|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
5-445 |
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: 742.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 5 SSPVITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAPGGEVIYQTLVDAIPMVLGQEIARLNKVVQ 84
Cdd:TIGR03247 2 TTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 85 QVHkgNQAADFDTFGKGAWTFELR--VNAVAALEAALLDLLGKALNVPVCELLGPGKQRDAVTVLGYLFYVGDRTKTDLP 162
Cdd:TIGR03247 82 DVR--ATFADRDAGGRGLQTFDLRttIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 163 YLESTPGSHAWYRLRHQQALNSEAVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRFPDARITVDPNGAWLLD 242
Cdd:TIGR03247 160 YRSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 243 EAIALCKGLNDVLTYAEDPCGAEQGFSGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWTLSGAV 322
Cdd:TIGR03247 240 EAIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 323 RVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELD 402
Cdd:TIGR03247 320 RVAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDGQ-RLTKEPLEIKGGKIQVPDKPGLGVEID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490239003 403 WEQVQKAHEAYTRLPGGARNDAGPMQYLIPGWTFDRKRPVFGR 445
Cdd:TIGR03247 399 MDAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
8-416 |
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: 586.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 8 VITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAPGG-EVIYQTLVDAIPMVLGQEIARLNKVVQQV 86
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 87 HkgNQAADFDTFGKGAWTFELRV--NAVAALEAALLDLLGKALNVPVCELLGpGKQRDAVTVLGYLFYVGDRTKTDLPYL 164
Cdd:cd03323 81 R--VAFADRDAGGRGLQTFDLRTtvHVVTAFEVALLDLLGQALGVPVADLLG-GGQRDSVPFLAYLFYKGDRHKTDLPYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 165 estpgshaWYRLRHQQALNSEAVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRFPDARITVDPNGAWLLDEA 244
Cdd:cd03323 158 --------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 245 IALCKGLNDVLTYAEDPCGaeqgfsGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVR 323
Cdd:cd03323 230 IRLAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 324 VAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELDW 403
Cdd:cd03323 304 VAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDGQ-VITGEPLRIKDGKVAVPDKPGLGVELDR 382
|
410
....*....|...
gi 490239003 404 EQVQKAHEAYTRL 416
Cdd:cd03323 383 DKLAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
9-409 |
8.00e-83 |
|
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: 258.98 E-value: 8.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 9 ITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAP----GGEVIYQTLVDAI-PMVLGQEIARLNKVV 83
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 84 QQVHKGNQAAdfdTFGKGA-----WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQRDAVTVLGYLFYvgdrtk 158
Cdd:COG4948 83 QRLYRALPGN---PAAKAAvdmalW--DLL---------------GKALGVPVYQLLG-GKVRDRVPVYATLGI------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 159 tdlpyleSTPgshawyrlrhqqalnsEAVVRLAEAAQDRyGFKDFKLKGGVLPGEQEIETARALKKRF-PDARITVDPNG 237
Cdd:COG4948 136 -------DTP----------------EEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 238 AWLLDEAIALCKGLNDV-LTYAEDPCGAEQGfsgrEVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFW 316
Cdd:COG4948 192 AWTLEEAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 317 -TLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDTHW-IWQEGDcrLTKNPLEIKHGKIAVPDA 394
Cdd:COG4948 268 gGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALP-NFDIVELDGpLLLADD--LVEDPLRIEDGYLTVPDG 344
|
410
....*....|....*
gi 490239003 395 PGLGVELDWEQVQKA 409
Cdd:COG4948 345 PGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
186-404 |
1.17e-58 |
|
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: 191.62 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 186 AVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCG 263
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 264 AEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNH 342
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239003 343 FdISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELDWE 404
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLLED-DLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-283 |
1.21e-18 |
|
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: 80.79 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 185 EAVVRLAEAAQDRYGFKDFKLKGGVlPGEQEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPC 262
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEPV 80
|
90 100
....*....|....*....|.
