|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-366 |
8.15e-118 |
|
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: 346.52 E-value: 8.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 2 KIDRMRVFMTR---------DKDRPRVIVALDTDDGLTGWGECYNHGPDKALPPIL-DYLYGFLSGQDPTRIDYLVNLLI 71
Cdd:cd03316 1 KITDVETFVLRvplpepggaVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIeDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 72 QQSRF-PPGALGLSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYAGVYTAPDAPAARDEFDRLNAEWGFTAFKL 150
Cdd:cd03316 81 RRLFWrGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 151 SPWRVDIHahrwGNVVKASADYFRSLRETVRDDYEIAFDAHaQIFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDL 230
Cdd:cd03316 161 KVGGPDSG----GEDLREDLARVRAVREAVGPDVDLMVDAN-GRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 231 KQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPMGPLATAVNVHFSAAT 310
Cdd:cd03316 236 RQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAAL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
4JN7_A 311 QNFRILEYrlpkgqayvyggkDIEKRQGETRYVVDPYLPKDGYLELrPDRPGWGVE 366
Cdd:cd03316 316 PNFGILEY-------------HLDDLPLREDLFKNPPEIEDGYVTV-PDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-374 |
3.53e-95 |
|
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: 288.64 E-value: 3.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 1 MKIDRMRVF-------------MTRDKDRPRVIVALDTDDGLTGWGEC--YNHGPDKALPPILDYLYGFLSGQDPTRIDY 65
Cdd:COG4948 1 MKITDIEVYpvrlplkrpftisRGTRTERDVVLVRVETDDGITGWGEAvpGGTGAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 66 LVNLLIQQSRFPPgalglSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYAGVyTAPDAPAARDEFDRLNAEwGF 145
Cdd:COG4948 81 LWQRLYRALPGNP-----AAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATL-GIDTPEEMAEEAREAVAR-GF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 146 TAFKLspwrvDIHAHRWGNVVKAsadyFRSLRETVRDDYEIAFDAHaQIFEPVAARQLGNALAPYDPLFYEEPLRPENID 225
Cdd:COG4948 154 RALKL-----KVGGPDPEEDVER----VRAVREAVGPDARLRVDAN-GAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 226 MWGDLKQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPM-GPLATAVNV 304
Cdd:COG4948 224 GLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 305 HFSAATQNFRILEYRLPKGQAyvyggKDIekrqgetryVVDPYLPKDGYLELrPDRPGWGVEMDEKAMEE 374
Cdd:COG4948 304 HLAAALPNFDIVELDGPLLLA-----DDL---------VEDPLRIEDGYLTV-PDGPGLGVELDEDALAR 358
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-393 |
1.95e-93 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 285.25 E-value: 1.95e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 1 MKIDRMRVFMTRdkdrPR-VIVALDTDDGLTGWGECYNHGPDKALPPILDYLYGFLSGQDPTRIDYLVNLLIQQSRFPPG 79
Cdd:PRK14017 1 MKITKLETFRVP----PRwLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGGFYRGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 80 ALGLSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYA---GVYTAPDAPAARDEFDRlnaewGFTAFKL---SPW 153
Cdd:PRK14017 77 PILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSwigGDRPADVAEAARARVER-----GFTAVKMngtEEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 154 RVdIHAHRWgnvVKASADYFRSLRETVRDDYEIAFDAHAQIFEPVAaRQLGNALAPYDPLFYEEPLRPENIDMWGDLKQG 233
Cdd:PRK14017 152 QY-IDSPRK---VDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMA-KVLAKELEPYRPMFIEEPVLPENAEALPEIAAQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 234 LNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPMGPLATAVNVHFSAATQNF 313
Cdd:PRK14017 227 TSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 314 RILEYRLpkgqayvyggkDIEKRQGETR--YVVDP--YLPKDGYLElRPDRPGWGVEMDEKAMEEEGYI--HWQRRVPKR 387
Cdd:PRK14017 307 FIQEQSL-----------GIHYNQGADLldYVKNKevFAYEDGFVA-IPTGPGLGIEIDEAKVRERAKTghDWRNPVWRH 374
|
....*.
