|
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: 742.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 5 SSPVITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAPGGDVIYQTLVDAIPMVLGQEVARLNKVVQ 84
Cdd:TIGR03247 2 TTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 85 QVHkgNQAADFDTFGKGAWTFELR--VNAVAALEAALLDLLGKALNVPVCELLGPGKQREAITVLGYLFYIGDRTKTDLP 162
Cdd:TIGR03247 82 DVR--ATFADRDAGGRGLQTFDLRttIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 163 YVENTPGNHEWYQLRHQKAMNSEAVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFPDARITVDPNGAWLLD 242
Cdd:TIGR03247 160 YRSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 243 EAISLCKGLNDVLTYAEDPCGAEQGFSGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWTLSGAV 322
Cdd:TIGR03247 240 EAIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 323 RVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELD 402
Cdd:TIGR03247 320 RVAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDGQ-RLTKEPLEIKGGKIQVPDKPGLGVEID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 882683 403 WEQVQKAHEAYKRLPGGARNDAGPMQYLIPGWTFDRKRPVFGR 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: 583.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 8 VITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAPGGD-VIYQTLVDAIPMVLGQEVARLNKVVQQV 86
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGAeALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 87 HkgNQAADFDTFGKGAWTFELRV--NAVAALEAALLDLLGKALNVPVCELLGpGKQREAITVLGYLFYIGDRTKTDLPYV 164
Cdd:cd03323 81 R--VAFADRDAGGRGLQTFDLRTtvHVVTAFEVALLDLLGQALGVPVADLLG-GGQRDSVPFLAYLFYKGDRHKTDLPYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 165 entpgnheWYQLRHQKAMNSEAVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFPDARITVDPNGAWLLDEA 244
Cdd:cd03323 158 --------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 245 ISLCKGLNDVLTYAEDPCGaeqgfsGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVR 323
Cdd:cd03323 230 IRLAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 324 VAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELDW 403
Cdd:cd03323 304 VAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDGQ-VITGEPLRIKDGKVAVPDKPGLGVELDR 382
|
410
....*....|...
gi 882683 404 EQVQKAHEAYKRL 416
Cdd:cd03323 383 DKLAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
9-409 |
1.74e-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: 260.52 E-value: 1.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 9 ITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAP----GGDVIYQTLVDAI-PMVLGQEVARLNKVV 83
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 84 QQVHKGNQAAdfdTFGKGA-----WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQREAITVLGYLFYigdrtk 158
Cdd:COG4948 83 QRLYRALPGN---PAAKAAvdmalW--DLL---------------GKALGVPVYQLLG-GKVRDRVPVYATLGI------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 159 tdlpyveNTPgnhewyqlrhqkamnsEAVVRLAEASQDRyGFKDFKLKGGVLPGEQEIDTVRALKKRF-PDARITVDPNG 237
Cdd:COG4948 136 -------DTP----------------EEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 238 AWLLDEAISLCKGLNDV-LTYAEDPCGAEQGfsgrEVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFW 316
Cdd:COG4948 192 AWTLEEAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 317 -TLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDTHW-IWQEGDcrLTQNPLEIKNGKIAVPDA 394
Cdd:COG4948 268 gGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALP-NFDIVELDGpLLLADD--LVEDPLRIEDGYLTVPDG 344
|
410
....*....|....*
gi 882683 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 |
4.21e-59 |
|
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: 192.78 E-value: 4.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 186 AVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCG 263
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 264 AEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNH 342
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882683 343 FdISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELDWE 404
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLLED-DLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-283 |
2.80e-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: 79.63 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 185 EAVVRLAEASQDRYGFKDFKLKGGVlPGEQEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPC 262
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEPV 80
|
90 100
....*....|....*....|.
