|
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: 952.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 5 FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL 84
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 85 TAVRNQFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY 164
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 165 QSQPDEQCDWYRLRHEEAMTPETVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNE 244
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 245 AISIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR 324
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 325 VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDM 404
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446029258 405 DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR 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: 716.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 9 VVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGG-EKIRKTLEDAIPLVVGKTLGEYKNVLTAV 87
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 88 RNQFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQqRSEVEMLGYLFFVGNRKATPLPYQsq 167
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 168 pdeqcdWYRLRHEEAMTPETVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIS 247
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 248 IGKYLKGSLAYAEDPCGaeqgfsGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVA 326
Cdd:cd03323 232 LAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 327 QMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDMDQ 406
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
410
....*....|.
gi 446029258 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 |
4.33e-81 |
|
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: 254.36 E-value: 4.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 10 VTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIP----GGEKIRKTLEDAI-PLVVGKTLGEYKNVL 84
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 85 TAVRNqfadrdaggrglqtfDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpy 164
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPVYATL------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 165 qsqpdeqcdwyrlrheEAMTPETVVRLAEAAYEkYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLN 243
Cdd:COG4948 134 ----------------GIDTPEEMAEEAREAVA-RGFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 244 EAISIGKYLKG-SLAYAEDPCGAEQGfsgrEVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFW-TMQG 321
Cdd:COG4948 197 EAIRLLRALEDlGLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 322 SVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGkITAIDTH---WIWQEgnqrLTKEPFEIKGGMVQVPTKPGL 398
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDgplLLADD----LVEDPLRIEDGYLTVPDGPGL 347
|
410
....*....|..
gi 446029258 399 GVELDMDQVMKA 410
Cdd:COG4948 348 GVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
188-405 |
2.89e-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: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 188 VVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAISIGKYLKG-SLAYAEDPCGA 265
Cdd:pfam13378 2 LAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEElGLLWIEEPVPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 266 EQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVAQMCHEFGLTWGSHSNNHF 344
Cdd:pfam13378 82 DD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446029258 345 dISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDMD 405
Cdd:pfam13378 158 -IGLAASLHLAAAVPNLLIQEYFLDPLLLE-DDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-284 |
5.54e-16 |
|
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: 73.08 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 185 PETVVRLAEAAYEKYGFNDFKLKGGVlAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAISIGKYLKG-SLAYAEDP 262
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDElGLEWIEEP 79
|
90 100
....*....|....*....|..
gi 446029258 263 CGAEQGfsgrEVMAEFRRATGL 284
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
113-410 |
1.06e-08 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 56.83 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgYLFFVGNRkatplpyqsqpdeqcdwyrlrheeamtPETVVRLA 192
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 193 EAAYEKyGFNDFKLKG----GVLAGEEEAESIVAlakRFPQAR--------VTLDPNGAWSLNEAISIGKYLKG-SLAYA 259
Cdd:PRK14017 133 RARVER-GFTAVKMNGteelQYIDSPRKVDAAVA---RVAAVReavgpeigIGVDFHGRVHKPMAKVLAKELEPyRPMFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 260 EDPCGAEQgfsgREVMAEFRRATGLPtatnmIAT--------DWRQMghtLSLQSVDIPLADPhfwTMQGSV----RVAQ 327
Cdd:PRK14017 209 EEPVLPEN----AEALPEIAAQTSIP-----IATgerlfsrwDFKRV---LEAGGVDIIQPDL---SHAGGItecrKIAA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 328 MCHEFGLTWGSHsNNHFDISLAMFTHVAAAAPGKI---TAIDTHWiwQEGNQRL----TKEPFEIKGGMVQVPTKPGLGV 400
Cdd:PRK14017 274 MAEAYDVALAPH-CPLGPIALAACLQVDAVSPNAFiqeQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGI 350
|
330
....*....|
gi 446029258 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: 952.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 5 FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVL 84
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 85 TAVRNQFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPY 164
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 165 QSQPDEQCDWYRLRHEEAMTPETVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNE 244
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 245 AISIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTMQGSVR 324
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 325 VAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDM 404
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446029258 405 DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR 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: 716.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 9 VVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGG-EKIRKTLEDAIPLVVGKTLGEYKNVLTAV 87
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 88 RNQFADRDAGGRGLQTFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQqRSEVEMLGYLFFVGNRKATPLPYQsq 167
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 168 pdeqcdWYRLRHEEAMTPETVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAIS 247
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 248 IGKYLKGSLAYAEDPCGaeqgfsGREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVA 326
Cdd:cd03323 232 LAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 327 QMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDMDQ 406
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
410
....*....|.