4JN7_A 388 PDGSYA 393
Cdd:PRK14017 375 ADGSVA 380
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-368 |
3.61e-92 |
|
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: 280.75 E-value: 3.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 2 KIDRMRVFMTRdkdRPRVIVALDTDDGLTGWGECYNHGPDKALPPILDYLYGFLSGQDPTRIDYLVNLLIQQSRFPPGAL 81
Cdd:cd03325 1 KITKIETFVVP---PRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGGFYRGGPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 82 GLSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYAGVytAPDAPAARDEFDRLNAEWGFTAFKLSPWRvDIHAHR 161
Cdd:cd03325 78 LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWI--GGDRPSDVAEAARARREAGFTAVKMNATE-ELQWID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 162 WGNVVKASADYFRSLRETVRDDYEIAFDAHAQIFEPVAArQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATG 241
Cdd:cd03325 155 TSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAK-DLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 242 ESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPMGPLATAVNVHFSAATQNFRILEYRLp 321
Cdd:cd03325 234 ERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSL- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
4JN7_A 322 kGQAYVYGGKDIEkrqgetrYVVDPYLP--KDGYLELrPDRPGWGVEMD 368
Cdd:cd03325 313 -GIHYNEGDDLLD-------YLVDPEVFdmENGYVKL-PTGPGLGIEID 352
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
131-371 |
3.88e-61 |
|
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: 196.63 E-value: 3.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 131 AARDEFDRLNAEWGFTAFKLSPWRVDihahrwgnvVKASADYFRSLRETVRDDYEIAFDAHaQIFEPVAARQLGNALAPY 210
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPD---------PEEDVERVRAVREAVGPGVDLMVDAN-GAWSVAEAIRLARALEEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 211 DPLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVA 290
Cdd:pfam13378 71 GLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 291 PHNPMGPLATAVNVHFSAATQNFRILEYRLPkgqaYVYGGKDIekrqgetryVVDPYLPKDGYLELrPDRPGWGVEMDEK 370
Cdd:pfam13378 151 PHSGGGPIGLAASLHLAAAVPNLLIQEYFLD----PLLLEDDL---------LTEPLEVEDGRVAV-PDGPGLGVELDED 216
|
.
4JN7_A 371 A 371
Cdd:pfam13378 217 A 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
19-368 |
1.46e-60 |
|
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: 199.10 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 19 VIVALDTDDGLTGWGECYNHGPDKALppILDYLYGFLSGQDPTRIDYLVNLLIQQSRF-PPGALGLSAISALDHCLWDLS 97
Cdd:cd03327 12 LFVEIETDDGTVGYANTTGGPVACWI--VDQHLARFLIGKDPSDIEKLWDQMYRATLAyGRKGIAMAAISAVDLALWDLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 98 AKAANVPVYKLLGGAVRDRVKVYAGVYTAPDAPAARDEFDRLNAEwGFTAFKLS-PW-RVDIHAHrwgnvVKASADYFRS 175
Cdd:cd03327 90 GKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEYLKE-GYRGMKMRfGYgPSDGHAG-----LRKNVELVRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 176 LRETVRDDYEIAFDAHAQIFEPVAARqLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYNRNEFLRLLQ 255
Cdd:cd03327 164 IREAVGYDVDLMLDCYMSWNLNYAIK-MARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 256 VKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHnpmgplATAV-NVHFSAATQNFRILEYrLPKgqayvyggKDIE 334
Cdd:cd03327 243 GRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPH------ASQIyNYHFIMSEPNSPFAEY-LPN--------SPDE 307
|
330 340 350
....*....|....*....|....*....|....*
4JN7_A 335 KRQGETRYV-VDPYLPKDGYLELrPDRPGWGVEMD 368
Cdd:cd03327 308 VGNPLFYYIfLNEPVPVNGYFDL-SDKPGFGLELN 341
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-391 |
1.01e-54 |
|