gi 882683 263 GAEQGfsgrEVMAEFRRATGL 283
Cdd:smart00922 81 PPDDL----EGLAELRRATPI 97
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
124-409 |
2.25e-06 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 49.51 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGpGKQREAITVlgYLFYIGDRtktdlpyventpgnhewyqlrhqkamnSEAVVRLAEASQDRyGFKDF 203
Cdd:PRK14017 95 GKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARVER-GFTAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLKGgvlPGE-QEIDTVRALKK---RF--------PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:PRK14017 144 KMNG---TEElQYIDSPRKVDAavaRVaavreavgPEIGIGVDFHGRVHKPMAKVLAKELEPYrPMFIEEPVLPEN---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLADP-HFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:PRK14017 217 AEALPEIAAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLGPIALA 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882683 349 MFTHVGAAAPgNPT----AIDTHwiWQEG----DCRLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQKA 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: 742.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 5 SSPVITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAPGGDVIYQTLVDAIPMVLGQEVARLNKVVQ 84
Cdd:TIGR03247 2 TTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 85 QVHkgNQAADFDTFGKGAWTFELR--VNAVAALEAALLDLLGKALNVPVCELLGPGKQREAITVLGYLFYIGDRTKTDLP 162
Cdd:TIGR03247 82 DVR--ATFADRDAGGRGLQTFDLRttIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 163 YVENTPGNHEWYQLRHQKAMNSEAVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFPDARITVDPNGAWLLD 242
Cdd:TIGR03247 160 YRSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 243 EAISLCKGLNDVLTYAEDPCGAEQGFSGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWTLSGAV 322
Cdd:TIGR03247 240 EAIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 323 RVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELD 402
Cdd:TIGR03247 320 RVAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDGQ-RLTKEPLEIKGGKIQVPDKPGLGVEID 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 882683 403 WEQVQKAHEAYKRLPGGARNDAGPMQYLIPGWTFDRKRPVFGR 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: 583.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 8 VITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAPGGD-VIYQTLVDAIPMVLGQEVARLNKVVQQV 86
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGAeALEALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 87 HkgNQAADFDTFGKGAWTFELRV--NAVAALEAALLDLLGKALNVPVCELLGpGKQREAITVLGYLFYIGDRTKTDLPYV 164
Cdd:cd03323 81 R--VAFADRDAGGRGLQTFDLRTtvHVVTAFEVALLDLLGQALGVPVADLLG-GGQRDSVPFLAYLFYKGDRHKTDLPYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 165 entpgnheWYQLRHQKAMNSEAVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFPDARITVDPNGAWLLDEA 244
Cdd:cd03323 158 --------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 245 ISLCKGLNDVLTYAEDPCGaeqgfsGREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVR 323
Cdd:cd03323 230 IRLAKELEGVLAYLEDPCG------GREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 324 VAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELDW 403
Cdd:cd03323 304 VAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDGQ-VITGEPLRIKDGKVAVPDKPGLGVELDR 382
|
410
....*....|...
gi 882683 404 EQVQKAHEAYKRL 416
Cdd:cd03323 383 DKLAKAHELYQRL 395
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
9-409 |
1.74e-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: 260.52 E-value: 1.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 9 ITDMKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAP----GGDVIYQTLVDAI-PMVLGQEVARLNKVV 83
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEALaPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 84 QQVHKGNQAAdfdTFGKGA-----WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQREAITVLGYLFYigdrtk 158
Cdd:COG4948 83 QRLYRALPGN---PAAKAAvdmalW--DLL---------------GKALGVPVYQLLG-GKVRDRVPVYATLGI------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 159 tdlpyveNTPgnhewyqlrhqkamnsEAVVRLAEASQDRyGFKDFKLKGGVLPGEQEIDTVRALKKRF-PDARITVDPNG 237
Cdd:COG4948 136 -------DTP----------------EEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 238 AWLLDEAISLCKGLNDV-LTYAEDPCGAEQGfsgrEVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFW 316
Cdd:COG4948 192 AWTLEEAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 317 -TLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDTHW-IWQEGDcrLTQNPLEIKNGKIAVPDA 394
Cdd:COG4948 268 gGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALP-NFDIVELDGpLLLADD--LVEDPLRIEDGYLTVPDG 344
|
410
....*....|....*
gi 882683 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 |
4.21e-59 |
|