gi 446029258 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 |
4.33e-81 |
|
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: 254.36 E-value: 4.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 10 VTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIP----GGEKIRKTLEDAI-PLVVGKTLGEYKNVL 84
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 85 TAVRNqfadrdaggrglqtfDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpy 164
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPVYATL------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 165 qsqpdeqcdwyrlrheEAMTPETVVRLAEAAYEkYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLN 243
Cdd:COG4948 134 ----------------GIDTPEEMAEEAREAVA-RGFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 244 EAISIGKYLKG-SLAYAEDPCGAEQGfsgrEVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFW-TMQG 321
Cdd:COG4948 197 EAIRLLRALEDlGLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 322 SVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPGkITAIDTH---WIWQEgnqrLTKEPFEIKGGMVQVPTKPGL 398
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDgplLLADD----LVEDPLRIEDGYLTVPDGPGL 347
|
410
....*....|..
gi 446029258 399 GVELDMDQVMKA 410
Cdd:COG4948 348 GVELDEDALARY 359
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
10-401 |
5.66e-54 |
|
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: 183.97 E-value: 5.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 10 VTEMQVIPVAGHDSMlmnlSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEKIR---KTLEDAI-PLVVGKTLGEYKNVLT 85
Cdd:cd03316 2 ITDVETFVLRVPLPE----PGGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSavaAAIEDLLaPLLIGRDPLDIERLWE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 86 AVRNQFADRDAGGrglqtfdlrTTIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyq 165
Cdd:cd03316 78 KLYRRLFWRGRGG---------VAMAAISAVDIALWDIKGKAAGVPVYKLLG-GKVRDRVRVYASG-------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 166 sqpdeqcdWYRLRheeamTPETVVRLAEAAYEKyGFNDFKLKGGVLAG-----EEEAESIVALAKRF-PQARVTLDPNGA 239
Cdd:cd03316 134 --------GGYDD-----SPEELAEEAKRAVAE-GFTAVKLKVGGPDSggedlREDLARVRAVREAVgPDVDLMVDANGR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 240 WSLNEAISIGKYLKGS-LAYAEDPCGAEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT 318
Cdd:cd03316 200 WDLAEAIRLARALEEYdLFWFEEPVPPDD----LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 319 -MQGSVRVAQMCHEFGLTWGSHSNNHfDISLAMFTHVAAAAPGkITAIDTHWIWQEGNQRLTKEPFEIKGGMVQVPTKPG 397
Cdd:cd03316 276 gITEAKKIAALAEAHGVRVAPHGAGG-PIGLAASLHLAAALPN-FGILEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPG 353
|
....