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: 184.57 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 2 KIDRMRVFMTRDKdRPRVIVALDTDDGLTGWGEC-YNHGPDKALPPILDYLYGFLSGQDPTRIDYLVNLLIQQSRFPPGA 80
Cdd:cd03322 1 KITAIEVIVTCPG-RNFVTLKITTDQGVTGLGDAtLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 81 LGLSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYAGVyTAPDAPAARDEFDRLNAEwGFTAFklspwRVDIHAh 160
Cdd:cd03322 80 VTMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHA-SGRDIPELLEAVERHLAQ-GYRAI-----RVQLPK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 161 rwgnvvkasadYFRSLRETVRDDYEIAFDAHAQIFePVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLAT 240
Cdd:cd03322 152 -----------LFEAVREKFGFEFHLLHDVHHRLT-PNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 241 GESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNP--MGPLATAVNVHFSAATQNFRILEY 318
Cdd:cd03322 220 GEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdLSPVGMAAALHLDLWVPNFGIQEY 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4JN7_A 319 RlpkgqayvyggkdieKRQGETRYVV-DPYLPKDGYLELrPDRPGWGVEMDEKAMEEEGYIHWQRRVPKRPDGS 391
Cdd:cd03322 300 M---------------RHAEETLEVFpHSVRFEDGYLHP-GEEPGLGVEIDEKAAAKFPYVPRYLPVARLEDGT 357
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-391 |
9.73e-39 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 143.13 E-value: 9.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 1 MKIDRMRVFMTrDKDRPRVIVALDTDDGLTGWGECYNHGPDKALPPIL-DYLYGFLSGQDPTRIDYLVNLLIQQSRFPPG 79
Cdd:PRK15072 1 MKIVDAEVIVT-CPGRNFVTLKITTDDGVTGLGDATLNGRELAVASYLqDHVCPLLIGRDAHRIEDIWQYLYRGAYWRRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 80 ALGLSAISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYaGVYTAPDAPAARDEFDRlNAEWGFTAFK---------- 149
Cdd:PRK15072 80 PVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVY-GHANGRDIDELLDDVAR-HLELGYKAIRvqcgvpglkt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 150 ------------------LSPWRVDIHAHRWGNVVkasADYFRSLRETVRDDYEIAFDAHAQIfEPVAARQLGNALAPYD 211
Cdd:PRK15072 158 tygvskgkglayepatkgLLPEEELWSTEKYLRFV---PKLFEAVRNKFGFDLHLLHDVHHRL-TPIEAARLGKSLEPYR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 212 PLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAP 291
Cdd:PRK15072 234 LFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 292 HNP--MGPLATAVNVHFSAATQNFRILEYrlpkgqayvyggkdieKRQGETRYVVDP--YLPKDGYleLRP-DRPGWGVE 366
Cdd:PRK15072 314 HGPtdLSPVCMAAALHFDLWVPNFGIQEY----------------MGHSEETLEVFPhsYTFEDGY--LHPgDAPGLGVD 375
|
410 420
....*....|....*....|....*
4JN7_A 367 MDEKAMEEEGYIHWQRRVPKRPDGS 391
Cdd:PRK15072 376 FDEKLAAKYPYEPAYLPVARLEDGT 400
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
4-318 |
4.10e-37 |
|
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: 134.38 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 4 DRMRVFMTRDKDRPRVIVALDTDDGLTGWGECynhgpdkalppildylygflsgqdptridylvnlliqqsrfppgalgl 83
Cdd:cd00308 12 RPFYLAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------------------ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 84 saISALDHCLWDLSAKAANVPVYKLLGGAVRDRVKVYagvytapdapaardefdrlnaewgftafklspwrvdihahrwg 163
Cdd:cd00308 44 --ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAY------------------------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 164 nvvkASADYFRSLRETVRDDYEIAFDAHAQIFEPvAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATgES 243
Cdd:cd00308 79 ----GSIERVRAVREAFGPDARLAVDANGAWTPK-EAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA-DE 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4JN7_A 244 LYNRNEF-LRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPMG-PLATAVNVHFSAATQNFRILEY 318