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: 192.78 E-value: 4.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 186 AVVRLAEASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCG 263
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 264 AEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNH 342
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882683 343 FdISLAMFTHVGAAAPGNPTAIDTHWIWQEGDcRLTQNPLEIKNGKIAVPDAPGLGVELDWE 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 |
8.33e-56 |
|
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: 188.59 E-value: 8.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 9 ITDMKVIPVAGHDSMLLNIGGAHNAYFTRnivvLTDNAGHTGIGEAPGG---DVIYQTLVDAI-PMVLGQEVARLNKVVQ 84
Cdd:cd03316 2 ITDVETFVLRVPLPEPGGAVTWRNLVLVR----VTTDDGITGWGEAYPGgrpSAVAAAIEDLLaPLLIGRDPLDIERLWE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 85 QVHKGNQAADFDTFGKGA--------WtfELRvnavaaleaalldllGKALNVPVCELLGpGKQREAITVLGYLFYIGDR 156
Cdd:cd03316 78 KLYRRLFWRGRGGVAMAAisavdialW--DIK---------------GKAAGVPVYKLLG-GKVRDRVRVYASGGGYDDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 157 TktdlpyventpgnhewyqlrhqkamnsEAVVRLAEASQDRyGFKDFKLKGGVLPGEQE-----IDTVRALKKRF-PDAR 230
Cdd:cd03316 140 P---------------------------EELAEEAKRAVAE-GFTAVKLKVGGPDSGGEdlredLARVRAVREAVgPDVD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 231 ITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIP 309
Cdd:cd03316 192 LMVDANGRWDLAEAIRLARALEEYdLFWFEEPVPPDD----LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDII 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 310 LADPHFWT-LSGAVRVAQLCDDWGLTWGCHSNNHfDISLAMFTHVGAAAPgNPTAIDTHWIWQEGDCRLTQNPLEIKNGK 388
Cdd:cd03316 268 QPDVTKVGgITEAKKIAALAEAHGVRVAPHGAGG-PIGLAASLHLAAALP-NFGILEYHLDDLPLREDLFKNPPEIEDGY 345
|
410
....*....|..
gi 882683 389 IAVPDAPGLGVE 400
Cdd:cd03316 346 VTVPDRPGLGVE 357
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
12-366 |
2.57e-41 |
|
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: 146.70 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 12 MKVIPVAGHDSMLLNIGGAHNAYFTRNIVVLTDNAGHTGIGEAPGGdvIYQTLVDAipmvlgqevarlnkvvqqvhkgnq 91
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEVISG--IDMALWDL------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 92 aadfdtfgkgawtfelrvnavaaleaalldlLGKALNVPVCELLGpGKQREAITVLGYlfyigdrtktdlpyventpgnh 171
Cdd:cd00308 55 -------------------------------AAKALGVPLAELLG-GGSRDRVPAYGS---------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 172 ewyqlrhqkamnseavvrlaeasqdrygfkdfklkggvlpgeqeIDTVRALKKRFP-DARITVDPNGAWLLDEAISLCKG 250
Cdd:cd00308 81 --------------------------------------------IERVRAVREAFGpDARLAVDANGAWTPKEAIRLIRA 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 251 LND-VLTYAEDPCGAEQgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDIPLADPHFWT-LSGAVRVAQLC 328
Cdd:cd00308 117 LEKyGLAWIEEPCAPDD----LEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGgLTESRRAADLA 192
|
330 340 350
....*....|....*....|....*....|....*...
gi 882683 329 DDWGLTWGCHSNNHFDISLAMFTHVGAAAPgNPTAIDT 366
Cdd:cd00308 193 EAFGIRVMVHGTLESSIGTAAALHLAAALP-NDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
39-408 |
1.55e-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: 115.49 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 39 IVVLTDNAGHTGIGEA--PGGDVIYQTLVDAI---------PMVLGQEVARLNKVVQQVHKgnqAADFDTFGKGAWTFEL 107
Cdd:cd03318 32 LVRLTTSDGVVGIGEAttPGGPAWGGESPETIkaiidrylaPLLIGRDATNIGAAMALLDR---AVAGNLFAKAAIEMAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 108 rvnavaaleaalLDLLGKALNVPVCELLGpGKQREAITVLgYLFYIGDrTKTDLpyventpgnhewyqlrhqkamnSEAV 187
Cdd:cd03318 109 ------------LDAQGRRLGLPVSELLG-GRVRDSLPVA-WTLASGD-TERDI----------------------AEAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 188 VRLAEASQDRygfkdFKLKGGVLPGEQEIDTVRALKKRFPD-ARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAE 265
Cdd:cd03318 152 EMLEAGRHRR-----FKLKMGARPPADDLAHVEAIAKALGDrASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVPRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 266 QgfsgREVMAEFRRATGLPVATNMIATNWREMGHAVMLNAVDI-PLADPHFWTLSGAVRVAQLCDDWGLtwGCHSNNHFD 344
Cdd:cd03318 227 N----LDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVfSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTMLE 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882683 345 --ISLAMFTHVGAAAPGNP--TAIDTHWIWQEgdcRLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03318 301 ssIGTAASAHLFATLPSLPfgCELFGPLLLAE---DLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
185-283 |
2.80e-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: 79.63 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 185 EAVVRLAEASQDRYGFKDFKLKGGVlPGEQEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPC 262
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEPV 80
|
90 100
....*....|....*....|.