gi 490239003 263 GAEQGfsgrEVMAEFRRATGL 283
Cdd:smart00922 81 PPDDL----EGLAELRRATPI 97
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
124-409 |
1.42e-06 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 50.28 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGpGKQRDAVTVlgYLFYVGDRtktdlpylestpgshawyrlrhqqalnSEAVVRLAEAAQDRyGFKDF 203
Cdd:PRK14017 95 GKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARVER-GFTAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLKGgvlPGE-QEIETARALKK---RF--------PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:PRK14017 144 KMNG---TEElQYIDSPRKVDAavaRVaavreavgPEIGIGVDFHGRVHKPMAKVLAKELEPYrPMFIEEPVLPEN---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLADP-HFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:PRK14017 217 AEALPEIAAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLGPIALA 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239003 349 MFTHVGAAAPgNPT----AIDTHwiWQEG----DCRLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQKA 409
Cdd:PRK14017 295 ACLQVDAVSP-NAFiqeqSLGIH--YNQGadllDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRER 360
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
5-445 |
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: 742.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 5 SSPVITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAPGGEVIYQTLVDAIPMVLGQEIARLNKVVQ 84
Cdd:TIGR03247 2 TTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 85 QVHkgNQAADFDTFGKGAWTFELR--VNAVAALEAALLDLLGKALNVPVCELLGPGKQRDAVTVLGYLFYVGDRTKTDLP 162
Cdd:TIGR03247 82 DVR--ATFADRDAGGRGLQTFDLRttIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 163 YLESTPGSHAWYRLRHQQALNSEAVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRFPDARITVDPNGAWLLD 242
Cdd:TIGR03247 160 YRSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 243 EAIALCKGLNDVLTYAEDPCGAEQGFSGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWTLSGAV 322
Cdd:TIGR03247 240 EAIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 323 RVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELD 402
Cdd:TIGR03247 320 RVAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDGQ-RLTKEPLEIKGGKIQVPDKPGLGVEID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490239003 403 WEQVQKAHEAYTRLPGGARNDAGPMQYLIPGWTFDRKRPVFGR 445
Cdd:TIGR03247 399 MDAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
8-416 |
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: 586.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 8 VITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAPGG-EVIYQTLVDAIPMVLGQEIARLNKVVQQV 86
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 87 HkgNQAADFDTFGKGAWTFELRV--NAVAALEAALLDLLGKALNVPVCELLGpGKQRDAVTVLGYLFYVGDRTKTDLPYL 164
Cdd:cd03323 81 R--VAFADRDAGGRGLQTFDLRTtvHVVTAFEVALLDLLGQALGVPVADLLG-GGQRDSVPFLAYLFYKGDRHKTDLPYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 165 estpgshaWYRLRHQQALNSEAVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRFPDARITVDPNGAWLLDEA 244
Cdd:cd03323 158 --------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 245 IALCKGLNDVLTYAEDPCGaeqgfsGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVR 323
Cdd:cd03323 230 IRLAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 324 VAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELDW 403
Cdd:cd03323 304 VAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDGQ-VITGEPLRIKDGKVAVPDKPGLGVELDR 382
|
410
....*....|...
gi 490239003 404 EQVQKAHEAYTRL 416
Cdd:cd03323 383 DKLAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
9-409 |
8.00e-83 |
|
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: 258.98 E-value: 8.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 9 ITDMKVIPVAGQDSMLLNIGGAHNAYFTRNIVVLTDSAGNTGVGEAP----GGEVIYQTLVDAI-PMVLGQEIARLNKVV 83
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 84 QQVHKGNQAAdfdTFGKGA-----WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQRDAVTVLGYLFYvgdrtk 158
Cdd:COG4948 83 QRLYRALPGN---PAAKAAvdmalW--DLL---------------GKALGVPVYQLLG-GKVRDRVPVYATLGI------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 159 tdlpyleSTPgshawyrlrhqqalnsEAVVRLAEAAQDRyGFKDFKLKGGVLPGEQEIETARALKKRF-PDARITVDPNG 237
Cdd:COG4948 136 -------DTP----------------EEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 238 AWLLDEAIALCKGLNDV-LTYAEDPCGAEQGfsgrEVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFW 316
Cdd:COG4948 192 AWTLEEAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 317 -TLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDTHW-IWQEGDcrLTKNPLEIKHGKIAVPDA 394