Cdd:cd00308 153 SVTTVDDaLEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAALPNDRAIET 229
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
16-368 |
1.23e-32 |
|
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: 125.97 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 16 RPRVIVALDTDDGLTGWgecYNHGPDKALPPILD-YLYGFLSGQDPTRIDYLVNLLIQQSRfppgALGLSAISALDHCLW 94
Cdd:cd03329 32 RKLALLTIETDEGAKGH---AFGGRPVTDPALVDrFLKKVLIGQDPLDRERLWQDLWRLQR----GLTDRGLGLVDIALW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 95 DLSAKAANVPVYKLLGGaVRDRVKVYAGVYTAPDA-----PAARDEFDRLNAEWGFTAFKLSPWRvdihahrwGNVVKAS 169
Cdd:cd03329 105 DLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLeglesPEAYADFAEECKALGYRAIKLHPWG--------PGVVRRD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 170 ADYFRSLRETVRDDYEIAFDAHAQiFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGES----LY 245
Cdd:cd03329 176 LKACLAVREAVGPDMRLMHDGAHW-YSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHsrgaLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 246 NRNEFLRllqVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPmgplaTAVNVHFSAATQNFRILEYRLP---- 321
Cdd:cd03329 255 SRADWVL---AGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGN-----GAANLHVIAAIRNTRYYERGLLhpsq 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
4JN7_A 322 KGQAYVYGGKDIEKrqgetryVVDpylpKDGYLELrPDRPGWGVEMD 368
Cdd:cd03329 327 KYDVYAGYLSVLDD-------PVD----SDGFVHV-PKGPGLGVEID 361
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
19-379 |
1.12e-31 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 123.69 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 19 VIVALDTDDGLTGWGecYNHGPDKALPPILDYLYGFLSGQDPTRI----DYLVNLLIQQSRfppGALGLSAISALDHCLW 94
Cdd:PRK15440 59 LVVEVEAENGQVGFA--VSTAGEMGAFIVEKHLNRFIEGKCVSDIeliwDQMLNATLYYGR---KGLVMNTISCVDLALW 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 95 DLSAKAANVPVYKLLGGAVRDRVKVYAgvyTAPDAPAARdefdrlnaEWGFTAFKLSPwrvdIHAHRWGNV-VKASADYF 173
Cdd:PRK15440 134 DLLGKVRGLPVYKLLGGAVRDELQFYA---TGARPDLAK--------EMGFIGGKMPL----HHGPADGDAgLRKNAAMV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 174 RSLRETVRDDYEIAFDAHAQIFEPVAARqLGNALAPYDPLFYEEPLRPEniDMWG--DLKQGL--NCVLATGESLYNRNE 249
Cdd:PRK15440 199 ADMREKVGDDFWLMLDCWMSLDVNYATK-LAHACAPYGLKWIEECLPPD--DYWGyrELKRNApaGMMVTSGEHEATLQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 250 FLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNpmgplATAVNVHFSAATQNFRILEYRLPKGQAyvyg 329
Cdd:PRK15440 276 FRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHG-----SSVYSHHFVITRTNSPFSEFLMMSPDA---- 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
4JN7_A 330 gkdiekrqGETRYVVDPYL-----PKDGYLEL-RPDRPGWGVEMDEKAMEEEGYIH 379
Cdd:PRK15440 347 --------DTVVPQFDPILldepvPVNGRIHKsVLDKPGFGVELNRDCNLKRPYSH 394
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
17-369 |
7.19e-26 |
|
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: 107.02 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 17 PRVIVALDTDDGLTGWGECYNHG--------PDKALPPILDYLYGFLSGQDPTRIDYLVNLLiqqSRFPPGALglSAISA 88
Cdd:cd03318 29 SLVLVRLTTSDGVVGIGEATTPGgpawggesPETIKAIIDRYLAPLLIGRDATNIGAAMALL---DRAVAGNL--FAKAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 89 LDHCLWDLSAKAANVPVYKLLGGAVRDRVKVyAGVYTAPDAPAARDEFDRLNAEWGFTAFKL----SPWRVDIhaHRWGN 164
Cdd:cd03318 104 IEMALLDAQGRRLGLPVSELLGGRVRDSLPV-AWTLASGDTERDIAEAEEMLEAGRHRRFKLkmgaRPPADDL--AHVEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 165 VVKASADYFRslretVRDDYEIAFDahaqifEPVAARQLgNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGESL 244