gi 882683 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 |
7.68e-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: 80.08 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGPgkQREAITVlGYLFYIGDRtktdlpyventpgnhewyqlrhqkamnsEAVVRLAEASqDRYGFKDF 203
Cdd:cd03315 57 GKRLGVPVYLLLGG--YRDRVRV-AHMLGLGEP----------------------------AEVAEEARRA-LEAGFRTF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLKGGVLPgEQEIDTVRALKKRFP-DARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRAT 281
Cdd:cd03315 105 KLKVGRDP-ARDVAVVAALREAVGdDAELRVDANRGWTPKQAIRALRALEDLgLDYVEQPLPADD----LEGRAALARAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 282 GLPVATNMIATNWREMGHAVMLNAVD---IPLADPHFwtLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTHVGAAAP 358
Cdd:cd03315 180 DTPIMADESAFTPHDAFRELALGAADavnIKTAKTGG--LTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALR 257
|
....*
gi 882683 359 GNPTA 363
Cdd:cd03315 258 AVTLP 262
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
124-402 |
7.53e-13 |
|
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: 69.28 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGpGKQREAITVLGYLFyiGDRTKTdlpyventpgnhewyqlrhqkamnseaVVRLAEASQDRyGFKDF 203
Cdd:cd03325 94 GKVLGVPVHQLLG-GQVRDRVRVYSWIG--GDRPSD---------------------------VAEAARARREA-GFTAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLkggVLPGEQE-----------IDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:cd03325 143 KM---NATEELQwidtskkvdaaVERVAALREAVgPDIDIGVDFHGRVSKPMAKDLAKELEPYrLLFIEEPVLPEN---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLAD-PHFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:cd03325 216 VEALAEIAARTTIPIATgERLFSRW-DFKELLEDGAVDIIQPDiSHAGGITELKKIAAMAEAYDVALAPH-CPLGPIALA 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882683 349 MFTHVGAAAP--------GNPTAIDTHWIWQEGdcrLTQNPLEIKNGKIAVPDAPGLGVELD 402
Cdd:cd03325 294 ASLHVDASTPnfliqeqsLGIHYNEGDDLLDYL---VDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
182-286 |
1.50e-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: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 182 MNSEAVVRLAEAsQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFP-DARITVDPNGAWLLDEAISLCKGLNDV-LTYAE 259
Cdd:cd03320 81 AGDAAALGEAKA-AYGGGYRTVKLKVGATSFEEDLARLRALREALPaDAKLRLDANGGWSLEEALAFLEALAAGrIEYIE 159
|
90 100
....*....|....*....|....*..
gi 882683 260 DPCGAEQgfsgreVMAEFRRATGLPVA 286
Cdd:cd03320 160 QPLPPDD------LAELRRLAAGVPIA 180
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
39-408 |
3.60e-12 |
|
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: 67.26 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 39 IVVLTDNAGHTGIGEA---PGGDVIYQTLVDA--------IPMVLGQEVARLNKVVQQVH--KGNQAAdfdtfgKGAwtF 105
Cdd:cd03317 28 IVELTDEEGITGYGEVvafEGPFYTEETNATAwhilkdylLPLLLGREFSHPEEVSERLApiKGNNMA------KAG--L 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 106 ELRVnavaaleaalLDLLGKALNVPVCELLGPGKQR-EAITVLGylfyigdrtktDLPYVENTPgnhewyqlrhqkamns 184
Cdd:cd03317 100 EMAV----------WDLYAKAQGQSLAQYLGGTRDSiPVGVSIG-----------IQDDVEQLL---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 185 EAVVRLAEasqdrYGFKDFKLKggVLPGeQEIDTVRALKKRFPDARITVDPNGAWLLDEaISLCKGLNDV-LTYAEDPCG 263
Cdd:cd03317 143 KQIERYLE-----EGYKRIKLK--IKPG-WDVEPLKAVRERFPDIPLMADANSAYTLAD-IPLLKRLDEYgLLMIEQPLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 264 AEQGFSGREVMAEFRRA-------TGLPVATNMIatnwrEMGHAVMLNavdipLADPHFWTLSGAVRVAQLCDDWGLTWG 336