Cdd:COG4948 268 gGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALP-NFDIVELDGpLLLADD--LVEDPLRIEDGYLTVPDG 344
|
410
....*....|....*
gi 490239003 395 PGLGVELDWEQVQKA 409
Cdd:COG4948 345 PGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
186-404 |
1.17e-58 |
|
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: 191.62 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 186 AVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCG 263
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 264 AEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNH 342
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239003 343 FdISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTKNPLEIKHGKIAVPDAPGLGVELDWE 404
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLLED-DLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
9-400 |
1.30e-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: 182.81 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 9 ITDMKVIPVAGQDSMLLNIGGAHNAYFTRnivvLTDSAGNTGVGEAPGG---EVIYQTLVDAI-PMVLGQEIARLNKVVQ 84
Cdd:cd03316 2 ITDVETFVLRVPLPEPGGAVTWRNLVLVR----VTTDDGITGWGEAYPGgrpSAVAAAIEDLLaPLLIGRDPLDIERLWE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 85 QVHKGNQAADFDTFGKGA--------WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQRDAVTVLGYLFYVGDR 156
Cdd:cd03316 78 KLYRRLFWRGRGGVAMAAisavdialW--DIK---------------GKAAGVPVYKLLG-GKVRDRVRVYASGGGYDDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 157 TktdlpylestpgshawyrlrhqqalnsEAVVRLAEAAQDRyGFKDFKLKGGVLPGEQE-----IETARALKKRF-PDAR 230
Cdd:cd03316 140 P---------------------------EELAEEAKRAVAE-GFTAVKLKVGGPDSGGEdlredLARVRAVREAVgPDVD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 231 ITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIP 309
Cdd:cd03316 192 LMVDANGRWDLAEAIRLARALEEYdLFWFEEPVPPDD----LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDII 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 310 LADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNHfDISLAMFTHVGAAAPgNPTAIDTHWIWQEGDCRLTKNPLEIKHGK 388
Cdd:cd03316 268 QPDVTKVGgITEAKKIAALAEAHGVRVAPHGAGG-PIGLAASLHLAAALP-NFGILEYHLDDLPLREDLFKNPPEIEDGY 345
|
410
....*....|..
gi 490239003 389 IAVPDAPGLGVE 400
Cdd:cd03316 346 VTVPDRPGLGVE 357
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
216-366 |
1.01e-40 |
|
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: 145.16 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 216 IETARALKKRFP-DARITVDPNGAWLLDEAIALCKGLND-VLTYAEDPCGAEQgfsgREVMAEFRRATGLPVATNMIATN 293
Cdd:cd00308 81 IERVRAVREAFGpDARLAVDANGAWTPKEAIRLIRALEKyGLAWIEEPCAPDD----LEGYAALRRRTGIPIAADESVTT 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490239003 294 WREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDT 366
Cdd:cd00308 157 VDDALEALELGAVDILQIKPTRVGgLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALP-NDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
39-408 |
7.96e-28 |
|
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: 113.57 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 39 IVVLTDSAGNTGVGEA--PGG--------EVIYQTLVDAI-PMVLGQEIARLNKVVQQVHKgnqAADFDTFGKGAWTFEL 107
Cdd:cd03318 32 LVRLTTSDGVVGIGEAttPGGpawggespETIKAIIDRYLaPLLIGRDATNIGAAMALLDR---AVAGNLFAKAAIEMAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 108 rvnavaaleaalLDLLGKALNVPVCELLGpGKQRDAVTVlgylfyvgdrtktdlpylestpgshAWyrlrhqqALNSEAV 187
Cdd:cd03318 109 ------------LDAQGRRLGLPVSELLG-GRVRDSLPV-------------------------AW-------TLASGDT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 188 VR-LAEAAQ--DRYGFKDFKLKGGVLPGEQEIETARALKKRFPD-ARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPC 262
Cdd:cd03318 144 ERdIAEAEEmlEAGRHRRFKLKMGARPPADDLAHVEAIAKALGDrASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 263 GAEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDI-PLADPHFWTLSGAVRVAQLCDDWGLtwGCHSNN 341
Cdd:cd03318 224 PREN----LDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVfSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGT 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490239003 342 HFD--ISLAMFTHVGAAAPGNP--TAIDTHWIWQEgdcRLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03318 298 MLEssIGTAASAHLFATLPSLPfgCELFGPLLLAE---DLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-283 |
1.21e-18 |
|
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: 80.79 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 185 EAVVRLAEAAQDRYGFKDFKLKGGVlPGEQEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPC 262
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEPV 80
|
90 100
....*....|....*....|.
