|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
5-446 |
0e+00 |
|
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a stereoisomer) to 5-dehydro-4-deoxyglucarate which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase (GenProp0716). The E. coli enzyme has been well-characterized.
Pssm-ID: 211799 [Multi-domain] Cd Length: 441 Bit Score: 953.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 5 FSTPVVSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL 84
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 85 TAVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY 164
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 165 QSQPDDKCDWYRLRHDEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNE 244
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 245 AIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR 324
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 325 VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDM 404
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490239004 405 DQVMKAHELYQKHGLGARDDAMGMQYLIPNWTFDNKRPCMVR 446
Cdd:TIGR03247 400 DAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
9-417 |
0e+00 |
|
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: 711.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 9 VVSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIPGG-EKIRKTLEDAIPLVVGKTLGEYKNVLTAV 87
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 88 RNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQqRSEVEMLGYLFFVGNRKATPLPYQsq 167
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 168 pddkcdWYRLRHDEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIK 247
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 248 IGKYLKGSLAYAEDPCGaeqgfsGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVA 326
Cdd:cd03323 232 LAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 327 QMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDMDQ 406
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
410
....*....|.
gi 490239004 407 VMKAHELYQKH 417
Cdd:cd03323 385 LAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
10-410 |
7.32e-80 |
|
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: 251.28 E-value: 7.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 10 VSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIP----GGEKIRKTLEDAI-PLVVGKTLGEYKNVL 84
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 85 TAVRNtfadrdaggrglqtfDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpy 164
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPVYATL------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 165 qsqpddkcdwyrlrhdEAMTPDAVVRLAEAAYEkYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLN 243
Cdd:COG4948 134 ----------------GIDTPEEMAEEAREAVA-RGFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 244 EAIKIGKYLKG-SLAYAEDPCGAEQGfsgrEVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFW-TMQG 321
Cdd:COG4948 197 EAIRLLRALEDlGLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 322 SVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGkITAIDTHW-IWQEgnQRLTKEPFEIKGGMVQVPAKPGLGV 400
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDGpLLLA--DDLVEDPLRIEDGYLTVPDGPGLGV 349
|
410
....*....|
gi 490239004 401 ELDMDQVMKA 410
Cdd:COG4948 350 ELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
187-405 |
2.14e-53 |
|
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: 177.76 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 187 AVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAIKIGKYLKG-SLAYAEDPCG 264
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEElGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 265 AEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVAQMCHEFGLTWGSHSNNH 343
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239004 344 FdISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDMD 405
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLLE-DDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-284 |
6.92e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 75.78 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 185 PDAVVRLAEAAYEKYGFNDFKLKGGVlAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAIKIGKYLKG-SLAYAEDP 262
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDElGLEWIEEP 79
|
90 100
....*....|....*....|..
gi 490239004 263 CGAEQGfsgrEVMAEFRRATGL 284
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
113-410 |
4.41e-08 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 54.90 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgYLFFVGNRkatplpyqsqpddkcdwyrlrhdeamtPDAVVRLA 192
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 193 EAAYEKyGFNDFKLKG----GVLAGEEEAESIVAlakRFPQAR--------VTLDPNGAWSLNEAIKIGKYLKG-SLAYA 259
Cdd:PRK14017 133 RARVER-GFTAVKMNGteelQYIDSPRKVDAAVA---RVAAVReavgpeigIGVDFHGRVHKPMAKVLAKELEPyRPMFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 260 EDPCGAEQgfsgREVMAEFRRATGLPtatnmIAT--------DWRQMghtLSLQSVDIPLADPhfwTMQGSV----RVAQ 327
Cdd:PRK14017 209 EEPVLPEN----AEALPEIAAQTSIP-----IATgerlfsrwDFKRV---LEAGGVDIIQPDL---SHAGGItecrKIAA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 328 MCHEFGLTWGSHsNNHFDISLAMFTHVAAAAPGKI---TAIDTHWiwQEGNQRL----TKEPFEIKGGMVQVPAKPGLGV 400
Cdd:PRK14017 274 MAEAYDVALAPH-CPLGPIALAACLQVDAVSPNAFiqeQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGI 350
|
330
....*....|
gi 490239004 401 ELDMDQVMKA 410
Cdd:PRK14017 351 EIDEAKVRER 360
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
5-446 |
0e+00 |
|
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a stereoisomer) to 5-dehydro-4-deoxyglucarate which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase (GenProp0716). The E. coli enzyme has been well-characterized.