gi 446029258 398 LGVE 401
Cdd:cd03316 354 LGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
188-405 |
2.89e-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: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 188 VVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAISIGKYLKG-SLAYAEDPCGA 265
Cdd:pfam13378 2 LAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEElGLLWIEEPVPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 266 EQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWT-MQGSVRVAQMCHEFGLTWGSHSNNHF 344
Cdd:pfam13378 82 DD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446029258 345 dISLAMFTHVAAAAPGKITAIDTHWIWQEGnQRLTKEPFEIKGGMVQVPTKPGLGVELDMD 405
Cdd:pfam13378 158 -IGLAASLHLAAAVPNLLIQEYFLDPLLLE-DDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
13-367 |
1.77e-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: 175.98 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 13 MQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEipggekirktledaiplvvgktlgeyknvltavrnqfa 92
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 93 drdaggrglqtfdlrttihVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyqsqpdeqc 172
Cdd:cd00308 43 -------------------VISGIDMALWDLAAKALGVPLAELLG-GGSRDRVPAYGSI--------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 173 dwyrlrheeamtpetvvrlaeaayekygfndfklkggvlageeeaESIVALAKRFP-QARVTLDPNGAWSLNEAISIGKY 251
Cdd:cd00308 82 ---------------------------------------------ERVRAVREAFGpDARLAVDANGAWTPKEAIRLIRA 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 252 L-KGSLAYAEDPCGAEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDIPLADPHFWTM-QGSVRVAQMC 329
Cdd:cd00308 117 LeKYGLAWIEEPCAPDD----LEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGlTESRRAADLA 192
|
330 340 350
....*....|....*....|....*....|....*...
gi 446029258 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 |
5.46e-22 |
|
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: 96.62 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 40 IVIIKDNSGHTGVGE--IPGG--------EKIRKTLEDAI-PLVVGKtlgeyknvltAVRNQfadrdagGRGLQTFDLRT 108
Cdd:cd03318 32 LVRLTTSDGVVGIGEatTPGGpawggespETIKAIIDRYLaPLLIGR----------DATNI-------GAAMALLDRAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 109 TIHVV--TGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYLffvgnrkatplpyqSQPDEQCDwyrlrheeamtpe 186
Cdd:cd03318 95 AGNLFakAAIEMALLDAQGRRLGLPVSELLG-GRVRDSLPVAWTL--------------ASGDTERD------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 187 tvVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAKRFP-QARVTLDPNGAWSLNEAISIGKYLKGS-LAYAEDPCG 264
Cdd:cd03318 147 --IAEAEEMLEAGRHRRFKLKMGARPPADDLAHVEAIAKALGdRASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 265 AEQgfsgREVMAEFRRATGLPTATNMIATDWRQMGHTLSLQSVDI-PLADPHFWTMQGSVRVAQMCHEFGLtwGSHSNNH 343
Cdd:cd03318 225 REN----LDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVfSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTM 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 344 FD--ISLAMFTHVAAAAPGkIT----AIDTHWIWQEgnqrLTKEPFEIKGGMVQVPTKPGLGVELDMDQV 407
Cdd:cd03318 299 LEssIGTAASAHLFATLPS-LPfgceLFGPLLLAED----LLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-284 |
5.54e-16 |
|
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: 73.08 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 185 PETVVRLAEAAYEKYGFNDFKLKGGVlAGEEEAESIVALAKRF-PQARVTLDPNGAWSLNEAISIGKYLKG-SLAYAEDP 262
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDElGLEWIEEP 79
|
90 100
....*....|....*....|..