gi 490239003 263 GAEQGfsgrEVMAEFRRATGL 283
Cdd:smart00922 81 PPDDL----EGLAELRRATPI 97
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
124-363 |
5.83e-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: 80.46 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGPgkQRDAVTVlGYLFYVGDRtktdlpylestpgshawyrlrhqqalnsEAVVRLAEAAqDRYGFKDF 203
Cdd:cd03315 57 GKRLGVPVYLLLGG--YRDRVRV-AHMLGLGEP----------------------------AEVAEEARRA-LEAGFRTF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLKGGVLPgEQEIETARALKKRFP-DARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRAT 281
Cdd:cd03315 105 KLKVGRDP-ARDVAVVAALREAVGdDAELRVDANRGWTPKQAIRALRALEDLgLDYVEQPLPADD----LEGRAALARAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 282 GLPVATNMIATNWREMGHAVMLNAVD---IPLADPHFwtLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAP 358
Cdd:cd03315 180 DTPIMADESAFTPHDAFRELALGAADavnIKTAKTGG--LTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALR 257
|
....*
gi 490239003 359 GNPTA 363
Cdd:cd03315 258 AVTLP 262
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
184-286 |
1.83e-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: 67.28 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 184 SEAVVRLAEAAQDRYGFKDFKLKGGVLPGEQEIETARALKKRFP-DARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDP 261
Cdd:cd03320 82 GDAAALGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPaDAKLRLDANGGWSLEEALAFLEALAAGrIEYIEQP 161
|
90 100
....*....|....*....|....*
gi 490239003 262 CGAEQgfsgreVMAEFRRATGLPVA 286
Cdd:cd03320 162 LPPDD------LAELRRLAAGVPIA 180
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
124-402 |
4.38e-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: 66.97 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGpGKQRDAVTVlgYLFYVGDRTKTdlpylestpgshawyrlrhqqalnseaVVRLAEAAQDRyGFKDF 203
Cdd:cd03325 94 GKVLGVPVHQLLG-GQVRDRVRV--YSWIGGDRPSD---------------------------VAEAARARREA-GFTAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLkggVLPGEQE-----------IETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:cd03325 143 KM---NATEELQwidtskkvdaaVERVAALREAVgPDIDIGVDFHGRVSKPMAKDLAKELEPYrLLFIEEPVLPEN---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLAD-PHFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:cd03325 216 VEALAEIAARTTIPIATgERLFSRW-DFKELLEDGAVDIIQPDiSHAGGITELKKIAAMAEAYDVALAPH-CPLGPIALA 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239003 349 MFTHVGAAAP--------GNPTAIDTHWIWQEGdcrLTKNPLEIKHGKIAVPDAPGLGVELD 402
Cdd:cd03325 294 ASLHVDASTPnfliqeqsLGIHYNEGDDLLDYL---VDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
39-408 |
1.03e-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: 66.10 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 39 IVVLTDSAGNTGVGEAPGGEV---IYQTLVDA--------IPMVLGQEIARLNKVVQQVH--KGNQAAdfdtfgKGAwtF 105
Cdd:cd03317 28 IVELTDEEGITGYGEVVAFEGpfyTEETNATAwhilkdylLPLLLGREFSHPEEVSERLApiKGNNMA------KAG--L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 106 ELRVnavaaleaalLDLLGKALNVPVCELLGPGKQRDAVTVLgylfyVGDrtktdlpylestpgshawyrlrhQQALnsE 185
Cdd:cd03317 100 EMAV----------WDLYAKAQGQSLAQYLGGTRDSIPVGVS-----IGI-----------------------QDDV--E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 186 AVVRLAEAAQDrYGFKDFKLKggVLPGeQEIETARALKKRFPDARITVDPNGAWLLDEaIALCKGLNDV-LTYAEDPCGA 264
Cdd:cd03317 140 QLLKQIERYLE-EGYKRIKLK--IKPG-WDVEPLKAVRERFPDIPLMADANSAYTLAD-IPLLKRLDEYgLLMIEQPLAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 265 EQGFSGREVMAEFRRA-------TGLPVATNMIatnwrEMGHAVMLNavdipLADPHFWTLSGAVRVAQLCDDWGLTWGC 337
Cdd:cd03317 215 DDLIDHAELQKLLKTPicldesiQSAEDARKAI-----ELGACKIIN-----IKPGRVGGLTEALKIHDLCQEHGIPVWC 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490239003 338 HS------NNHFDISLAmfTHVGAAAPGNPTAIDTHWiwqEGDcrLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03317 285 GGmlesgiGRAHNVALA--SLPNFTYPGDISASSRYF---EED--IITPPFELENGIISVPTGPGIGVTVDREALKK 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 ... |
36-286 |
2.69e-11 |
|
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: 64.52 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 36 TRNIVVLTDSAGNTGVGEAPGGEVIY--------QTLVDAIPMVLGQEIaRLNKVVQQVHK---GNQAAdfdtfgKGA-- 102
Cdd:cd03319 25 AENVIVEIELDGITGYGEAAPTPRVTgetvesvlAALKSVRPALIGGDP-RLEKLLEALQEllpGNGAA------RAAvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 103 ---WtfELRvnavaaleaalldllGKALNVPVCELLGPGKQRD---AVTV-LGylfyvgdrtktdlpylesTPgshawyr 175
Cdd:cd03319 98 ialW--DLE---------------AKLLGLPLYQLWGGGAPRPletDYTIsID------------------TP------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 176 lrhqqalnsEAVVRLAEAAQDRyGFKDFKLKGGvLPGEQEIETARALKKRFPDARITVDPNGAWLLDEAIALCKGLND-V 254
Cdd:cd03319 136 ---------EAMAAAAKKAAKR-GFPLLKIKLG-GDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAElG 204
|
250 260 270
....*....|....*....|....*....|..