Pssm-ID: 211799 [Multi-domain] Cd Length: 441 Bit Score: 953.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 5 FSTPVVSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL 84
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 85 TAVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY 164
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 165 QSQPDDKCDWYRLRHDEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNE 244
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 245 AIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR 324
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 325 VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDM 404
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490239004 405 DQVMKAHELYQKHGLGARDDAMGMQYLIPNWTFDNKRPCMVR 446
Cdd:TIGR03247 400 DAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
9-417 |
0e+00 |
|
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: 711.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 9 VVSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIPGG-EKIRKTLEDAIPLVVGKTLGEYKNVLTAV 87
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 88 RNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQqRSEVEMLGYLFFVGNRKATPLPYQsq 167
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 168 pddkcdWYRLRHDEAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIK 247
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 248 IGKYLKGSLAYAEDPCGaeqgfsGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVA 326
Cdd:cd03323 232 LAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 327 QMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDMDQ 406
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
410
....*....|.
gi 490239004 407 VMKAHELYQKH 417
Cdd:cd03323 385 LAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
10-410 |
7.32e-80 |
|
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: 251.28 E-value: 7.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 10 VSSMQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEIP----GGEKIRKTLEDAI-PLVVGKTLGEYKNVL 84
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 85 TAVRNtfadrdaggrglqtfDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpy 164
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPVYATL------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 165 qsqpddkcdwyrlrhdEAMTPDAVVRLAEAAYEkYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLN 243
Cdd:COG4948 134 ----------------GIDTPEEMAEEAREAVA-RGFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 244 EAIKIGKYLKG-SLAYAEDPCGAEQGfsgrEVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFW-TMQG 321
Cdd:COG4948 197 EAIRLLRALEDlGLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 322 SVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGkITAIDTHW-IWQEgnQRLTKEPFEIKGGMVQVPAKPGLGV 400
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDGpLLLA--DDLVEDPLRIEDGYLTVPDGPGLGV 349
|
410
....*....|
gi 490239004 401 ELDMDQVMKA 410
Cdd:COG4948 350 ELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
187-405 |
2.14e-53 |
|
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: 177.76 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 187 AVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAIKIGKYLKG-SLAYAEDPCG 264
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEElGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 265 AEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVAQMCHEFGLTWGSHSNNH 343
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239004 344 FdISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPAKPGLGVELDMD 405
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLLE-DDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
28-401 |
6.58e-53 |
|
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: 181.27 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 28 LSGAHAPFFTRNIVVIK--DNSGHTGVGEIPGGEKIR---KTLEDAI-PLVVGKTLGEYKNVLTAVRNTFADRDAGGrgl 101
