHAS-GRDIPELLEAVERHLAQGYRAIR-----------VQLPKL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 181 IMAAREGLGPDGDLMVDVGQ--------IFGEDVEAAaaRLptldaagvLWLEEPFDAGALAAHAALAGRGArVRIAGGE 252
Cdd:cd03322 153 FEAVREKFGFEFHLLHDVHHrltpnqaaRFGKDVEPY--RL--------FWMEDPTPAENQEAFRLIRQHTA-TPLAVGE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 253 AAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNH--TFTSHLALSASLQPFAGLEADRICEYPA 330
Cdd:cd03322 222 VFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHgpTDLSPVGMAAALHLDLWVPNFGIQEYMR 301
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500165465 331 APQQlALDITGDHIRPDgEGLIRAPEAPGLGLQVAASALRRY 372
Cdd:cd03322 302 HAEE-TLEVFPHSVRFE-DGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
144-228 |
5.17e-10 |
|
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: 56.14 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 144 PQETLERARAARRD-GFAAVKFGWGpigrGTVAADADQIMAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVL 222
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVG----GGPLEDLARVAAVREAVGPDADLMVDANGAW--TAEEAIRALEALDELGLE 74
|
....*.
gi 500165465 223 WLEEPF 228
Cdd:smart00922 75 WIEEPV 80
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
97-315 |
5.38e-10 |
|
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: 59.58 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 97 APHML-SGIEMALWDLLGRRLSAPAWALlgysanhgKRPYASLLFGDTPQEtLERARAARRDGFAAVKFgwgPIGRGTVA 175
Cdd:cd03320 44 APLPLaFGIESALANLEALLVGFTRPRN--------RIPVNALLPAGDAAA-LGEAKAAYGGGYRTVKL---KVGATSFE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 176 ADADQIMAAREGLGPDGDLMVDVGQIFgeDVEAAAARLPTLDAAGVLWLEEPFDAGALAAHAALAGRgarVRIAGGEAAH 255
Cdd:cd03320 112 EDLARLRALREALPADAKLRLDANGGW--SLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAG---VPIALDESLR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500165465 256 NFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYV-NHTFTSHLALSASLQ 315
Cdd:cd03320 187 RLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVvSSALESSIGLGALAH 247
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
99-363 |
7.32e-06 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. 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: 239442 [Multi-domain] Cd Length: 385 Bit Score: 47.77 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 99 HMLSGIEMALWDLLGRRLSAPAWALLGYSANHGKRPYASLLFGD----TPQETLERARAARRD----GFAAVKFgwgPIG 170
Cdd:cd03326 108 VAVGALDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAAggyyYPGDDLGRLRDEMRRyldrGYTVVKI---KIG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 171 RGTVAADADQIMAAREGLGPDGDLMVDVGQIFGEDVEAAAARlpTLDAAGVLWLEEPFDAGALAAHAALAGRGARVrIAG 250
Cdd:cd03326 185 GAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAK--ALAPYGLRWYEEPGDPLDYALQAELADHYDGP-IAT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 251 GEAAHNFHMAQHLMDYGRI----GFIQIDCGRIGGLGPAKRVADAAQARG------ITYVNHTFTSHLALSASLqpfAGL 320
Cdd:cd03326 262 GENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGwsrrrfFPHGGHLMSLHIAAGLGL---GGN 338
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 500165465 321 EAdriceYPAAPQqlALDITGDHIRPDGeGLIRAPEAPGLGLQ 363
Cdd:cd03326 339 ES-----YPDVFQ--PFGGFADGCKVEN-GYVRLPDAPGIGFE 373
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
22-125 |
1.77e-04 |
|
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: 40.92 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 22 GSQDALLVRVA-AGGHIGWGECEAAPlpsiaafvcpkshgvcrPVSDSVLGQRLD--GPDDIARIAALVGYNSMDLLQA- 97
Cdd:pfam02746 24 QQQSLVIVRIEtSEGVVGIGEATSYG-----------------GRAETIKAILDDhlAPLLIGRDAANISDLWQLMYRAa 86
|
90 100 110
....*....|....*....|....*....|.
gi 500165465 98 -PHM--LSGIEMALWDLLGRRLSAPAWALLG 125
Cdd:pfam02746 87 lGNMsaKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
35-372 |
1.53e-03 |
|
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: 40.38 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 35 GHIGWGECE------AAPLPSIAAFVCPKSHGVCRPVSDSVLGQRLDgpddiaRIAALVGYNSMDLLQAPHMLSGIEMAL 108
Cdd:cd03323 40 GNTGVGESPggaealEALLEAARSLVGGDVFGAYLAVLESVRVAFAD------RDAGGRGLQTFDLRTTVHVVTAFEVAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 109 WDLLGRRLSAPAWALLG--------------YSANHGKRPYASLLFGD------TPQETLERARAAR-RDGFAAVKFgwg 167
Cdd:cd03323 114 LDLLGQALGVPVADLLGggqrdsvpflaylfYKGDRHKTDLPYPWFRDrwgealTPEGVVRLARAAIdRYGFKSFKL--- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 168 pigRGTVAADADQIMA----------AREGLGPDGDLMVDVGQIFGEDVEaaaarlptldaaGVL-WLEEPfdaGALAAH 236
Cdd:cd03323 191 ---KGGVLPGEEEIEAvkalaeafpgARLRLDPNGAWSLETAIRLAKELE------------GVLaYLEDP---CGGREG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 237 AALAGRGARVRIAGGEAAHNFHMAQHLMDYGRIGFIQIDCGRIGGLGPAKRVADAAQARGITYVNHTfTSHLALsaSLQP 316
Cdd:cd03323 253 MAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHS-NNHLGI--SLAM 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500165465 317 FAGLEADRICEYPAA----PQQLALDITGDHIRPDGeGLIRAPEAPGLGLQVAASALRRY 372
Cdd:cd03323 330 MTHVAAAAPGLITACdthwIWQDGQVITGEPLRIKD-GKVAVPDKPGLGVELDRDKLAKA 388
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
173-227 |
7.07e-03 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 38.03 E-value: 7.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 500165465 173 TVAADADQIMAAREGLGPDGDLMVDVGQifGEDVEAAAARLPTLDAAGVL-WLEEP 227
Cdd:PRK02901 116 TLADDVARVNAVRDALGPDGRVRVDANG--GWSVDEAVAAARALDADGPLeYVEQP 169
|
|
| |