gi 490239003 255 LTYAEDPCGAEQgfsgREVMAEFRRATGLPVA 286
Cdd:cd03319 205 VELIEQPVPAGD----DDGLAYLRDKSPLPIM 232
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
190-408 |
2.00e-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: 55.95 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 190 LAEAAQDR------YGFKDFKLKGGVLPGEQEIETARALKKRFPDA-RITVDPNGAWLLDEAIALCKGLNDV-LTYAEDP 261
Cdd:cd03321 141 GAKLATERavtaaeEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGvGLMVDYNQSLTVPEAIERGQALDQEgLTWIEEP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 262 CGAEQgfsgREVMAEFRRATGLPVatnMIATNW---REMGHAVMLNAVDIPLAD-PHFWTLSGAVRVAQLCDDWGLTWGC 337
Cdd:cd03321 221 TLQHD----YEGHARIASALRTPV---QMGENWlgpEEMFKALSAGACDLVMPDlMKIGGVTGWLRASALAEQAGIPMSS 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490239003 338 HSNNHFDISLAMFThvgaaapgnPTAidtHWI----WQEGdcrLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03321 294 HLFQEISAHLLAVT---------PTA---HWLeyvdWAGA---ILEPPLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
124-408 |
1.40e-07 |
|
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: 53.17 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGPGKQRdavtvlgylfyvgdrtktdLPYLESTPGSHAWYRLRHqqalnSEAVVRLAEAAQDRyGFKDF 203
Cdd:cd03329 108 GKYLGLPVHRLLGGYREK-------------------IPAYASTMVGDDLEGLES-----PEAYADFAEECKAL-GYRAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLKGGVLPG-EQEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCgAEQGFSGREVMAEFRR- 279
Cdd:cd03329 163 KLHPWGPGVvRRDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLGRALEELgFFWYEDPL-REASISSYRWLAEKLDi 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 280 ---ATGLPVATNMIATNWremghaVMLNAVDIPLADPHF-WTLSGAVRVAQLCDDWGLTWGCHSNNhfdislAMFTHVGA 355
Cdd:cd03329 242 pilGTEHSRGALESRADW------VLAGATDFLRADVNLvGGITGAMKTAHLAEAFGLDVELHGNG------AANLHVIA 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490239003 356 AAPgNPTAID---THWIWQEGDCRLTKNPLEI---KHGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03329 310 AIR-NTRYYErglLHPSQKYDVYAGYLSVLDDpvdSDGFVHVPKGPGLGVEIDFDYIER 367
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
199-286 |
4.69e-07 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 51.35 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 199 GFKDFKLKGGVLPGEQEIETARALKKRFPD-ARITVDPNGAWLLDEAIALCKGLN----DVLTYAEDPCgaeqgfSGREV 273
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLDANGGLSPDEAQQFLKALDpnlrGRIAFLEEPL------PDADE 197
|
90
....*....|...