Cdd:cd03316 14 LPEPGGAVTWRNLVLVRvtTDDGITGWGEAYPGGRPSavaAAIEDLLaPLLIGRDPLDIERLWEKLYRRLFWRGRGG--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 102 qtfdlrTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyqsqpddkcdWYRLRhde 181
Cdd:cd03316 91 ------VAMAAISAVDIALWDIKGKAAGVPVYKLLG-GKVRDRVRVYASG----------------------GGYDD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 182 amTPDAVVRLAEAAYEKyGFNDFKLKGGVLAG-----EEEAESIVALAKRF-PQARVTLDPNGAWSLNEAIKIGKYLKGS 255
Cdd:cd03316 139 --SPEELAEEAKRAVAE-GFTAVKLKVGGPDSggedlREDLARVRAVREAVgPDVDLMVDANGRWDLAEAIRLARALEEY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 256 -LAYAEDPCGAEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVAQMCHEFG 333
Cdd:cd03316 216 dLFWFEEPVPPDD----LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGgITEAKKIAALAEAHG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490239004 334 LTWGSHSNNHfDISLAMFTHVAAAAPGkITAIDTHWIWQEGNQRLTKEPFEIKGGMVQVPAKPGLGVE 401
Cdd:cd03316 292 VRVAPHGAGG-PIGLAASLHLAAALPN-FGILEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
13-367 |
2.28e-52 |
|
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: 175.59 E-value: 2.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 13 MQVIPVAGHDSMLMNLSGAHAPFFTRNIVVIKDNSGHTGVGEipggekirktledaiplvvgktlgeyknvltavrntfa 92
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 93 drdaggrglqtfdlrttihVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyqsqpddkc 172
Cdd:cd00308 43 -------------------VISGIDMALWDLAAKALGVPLAELLG-GGSRDRVPAYGSI--------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 173 dwyrlrhdeamtpdavvrlaeaayekygfndfklkggvlageeeaESIVALAKRFP-QARVTLDPNGAWSLNEAIKIGKY 251
Cdd:cd00308 82 ---------------------------------------------ERVRAVREAFGpDARLAVDANGAWTPKEAIRLIRA 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 252 L-KGSLAYAEDPCGAEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTM-QGSVRVAQMC 329
Cdd:cd00308 117 LeKYGLAWIEEPCAPDD----LEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGlTESRRAADLA 192
|
330 340 350
....*....|....*....|....*....|....*...
gi 490239004 330 HEFGLTWGSHSNNHFDISLAMFTHVAAAAPgKITAIDT 367
Cdd:cd00308 193 EAFGIRVMVHGTLESSIGTAAALHLAAALP-NDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
40-407 |
1.16e-21 |
|
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: 95.85 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 40 IVVIKDNSGHTGVGE--IPGG--------EKIRKTLEDAI-PLVVGKtlgeyknvltAVRNTfadrdagGRGLQTFDLRT 108
Cdd:cd03318 32 LVRLTTSDGVVGIGEatTPGGpawggespETIKAIIDRYLaPLLIGR----------DATNI-------GAAMALLDRAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 109 TIHVVT--GIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyqSQPDDKCDwyrlrhdeamtpd 186
Cdd:cd03318 95 AGNLFAkaAIEMALLDAQGRRLGLPVSELLG-GRVRDSLPVAWTL--------------ASGDTERD------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 187 avVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFP-QARVTLDPNGAWSLNEAIKIGKYLKGS-LAYAEDPCG 264
Cdd:cd03318 147 --IAEAEEMLEAGRHRRFKLKMGARPPADDLAHVEAIAKALGdRASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 265 AEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDI-PLADPHFWTMQGSVRVAQMCHEFGLtwGSHSNNH 343
Cdd:cd03318 225 REN----LDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVfSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTM 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 344 FD--ISLAMFTHVAAAAPGkIT----AIDTHWIWQEgnqrLTKEPFEIKGGMVQVPAKPGLGVELDMDQV 407
Cdd:cd03318 299 LEssIGTAASAHLFATLPS-LPfgceLFGPLLLAED----LLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-284 |
6.92e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 75.78 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 185 PDAVVRLAEAAYEKYGFNDFKLKGGVlAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAIKIGKYLKG-SLAYAEDP 262
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDElGLEWIEEP 79
|
90 100
....*....|....*....|..