gi 446029258 263 CGAEQGfsgrEVMAEFRRATGL 284
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
113-403 |
4.93e-14 |
|
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: 73.13 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgylffvgnrkatplpYQsqpdeqcdwyrlrHEEAMTPETVVRLA 192
Cdd:cd03325 82 ISGIDQALWDIKGKVLGVPVHQLLG-GQVRDRVRV----------------YS-------------WIGGDRPSDVAEAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 193 EAAYEKyGFNDFKLkggVLAGE----EEAESIVALAKRF--------PQARVTLDPNGAWSLNEAISIGKYLKG-SLAYA 259
Cdd:cd03325 132 RARREA-GFTAVKM---NATEElqwiDTSKKVDAAVERVaalreavgPDIDIGVDFHGRVSKPMAKDLAKELEPyRLLFI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 260 EDPCGAEQgfsgREVMAEFRRATGLPTATN--MIAT-DWRQMghtLSLQSVDIPLAD-PHFWTMQGSVRVAQMCHEFGLT 335
Cdd:cd03325 208 EEPVLPEN----VEALAEIAARTTIPIATGerLFSRwDFKEL---LEDGAVDIIQPDiSHAGGITELKKIAAMAEAYDVA 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446029258 336 WGSHsNNHFDISLAMFTHVAAAAP--------GKITAIDTHWIWQEGnqrLTKEPFEIKGGMVQVPTKPGLGVELD 403
Cdd:cd03325 281 LAPH-CPLGPIALAASLHVDASTPnfliqeqsLGIHYNEGDDLLDYL---VDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
115-335 |
6.46e-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: 71.60 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 115 GIEAAMLDLLGQHLGVNVASLLGDGQQRSEVE-MLGylffvgnrkatplpyqsqpdeqcdwyrlrheeAMTPETVVRLAE 193
Cdd:cd03315 47 AVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAhMLG--------------------------------LGEPAEVAEEAR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 194 AAYEkYGFNDFKLKGGVLAgEEEAESIVALAKRFPQ-ARVTLDPNGAWSLNEAISIGKYLKGS-LAYAEDPCGAEQgfsg 271
Cdd:cd03315 95 RALE-AGFRTFKLKVGRDP-ARDVAVVAALREAVGDdAELRVDANRGWTPKQAIRALRALEDLgLDYVEQPLPADD---- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446029258 272 REVMAEFRRATGLPTATN---MIATDWRQMGHTLSLQSVDIPLADPHFWTmqGSVRVAQMCHEFGLT 335
Cdd:cd03315 169 LEGRAALARATDTPIMADesaFTPHDAFRELALGAADAVNIKTAKTGGLT--KAQRVLAVAEALGLP 233
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
185-359 |
9.89e-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: 64.97 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 185 PETVVRLAEAAYEKyGFNDFKLKGGVLAGEEEAESIVALAKRFP-QARVTLDPNGAWSLNEAISIGKYL-KGSLAYAEDP 262
Cdd:cd03320 83 DAAALGEAKAAYGG-GYRTVKLKVGATSFEEDLARLRALREALPaDAKLRLDANGGWSLEEALAFLEALaAGRIEYIEQP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 263 CGAEQgfsgreVMAEFRRATGLPtatnmIATDwrqmgHTLSLQSVDIPLADPHfW--------TMQGSVR----VAQMCH 330
Cdd:cd03320 162 LPPDD------LAELRRLAAGVP-----IALD-----ESLRRLDDPLALAAAG-AlgalvlkpALLGGPRalleLAEEAR 224
|
170 180 190
....*....|....*....|....*....|..
gi 446029258 331 EFGL-TWGSHSnnhFD--ISLAMFTHVAAAAP 359
Cdd:cd03320 225 ARGIpAVVSSA---LEssIGLGALAHLAAALP 253
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
40-409 |
1.73e-10 |
|
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: 62.25 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 40 IVIIKDNSGHTGVGEIPGGEKIRKTLED-----------AIPLVVGKTLGEYKNVLTAVR----NQFAdrdaggrglqtf 104
Cdd:cd03317 28 IVELTDEEGITGYGEVVAFEGPFYTEETnatawhilkdyLLPLLLGREFSHPEEVSERLApikgNNMA------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 105 dlrttihvVTGIEAAMLDLLGQHLGVNVASLLGdgQQRSEVEM---LGylffvgnrkatplpyQSQPDEQcdwyrlrhee 181
Cdd:cd03317 96 --------KAGLEMAVWDLYAKAQGQSLAQYLG--GTRDSIPVgvsIG---------------IQDDVEQ---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 182 amTPETVVRLAEAAYEKygfndFKLKggvLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAISIGKYLKGSLAYAED 261
Cdd:cd03317 141 --LLKQIERYLEEGYKR-----IKLK---IKPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 262 PCGAEQGFSGREVMAEF----------------RRATGLPTAT--NM-IAtdwRQMGHTLSLQSVDI-PLADPHFWtmqg 321
Cdd:cd03317 211 PLAADDLIDHAELQKLLktpicldesiqsaedaRKAIELGACKiiNIkPG---RVGGLTEALKIHDLcQEHGIPVW---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 322 svrVAQMChEFGLtwGSHSNNHFDiSLAMFTHvaaaaPGKITAIDTHWIwqegnQRLTKEPFEIKGGMVQVPTKPGLGVE 401
Cdd:cd03317 284 ---CGGML-ESGI--GRAHNVALA-SLPNFTY-----PGDISASSRYFE-----EDIITPPFELENGIISVPTGPGIGVT 346
|
....*...