Cdd:cd03318 181 IAKALGDRAS-----VRVDVNQAWD------ESTAIRAL-PRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 245 YNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYfvGVAPHNPM---GPLATAVNVHFSAATQNfrileyrLP 321
Cdd:cd03318 249 SGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAA--GIALYGGTmleSSIGTAASAHLFATLPS-------LP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
4JN7_A 322 kgqayvYGGKDIEKRQGETRYVVDPYLPKDGYLELrPDRPGWGVEMDE 369
Cdd:cd03318 320 ------FGCELFGPLLLAEDLLEEPLAYRDGELHV-PTGPGLGVRLDE 360
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
28-369 |
1.75e-24 |
|
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: 102.88 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 28 GLTGWGECYNHGPDKALppILDYLYGFLSGQDPTRIDYLVNLLIQQSRFP-PGALGLSAISALDHCLWDLSAKAANVPVY 106
Cdd:cd03328 39 GRTGLGYTYADAAAAAL--VDGLLAPVVEGRDALDPPAAWEAMQRAVRNAgRPGVAAMAISAVDIALWDLKARLLGLPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 107 KLLgGAVRDRVKVY-AGVYTAPDAPAARDEFDRLnAEWGFTAFKL---SPWRVDIhahrwgnvvkasaDYFRSLRETVRD 182
Cdd:cd03328 117 RLL-GRAHDSVPVYgSGGFTSYDDDRLREQLSGW-VAQGIPRVKMkigRDPRRDP-------------DRVAAARRAIGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 183 DYEIAFDAHAQiFEPVAARQLGNALAPYDPLFYEEPLRPENIdmwgdlkQGLNCV---------LATGESLYNRNEFLRL 253
Cdd:cd03328 182 DAELFVDANGA-YSRKQALALARAFADEGVTWFEEPVSSDDL-------AGLRLVrergpagmdIAAGEYAYTLAYFRRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 254 LQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHnpmgpLATAVNVHFSAATQNFRILEyrlpkgqaYVYGGKDI 333
Cdd:cd03328 254 LEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH-----CAPALHAHVACAVPRLRHLE--------WFHDHVRI 320
|
330 340 350
....*....|....*....|....*....|....*..
4JN7_A 334 EkrqgetRYVVDPYL-PKDGYLELRPDRPGWGVEMDE 369
Cdd:cd03328 321 E------RMLFDGAPdPSGGALRPDLSRPGLGLELRA 351
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
87-314 |
8.57e-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: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 87 SALDHCLWDLSAKAANVPVYKLLGGaVRDRVKVyaGVYTAPDAPAARDEFDRLNAEWGFTAFKLspwRVDIHAHRWGNVV 166
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRV--AHMLGLGEPAEVAEEARRALEAGFRTFKL---KVGRDPARDVAVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 167 KAsadyfrsLRETVRDDYEIAFDAHaQIFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYN 246
Cdd:cd03315 120 AA-------LREAVGDDAELRVDAN-RGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4JN7_A 247 RNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHNPM-GPLATAVNVHFSAATQNFR 314
Cdd:cd03315 192 PHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIeSGLGTLANAHLAAALRAVT 260
|
|
| 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 ... |
19-285 |
1.26e-16 |
|
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: 79.93 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 19 VIVALdTDDGLTGWGEC----YNHG--PDKALPpILDYLYGFLSGQDPtRIDYLVNLLiqQSRFPPGAlglSAISALDHC 92
Cdd:cd03319 28 VIVEI-ELDGITGYGEAaptpRVTGetVESVLA-ALKSVRPALIGGDP-RLEKLLEAL--QELLPGNG---AARAAVDIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 93 LWDLSAKAANVPVYKLLGGAVRDRVkVYAgvYTAP-DAPAARDEFDRLNAEWGFTAFKL---SPWRVDIhahrwgNVVKA 168
Cdd:cd03319 100 LWDLEAKLLGLPLYQLWGGGAPRPL-ETD--YTISiDTPEAMAAAAKKAAKRGFPLLKIklgGDLEDDI------ERIRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 169 sadyfrsLRETVrDDYEIAFDAHaQIFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYNRN 248
Cdd:cd03319 171 -------IREAA-PDARLRVDAN-QGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAA 241
|
250 260 270
....*....|....*....|....*....|....*..