gi 490239004 263 CGAEQGfsgrEVMAEFRRATGL 284
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
115-335 |
2.41e-14 |
|
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: 72.76 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 115 GIEAAMLDLLGQHLGVNVASLLGDGQQRSEVE-MLGylffvgnrkatplpyqsqpddkcdwyrlrhdeAMTPDAVVRLAE 193
Cdd:cd03315 47 AVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAhMLG--------------------------------LGEPAEVAEEAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 194 AAYEkYGFNDFKLKGGVLAgEEEAESIVALAKRFPQ-ARVTLDPNGAWSLNEAIKIGKYLKGS-LAYAEDPCGAEQgfsg 271
Cdd:cd03315 95 RALE-AGFRTFKLKVGRDP-ARDVAVVAALREAVGDdAELRVDANRGWTPKQAIRALRALEDLgLDYVEQPLPADD---- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490239004 272 REVMAEFRRATGLPTATN---MIATDWRQMGHTLSLQSVDIPLADPHFWTmqGSVRVAQMCHEFGLT 335
Cdd:cd03315 169 LEGRAALARATDTPIMADesaFTPHDAFRELALGAADAVNIKTAKTGGLT--KAQRVLAVAEALGLP 233
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
113-403 |
1.05e-12 |
|
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: 68.89 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgylffvgnrkatplpYQsqpddkcdwyrlrHDEAMTPDAVVRLA 192
Cdd:cd03325 82 ISGIDQALWDIKGKVLGVPVHQLLG-GQVRDRVRV----------------YS-------------WIGGDRPSDVAEAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 193 EAAYEKyGFNDFKLkggVLAGE----EEAESIVALAKRF--------PQARVTLDPNGAWSLNEAIKIGKYLKG-SLAYA 259
Cdd:cd03325 132 RARREA-GFTAVKM---NATEElqwiDTSKKVDAAVERVaalreavgPDIDIGVDFHGRVSKPMAKDLAKELEPyRLLFI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 260 EDPCGAEQgfsgREVMAEFRRATGLPTATN--MIAT-DWRQMghtLSLQSVDIPLAD-PHFWTMQGSVRVAQMCHEFGLT 335
Cdd:cd03325 208 EEPVLPEN----VEALAEIAARTTIPIATGerLFSRwDFKEL---LEDGAVDIIQPDiSHAGGITELKKIAAMAEAYDVA 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490239004 336 WGSHsNNHFDISLAMFTHVAAAAP--------GKITAIDTHWIWQEGnqrLTKEPFEIKGGMVQVPAKPGLGVELD 403
Cdd:cd03325 281 LAPH-CPLGPIALAASLHVDASTPnfliqeqsLGIHYNEGDDLLDYL---VDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
185-359 |
3.68e-12 |
|
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: 66.13 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 185 PDAVVRLAEAAYEKyGFNDFKLKGGVLAGEEEAESIVALAKRFP-QARVTLDPNGAWSLNEAIKIGKYL-KGSLAYAEDP 262
Cdd:cd03320 83 DAAALGEAKAAYGG-GYRTVKLKVGATSFEEDLARLRALREALPaDAKLRLDANGGWSLEEALAFLEALaAGRIEYIEQP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 263 CGAEQgfsgreVMAEFRRATGLPtatnmIATDwrqmgHTLSLQSVDIPLADPHfW--------TMQGSVR----VAQMCH 330
Cdd:cd03320 162 LPPDD------LAELRRLAAGVP-----IALD-----ESLRRLDDPLALAAAG-AlgalvlkpALLGGPRalleLAEEAR 224
|
170 180 190
....*....|....*....|....*....|..
gi 490239004 331 EFGL-TWGSHSnnhFD--ISLAMFTHVAAAAP 359
Cdd:cd03320 225 ARGIpAVVSSA---LEssIGLGALAHLAAALP 253
|
|
| 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 ... |
37-285 |
1.24e-09 |
|
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: 59.12 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 37 TRNIVVIKDNSGHTGVGEIPG-----GE---KIRKTLEDAIPLVVGKTLgEYKNVLTAVrNTFADRDAGGRglqtfdlrt 108
Cdd:cd03319 25 AENVIVEIELDGITGYGEAAPtprvtGEtveSVLAALKSVRPALIGGDP-RLEKLLEAL-QELLPGNGAAR--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 109 tihvvTGIEAAMLDLLGQHLGVNVASLLGDGQQRsevemlgylffvgnrkatPLPYqsqpddkcdwyrlrhdeAMT---- 184
Cdd:cd03319 94 -----AAVDIALWDLEAKLLGLPLYQLWGGGAPR------------------PLET-----------------DYTisid 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 185 -PDAVVRLAEAaYEKYGFNDFKLKGGvLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIKIGKYLKGS-LAYAEDP 262
Cdd:cd03319 134 tPEAMAAAAKK-AAKRGFPLLKIKLG-GDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELgVELIEQP 211
|
250 260
....*....|....*....|...