gi 446029258 402 LDMDQVMK 409
Cdd:cd03317 347 VDREALKK 354
|
|
| 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 ... |
40-285 |
3.61e-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: 57.97 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 40 IVIIKDnSGHTGVGEIPG-----GE---KIRKTLEDAIPLVVGKTLgEYKNVLTAVrNQFADRDAGGRglqtfdlrttih 111
Cdd:cd03319 29 IVEIEL-DGITGYGEAAPtprvtGEtveSVLAALKSVRPALIGGDP-RLEKLLEAL-QELLPGNGAAR------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 112 vvTGIEAAMLDLLGQHLGVNVASLLGDGQQRsevemlgylffvgnrkatPLPYqsqpdeqcdwyrlrheeAMT-----PE 186
Cdd:cd03319 94 --AAVDIALWDLEAKLLGLPLYQLWGGGAPR------------------PLET-----------------DYTisidtPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 187 TVVRLAEAaYEKYGFNDFKLKGGvLAGEEEAESIVALAKRFPQARVTLDPNGAWSLNEAISIGKYLKGS-LAYAEDPCGA 265
Cdd:cd03319 137 AMAAAAKK-AAKRGFPLLKIKLG-GDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELgVELIEQPVPA 214
|
250 260
....*....|....*....|
gi 446029258 266 EQgfsgREVMAEFRRATGLP 285
Cdd:cd03319 215 GD----DDGLAYLRDKSPLP 230
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
113-410 |
1.06e-08 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 56.83 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 113 VTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMlgYLFFVGNRkatplpyqsqpdeqcdwyrlrheeamtPETVVRLA 192
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 193 EAAYEKyGFNDFKLKG----GVLAGEEEAESIVAlakRFPQAR--------VTLDPNGAWSLNEAISIGKYLKG-SLAYA 259
Cdd:PRK14017 133 RARVER-GFTAVKMNGteelQYIDSPRKVDAAVA---RVAAVReavgpeigIGVDFHGRVHKPMAKVLAKELEPyRPMFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 260 EDPCGAEQgfsgREVMAEFRRATGLPtatnmIAT--------DWRQMghtLSLQSVDIPLADPhfwTMQGSV----RVAQ 327
Cdd:PRK14017 209 EEPVLPEN----AEALPEIAAQTSIP-----IATgerlfsrwDFKRV---LEAGGVDIIQPDL---SHAGGItecrKIAA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 328 MCHEFGLTWGSHsNNHFDISLAMFTHVAAAAPGKI---TAIDTHWiwQEGNQRL----TKEPFEIKGGMVQVPTKPGLGV 400
Cdd:PRK14017 274 MAEAYDVALAPH-CPLGPIALAACLQVDAVSPNAFiqeQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGI 350
|
330
....*....|
gi 446029258 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 |
2.14e-07 |
|
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: 52.48 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 65 LEDAIPLVVGKTLgeyknVLTAVRNQFADRD--AGGRGLQTFDLrttihvvTGIEAAMLDLLGQHLGVNVASLLGdgqqr 142
Cdd:cd03321 63 LDDMAALLVGEPL-----APAELERALAKRFrlLGYTGLVRMAA-------AGIDMAAWDALAKVHGLPLAKLLG----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 143 sevemlgylffvgnrkATPLPYQSQPDEQCDWYRLRHEEAmtpetvVRLAEAayekyGFNDFKLKGGVLAGEEEAESIVA 222