gi 490239003 274 MAEFRRATGLPVA 286
Cdd:TIGR01927 198 MSAFSEATGTAIA 210
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
124-409 |
1.42e-06 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 50.28 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGpGKQRDAVTVlgYLFYVGDRtktdlpylestpgshawyrlrhqqalnSEAVVRLAEAAQDRyGFKDF 203
Cdd:PRK14017 95 GKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARVER-GFTAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLKGgvlPGE-QEIETARALKK---RF--------PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:PRK14017 144 KMNG---TEElQYIDSPRKVDAavaRVaavreavgPEIGIGVDFHGRVHKPMAKVLAKELEPYrPMFIEEPVLPEN---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLADP-HFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:PRK14017 217 AEALPEIAAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLGPIALA 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490239003 349 MFTHVGAAAPgNPT----AIDTHwiWQEG----DCRLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQKA 409
Cdd:PRK14017 295 ACLQVDAVSP-NAFiqeqSLGIH--YNQGadllDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRER 360
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
45-402 |
8.67e-06 |
|
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: 47.71 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 45 SAGNTGVGEAPGGEVIYQTLVDAI-PMVLGQEIARLNKVVQQVHKGNQAADfdtfGKGawtfeLRVNAVAALEAALLDLL 123
Cdd:cd03327 19 DDGTVGYANTTGGPVACWIVDQHLaRFLIGKDPSDIEKLWDQMYRATLAYG----RKG-----IAMAAISAVDLALWDLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGpGKQRDAVTvlgylFYvgdrtktdlpylestpGSHAWYrlrhqqalnSEAVVRLAEAAQ-DRYGFKD 202
Cdd:cd03327 90 GKIRGEPVYKLLG-GRTRDKIP-----AY----------------ASGLYP---------TDLDELPDEAKEyLKEGYRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 203 FKLKGGVLPGE------QEIETARALKKRF-PDARITVDPNGAWLLDEAIALCKGLNDV-LTYAEDPCGAEQgFSGrevM 274
Cdd:cd03327 139 MKMRFGYGPSDghaglrKNVELVRAIREAVgYDVDLMLDCYMSWNLNYAIKMARALEKYeLRWIEEPLIPDD-IEG---Y 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 275 AEFRRATGLPVAT-NMIATNW--REMghaVMLNAVDIPLADPHfWT--LSGAVRVAQLCDDWGLTWGCHSNNHFDISLAM 349
Cdd:cd03327 215 AELKKATGIPISTgEHEYTVYgfKRL---LEGRAVDILQPDVN-WVggITELKKIAALAEAYGVPVVPHASQIYNYHFIM 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490239003 350 FTHVGAAAPGNPTAIDTHWIWQEGDcrLTKNPLEIKHGKIAVPDAPGLGVELD 402
Cdd:cd03327 291 SEPNSPFAEYLPNSPDEVGNPLFYY--IFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
124-423 |
2.57e-05 |
|
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: 46.28 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 124 GKALNVPVCELLGpGKQRDAVTVLGYlfyvgdRTKTDLPYLESTPGSHAWYRLRHQQAlnseAVVRLAEAAQDRYGFkDF 203
Cdd:cd03322 97 GKAAGMPLYQLLG-GKSRDGIMVYSH------ASGRDIPELLEAVERHLAQGYRAIRV----QLPKLFEAVREKFGF-EF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 204 KLkggvlpgeqeietaralkkrFPDARITVDPNgawlldEAIALCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRATG 282
Cdd:cd03322 165 HL--------------------LHDVHHRLTPN------QAARFGKDVEPYrLFWMEDPTPAEN----QEAFRLIRQHTA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490239003 283 LPVATNMIATNWREMGHAVMLNAVD-IPLADPHFWTLSGAVRVAQLCDDWGLTWGCH-----------SNNHFDISLAMF 350
Cdd:cd03322 215 TPLAVGEVFNSIWDWQNLIQERLIDyIRTTVSHAGGITPARKIADLASLYGVRTGWHgptdlspvgmaAALHLDLWVPNF 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490239003 351 thvgaaapgnptAIDTHWIWQEGDCRLTKNPLEIKHGKIAVPDAPGLGVELDWEQVQKAHEAYTRLPGGARND 423
Cdd:cd03322 295 ------------GIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPVARLED 355
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
227-286 |
2.65e-05 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490239003 227 PDARITVDPNGAWLLDEAIALCKGLN--DVLTYAEDPCgaeqgfSGREVMAEFRRATGLPVA 286
Cdd:PRK02901 133 PDGRVRVDANGGWSVDEAVAAARALDadGPLEYVEQPC------ATVEELAELRRRVGVPIA 188
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
199-244 |
5.63e-03 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 38.84 E-value: 5.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490239003 199 GFKDFKLKGGVLPGEQEIETARALKKRFP-DARITVDPNGAWLLDEA 244
Cdd:PRK02714 133 GYRTFKWKIGVDPLEQELKIFEQLLERLPaGAKLRLDANGGLSLEEA 179
|
|
| |