gi 490239004 263 CGAEQgfsgREVMAEFRRATGLP 285
Cdd:cd03319 212 VPAGD----DDGLAYLRDKSPLP 230
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
40-409 |
2.73e-09 |
|
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: 58.40 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 40 IVVIKDNSGHTGVGEIPGGEKIRKTLED-----------AIPLVVGKTLGEyknvltavRNTFADRDAGGRGLQTfdlrt 108
Cdd:cd03317 28 IVELTDEEGITGYGEVVAFEGPFYTEETnatawhilkdyLLPLLLGREFSH--------PEEVSERLAPIKGNNM----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 109 tihVVTGIEAAMLDLLGQHLGVNVASLLGdgQQRSEVEmlgylffVGnrkaTPLPYQSQPDDkcdwyrlrhdeamTPDAV 188
Cdd:cd03317 95 ---AKAGLEMAVWDLYAKAQGQSLAQYLG--GTRDSIP-------VG----VSIGIQDDVEQ-------------LLKQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 189 VRLAEAAYEKygfndFKLKggvLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIKIGKYLKGSLAYAEDPCGAEQG 268
Cdd:cd03317 146 ERYLEEGYKR-----IKLK---IKPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQPLAADDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 269 FSGREVMAEF----------------RRATGLPTAT--NM-IAtdwRQMGHTLSLQSVDI-PLADPHFWtmqgsvrVAQM 328
Cdd:cd03317 218 IDHAELQKLLktpicldesiqsaedaRKAIELGACKiiNIkPG---RVGGLTEALKIHDLcQEHGIPVW-------CGGM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 329 ChEFGLtwGSHSNNHFDiSLAMFTHvaaaaPGKITAIDTHWIwqegnQRLTKEPFEIKGGMVQVPAKPGLGVELDMDQVM 408
Cdd:cd03317 288 L-ESGI--GRAHNVALA-SLPNFTY-----PGDISASSRYFE-----EDIITPPFELENGIISVPTGPGIGVTVDREALK 353
|
.
gi 490239004 409 K 409
Cdd:cd03317 354 K 354
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
113-410 |
4.41e-08 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 54.90 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgYLFFVGNRkatplpyqsqpddkcdwyrlrhdeamtPDAVVRLA 192
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 193 EAAYEKyGFNDFKLKG----GVLAGEEEAESIVAlakRFPQAR--------VTLDPNGAWSLNEAIKIGKYLKG-SLAYA 259
Cdd:PRK14017 133 RARVER-GFTAVKMNGteelQYIDSPRKVDAAVA---RVAAVReavgpeigIGVDFHGRVHKPMAKVLAKELEPyRPMFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 260 EDPCGAEQgfsgREVMAEFRRATGLPtatnmIAT--------DWRQMghtLSLQSVDIPLADPhfwTMQGSV----RVAQ 327
Cdd:PRK14017 209 EEPVLPEN----AEALPEIAAQTSIP-----IATgerlfsrwDFKRV---LEAGGVDIIQPDL---SHAGGItecrKIAA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 328 MCHEFGLTWGSHsNNHFDISLAMFTHVAAAAPGKI---TAIDTHWiwQEGNQRL----TKEPFEIKGGMVQVPAKPGLGV 400
Cdd:PRK14017 274 MAEAYDVALAPH-CPLGPIALAACLQVDAVSPNAFiqeQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGI 350
|
330
....*....|
gi 490239004 401 ELDMDQVMKA 410
Cdd:PRK14017 351 EIDEAKVRER 360
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
65-409 |
4.46e-08 |
|
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: 54.80 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 65 LEDAIPLVVGKTLgeyknVLTAVRNTFADRD--AGGRGLQTFDLrttihvvTGIEAAMLDLLGQHLGVNVASLLGdgqqr 142