4JN7_A 249 EFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAY 285
Cdd:cd03319 242 DAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAA 278
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
85-367 |
1.74e-16 |
|
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: 80.46 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 85 AISALDHCLWDLSAKAANVPVYKLL-----------------------------------GGAVRD---RVKVYAGVYTA 126
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqpGKAAREadlLAEGYPAYTTS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 127 PDAPAARDE-FDRLNAEW---GFTAFKLSpwrvdihahrwgnvVKAS-ADYFRSL---RETVRDDYEIAFDAHaQIFEPV 198
Cdd:cd03324 190 AGWLGYSDEkLRRLCKEAlaqGFTHFKLK--------------VGADlEDDIRRCrlaREVIGPDNKLMIDAN-QRWDVP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 199 AARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCV---LATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEM 275
Cdd:cd03324 255 EAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLpigVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNEN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 276 RRIATLAEAYFVGVAPHnpmgplatAVNVHFSAATQNFRILEYrlpkgqAYVYGGKdiEKRQGEtrYV-------VDPYL 348
Cdd:cd03324 335 LAVLLMAAKFGVPVCPH--------AGGVGLCELVQHLSMIDY------ICVSGSK--EGRVIE--YVdhlhehfVYPVV 396
|
330
....*....|....*....
4JN7_A 349 PKDGYLeLRPDRPGWGVEM 367
Cdd:cd03324 397 IQNGAY-MPPTDPGYSIEM 414
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
10-110 |
4.49e-16 |
|
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: 73.66 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 10 MTRDKDRPRVIVALDTDDGLTGWGECYNHGP--DKALPPILDYLYGFLSGQDPTRIDYLVNLLIQqsrfppGALG-LSAI 86
Cdd:pfam02746 20 FGTVQQQSLVIVRIETSEGVVGIGEATSYGGraETIKAILDDHLAPLLIGRDAANISDLWQLMYR------AALGnMSAK 93
|
90 100
....*....|....*....|....
4JN7_A 87 SALDHCLWDLSAKAANVPVYKLLG 110
Cdd:pfam02746 94 AAIDMALWDLKAKVLNLPLADLLG 117
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
17-373 |
4.50e-14 |
|
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: 72.90 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 17 PRVIVALDTDDGLTG--WGECYNHGPDKALPPILDYLYGFLSGqdptriDYLVNLLIQQ---SRFP-PGALGLS--AISA 88
Cdd:cd03321 30 PLVLIDLATDEGVTGhsYLFTYTPAALKSLKQLLDDMAALLVG------EPLAPAELERalaKRFRlLGYTGLVrmAAAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 89 LDHCLWDLSAKAANVPVYKLLGGAVRDrVKVYaGVYTAPDAPAARDEFDRLnAEWGFTAFKLSPWRVDihahrwgnvVKA 168
Cdd:cd03321 104 IDMAAWDALAKVHGLPLAKLLGGNPRP-VQAY-DSHGLDGAKLATERAVTA-AEEGFHAVKTKIGYPT---------ADE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 169 SADYFRSLRETVRDDYEIAFDaHAQIFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNCVLATGESLYNRN 248
Cdd:cd03321 172 DLAVVRSIRQAVGDGVGLMVD-YNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 249 EFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPHnpmgpLATAVNVHFSAATQNFRILEYrlpkgqayvy 328
Cdd:cd03321 251 EMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH-----LFQEISAHLLAVTPTAHWLEY---------- 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
4JN7_A 329 ggKDIEKRQGETRYVVdpylpKDGYLeLRPDRPGWGVEMDEKAME 373
Cdd:cd03321 316 --VDWAGAILEPPLKF-----EDGNA-VIPDEPGNGIIWREKAVR 352
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
17-374 |
1.16e-13 |
|
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: 71.97 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 17 PRVIVALDTDDGLTGWGECYNHGP--DKALPPILDYLYGFLSGQDPTRIDYLVNLLIQQSrfpPGALGL---------SA 85