Cdd:cd03321 126 ----------------GNPRPVQAYDSHGLDGAKLATERA------VTAAEE-----GFHAVKTKIGYPTADEDLAVVRS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 223 LAKRFP-QARVTLDPNGAWSLNEAISIGKYLKGS-LAYAEDPCGAEQgfsgREVMAEFRRATGLPTatnMIATDW---RQ 297
Cdd:cd03321 179 IRQAVGdGVGLMVDYNQSLTVPEAIERGQALDQEgLTWIEEPTLQHD----YEGHARIASALRTPV---QMGENWlgpEE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 298 MGHTLSLQSVDIPLAD-PHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDIslamftHVAAAAPgkiTAidtHWI----WQ 372
Cdd:cd03321 252 MFKALSAGACDLVMPDlMKIGGVTGWLRASALAEQAGIPMSSHLFQEISA------HLLAVTP---TA---HWLeyvdWA 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 446029258 373 EGnqrLTKEPFEIKGGMVQVPTKPGLGVELDMDQVMK 409
Cdd:cd03321 320 GA---ILEPPLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
109-410 |
1.60e-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: 43.58 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 109 TIHVVTGIEAAMLDLLGQHLGVNVASLLGdGQQRSEVEMLGYlffvGNRKATPLPYQSQPDEQCDWYRlrHEEAMTPetv 188
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLG-GKSRDGIMVYSH----ASGRDIPELLEAVERHLAQGYR--AIRVQLP--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 189 vRLAEAAYEKYGFNDFKLKGGvlageeeaesivalakrfpQARVTldPNgawslnEAISIGKYLKGS-LAYAEDPCGAEQ 267
Cdd:cd03322 151 -KLFEAVREKFGFEFHLLHDV-------------------HHRLT--PN------QAARFGKDVEPYrLFWMEDPTPAEN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 268 gfsgREVMAEFRRATGLPTAT----NMIAtDWRQMghtLSLQSVD-IPLADPHFWTMQGSVRVAQMCHEFGLTWGSH--- 339
Cdd:cd03322 203 ----QEAFRLIRQHTATPLAVgevfNSIW-DWQNL---IQERLIDyIRTTVSHAGGITPARKIADLASLYGVRTGWHgpt 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446029258 340 --------SNNHFDISLAMFthvaaaapgkitAIDTHWIWQEGNQRLTKEPFEIKGGMVQVPTKPGLGVELDMDQVMKA 410
Cdd:cd03322 275 dlspvgmaAALHLDLWVPNF------------GIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
228-287 |
2.66e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 2.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446029258 228 PQARVTLDPNGAWSLNEAISIGKYLK--GSLAYAEDPCGaeqgfSGREvMAEFRRATGLPTA 287
Cdd:PRK02901 133 PDGRVRVDANGGWSVDEAVAAARALDadGPLEYVEQPCA-----TVEE-LAELRRRVGVPIA 188
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
146-287 |
6.42e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 41.75 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446029258 146 EMLGYLFFVGNRKATPLPYQsQPDEQCDwyRLRheeAMTPETVVrlaeaayekygfndfKLKGGVLAGEEEAESIVALAK 225
Cdd:PRK05105 95 ELAGTLPQAANYRTAPLCYG-DPDELIL--KLA---DMPGEKVA---------------KVKVGLYEAVRDGMLVNLLLE 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446029258 226 RFPQARVTLDPNGAWSLNEAISIGKYLK----GSLAYAEDPCGAeqgfsgREVMAEFRRATGLPTA 287
Cdd:PRK05105 154 AIPDLKLRLDANRGWTLEKAQQFAKYVPpdyrHRIAFLEEPCKT------PDDSRAFARATGIAIA 213
|
|
| |