Cdd:cd03321 63 LDDMAALLVGEPL-----APAELERALAKRFrlLGYTGLVRMAA-------AGIDMAAWDALAKVHGLPLAKLLG----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 143 sevemlgylffvgnrkATPLPYQSQPDDKCDWYRLRHDEAmtpdavVRLAEAayekyGFNDFKLKGGVLAGEEEAESIVA 222
Cdd:cd03321 126 ----------------GNPRPVQAYDSHGLDGAKLATERA------VTAAEE-----GFHAVKTKIGYPTADEDLAVVRS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 223 LAKRFP-QARVTLDPNGAWSLNEAIKIGKYLKGS-LAYAEDPCGAEQgfsgREVMAEFRRATGLPTatnMIATDW---RQ 297
Cdd:cd03321 179 IRQAVGdGVGLMVDYNQSLTVPEAIERGQALDQEgLTWIEEPTLQHD----YEGHARIASALRTPV---QMGENWlgpEE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 298 MGHTLSLQSVDIPLAD-PHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDislamfTHVAAAAPgkiTAidtHWI----WQ 372
Cdd:cd03321 252 MFKALSAGACDLVMPDlMKIGGVTGWLRASALAEQAGIPMSSHLFQEIS------AHLLAVTP---TA---HWLeyvdWA 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 490239004 373 EGnqrLTKEPFEIKGGMVQVPAKPGLGVELDMDQVMK 409
Cdd:cd03321 320 GA---ILEPPLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
228-287 |
3.37e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 42.65 E-value: 3.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239004 228 PQARVTLDPNGAWSLNEAIKIGKYLK--GSLAYAEDPCGaeqgfSGREvMAEFRRATGLPTA 287
Cdd:PRK02901 133 PDGRVRVDANGGWSVDEAVAAARALDadGPLEYVEQPCA-----TVEE-LAELRRRVGVPIA 188
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
109-410 |
3.82e-04 |
|
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: 42.43 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 109 TIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYlffvGNRKATPLPYQSQPDDKCDWYRlrHDEAMTPdav 188
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLG-GKSRDGIMVYSH----ASGRDIPELLEAVERHLAQGYR--AIRVQLP--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 189 vRLAEAAYEKYGFNDFKLKGGvlageeeaesivalakrfpQARVTldPNgawslnEAIKIGKYLKGS-LAYAEDPCGAEQ 267
Cdd:cd03322 151 -KLFEAVREKFGFEFHLLHDV-------------------HHRLT--PN------QAARFGKDVEPYrLFWMEDPTPAEN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 268 gfsgREVMAEFRRATGLPTAT----NMIAtDWRQMghtLSLQSVD-IPLADPHFWTMQGSVRVAQMCHEFGLTWGSH--- 339
Cdd:cd03322 203 ----QEAFRLIRQHTATPLAVgevfNSIW-DWQNL---IQERLIDyIRTTVSHAGGITPARKIADLASLYGVRTGWHgpt 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239004 340 --------SNNHFDISLAMFthvaaaapgkitAIDTHWIWQEGNQRLTKEPFEIKGGMVQVPAKPGLGVELDMDQVMKA 410
Cdd:cd03322 275 dlspvgmaAALHLDLWVPNF------------GIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
146-287 |
9.82e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 40.98 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239004 146 EMLGYLFFVGNRKATPLPYQsQPDDkcdwyrlrhdeamtpdAVVRLAEAAYEKYGfndfKLKGGVLAGEEEAESIVALAK 225
Cdd:PRK05105 95 ELAGTLPQAANYRTAPLCYG-DPDE----------------LILKLADMPGEKVA----KVKVGLYEAVRDGMLVNLLLE 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490239004 226 RFPQARVTLDPNGAWSLNEAIKIGKYLK----GSLAYAEDPCGAeqgfsgREVMAEFRRATGLPTA 287
Cdd:PRK05105 154 AIPDLKLRLDANRGWTLEKAQQFAKYVPpdyrHRIAFLEEPCKT------PDDSRAFARATGIAIA 213
|
|
| |