Cdd:cd03323 29 TRNIVELTDDNGNTGVGESPGGAEalEALLEAARSLVGGDVFGAYLAVLESVRVAFADRD---AGGRGLqtfdlrttvHV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 86 ISALDHCLWDLSAKAANVPVYKLLGGAVRDRVK-------VYAGVYTAPDAPAARDEF-------------DRLNAEWGF 145
Cdd:cd03323 106 VTAFEVALLDLLGQALGVPVADLLGGGQRDSVPflaylfyKGDRHKTDLPYPWFRDRWgealtpegvvrlaRAAIDRYGF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 146 TAFKLSpwrvdihahrwGNVVKAS--ADYFRSLRETVrDDYEIAFDAHA--QIFEPVA-ARQLGNALApydplFYEEPLr 220
Cdd:cd03323 186 KSFKLK-----------GGVLPGEeeIEAVKALAEAF-PGARLRLDPNGawSLETAIRlAKELEGVLA-----YLEDPC- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 221 pENIDMWGDLKQGLNCVLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEAYFVGVAPH--NPMGpL 298
Cdd:cd03323 248 -GGREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHsnNHLG-I 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4JN7_A 299 ATAVNVHFSAATQNfriLEYrlpkgqayvyggkDIEK---RQGETRYVVDPYLPKDGYLELrPDRPGWGVEMDEKAMEE 374
Cdd:cd03323 326 SLAMMTHVAAAAPG---LIT-------------ACDThwiWQDGQVITGEPLRIKDGKVAV-PDKPGLGVELDRDKLAK 387
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
85-278 |
5.56e-12 |
|
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: 66.65 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 85 AISALDHCLWDLSAKAANVPVYKLLG-----GAVRDRVKVYAG---VYTAPDAPAARDEFDRLnAEWGFTAFKLSPWRVD 156
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAAggyYYPGDDLGRLRDEMRRY-LDRGYTVVKIKIGGAP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 157 IHAHRwgNVVKASADyfrslreTVRDDYEIAFDAHAQiFEPVAARQLGNALAPYDPLFYEEPLRPENIDMWGDLKQGLNC 236
Cdd:cd03326 188 LDEDL--RRIEAALD-------VLGDGARLAVDANGR-FDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
4JN7_A 237 VLATGESLYNRNEFLRLLQVKGA----DLIQPDICVVGGISEMRRI 278
Cdd:cd03326 258 PIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRM 303
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
12-374 |
1.13e-11 |
|
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: 65.33 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 12 RDKDRPRVIVALDTDDGLTGWGECYN-HGP-------DKALPPILDYLYGFLSGQDPTRIDYLVNLL--IQQSRFppgal 81
Cdd:cd03317 20 TLNEREFLIVELTDEEGITGYGEVVAfEGPfyteetnATAWHILKDYLLPLLLGREFSHPEEVSERLapIKGNNM----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 82 glsAISALDHCLWDLSAKAANVPVYKLLGGaVRDRVKVYAGVYTAPDAPAARDEFDRLNAEwGFTAFKL--SP-WRVDih 158
Cdd:cd03317 95 ---AKAGLEMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQLLKQIERYLEE-GYKRIKLkiKPgWDVE-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 159 ahrwgnVVKAsadyfrslretVRDDY-EIAFDAHA-QIFEPVAARQLgNALAPYDPLFYEEPLRPENIDMWGDLKQGLNC 236
Cdd:cd03317 168 ------PLKA-----------VRERFpDIPLMADAnSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 237 VLATGESLYNRNEFLRLLQVKGADLIQPDICVVGGISEMRRIATLAEA----YFVGvaphnpmGPLAT----AVNVHFSA 308
Cdd:cd03317 230 PICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEhgipVWCG-------GMLESgigrAHNVALAS 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4JN7_A 309 atqnfrileyrLPKgqaYVYGGkDIekrQGETRY-----VVDPYLPKDGYLELrPDRPGWGVEMDEKAMEE 374
Cdd:cd03317 303 -----------LPN---FTYPG-DI---SASSRYfeediITPPFELENGIISV-PTGPGIGVTVDREALKK 354
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
131-225 |
6.00e-09 |
|
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: 53.05 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4JN7_A 131 AARDEFDRLNAEWGFTAFKLSPWRVDIHAhrwgnvvkasADYFRSLRETVRDDYEIAFDAHaQIFEPVAARQLGNALAPY 210
Cdd:smart00922 3 ELAEAARRAVAEAGFRAVKVKVGGGPLED----------LARVAAVREAVGPDADLMVDAN-GAWTAEEAIRALEALDEL 71
|
90
....*....|....*
4JN7_A 211 DPLFYEEPLRPENID 225
Cdd:smart00922 72 GLEWIEEPVPPDDLE 86
|
|
| |