Cdd:cd03317 214 ADDLIDHAELQKLLKTPicldesiQSAEDARKAI-----ELGACKIIN-----IKPGRVGGLTEALKIHDLCQEHGIPVW 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882683 337 CHS------NNHFDISLAmfTHVGAAAPGNPTAIDTHWiwqEGDcrLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03317 284 CGGmlesgiGRAHNVALA--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 |
5.64e-12 |
|
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: 66.44 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 36 TRNIVVLTDNAGHTGIGEAPGGDVIY--------QTLVDAIPMVLGQEVaRLNKVVQQVHK---GNQAAdfdtfgKGA-- 102
Cdd:cd03319 25 AENVIVEIELDGITGYGEAAPTPRVTgetvesvlAALKSVRPALIGGDP-RLEKLLEALQEllpGNGAA------RAAvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 103 ---WtfELRvnavaaleaalldllGKALNVPVCELLGPGKQRE---AITVlgylfyigdrtktdlpyVENTPgnhewyql 176
Cdd:cd03319 98 ialW--DLE---------------AKLLGLPLYQLWGGGAPRPletDYTI-----------------SIDTP-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 177 rhqkamnsEAVVRLAEASQDRyGFKDFKLKGGvLPGEQEIDTVRALKKRFPDARITVDPNGAWLLDEAISLCKGLND-VL 255
Cdd:cd03319 136 --------EAMAAAAKKAAKR-GFPLLKIKLG-GDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAElGV 205
|
250 260 270
....*....|....*....|....*....|.
gi 882683 256 TYAEDPCGAEQgfsgREVMAEFRRATGLPVA 286
Cdd:cd03319 206 ELIEQPVPAGD----DDGLAYLRDKSPLPIM 232
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
199-408 |
5.86e-10 |
|
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: 60.57 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 199 GFKDFKLKGGVLPGEQEIDTVRALKKRFPDA-RITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsgREVMAE 276
Cdd:cd03321 156 GFHAVKTKIGYPTADEDLAVVRSIRQAVGDGvGLMVDYNQSLTVPEAIERGQALDQEgLTWIEEPTLQHD----YEGHAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 277 FRRATGLPVatnMIATNW---REMGHAVMLNAVDIPLAD-PHFWTLSGAVRVAQLCDDWGLTWGCHSNNHFDISLAMFTh 352
Cdd:cd03321 232 IASALRTPV---QMGENWlgpEEMFKALSAGACDLVMPDlMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVT- 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 353 vgaaapgnPTAidtHWI----WQEGdcrLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03321 308 --------PTA---HWLeyvdWAGA---ILEPPLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
193-286 |
3.14e-08 |
|
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: 54.81 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 193 ASQDRYGFKDFKLKGGVLPGEQEIDTVRALKKRFPD-ARITVDPNGAWLLDEAISLCKGLN----DVLTYAEDPCgaeqg 267
Cdd:TIGR01927 118 RSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLDANGGLSPDEAQQFLKALDpnlrGRIAFLEEPL----- 192
|
90
....*....|....*....
gi 882683 268 fSGREVMAEFRRATGLPVA 286
Cdd:TIGR01927 193 -PDADEMSAFSEATGTAIA 210
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
41-402 |
4.65e-07 |
|
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: 51.56 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 41 VLTDNaGHTGIGEAPGGDVIYQTLVDAI-PMVLGQEVARLNKVVQQVHKGNQAADfdtfGKGawtfeLRVNAVAALEAAL 119
Cdd:cd03327 16 IETDD-GTVGYANTTGGPVACWIVDQHLaRFLIGKDPSDIEKLWDQMYRATLAYG----RKG-----IAMAAISAVDLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 120 LDLLGKALNVPVCELLGpGKQREAITvlgylFYIGDRTKTDLpyventpgnhewyqlrhqKAMNSEAVVRLAEasqdryG 199
Cdd:cd03327 86 WDLLGKIRGEPVYKLLG-GRTRDKIP-----AYASGLYPTDL------------------DELPDEAKEYLKE------G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 200 FKDFKLKGGVLPGE------QEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgFSGr 271
Cdd:cd03327 136 YRGMKMRFGYGPSDghaglrKNVELVRAIREAVgYDVDLMLDCYMSWNLNYAIKMARALEKYeLRWIEEPLIPDD-IEG- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 272 evMAEFRRATGLPVAT-NMIATNW--REMghaVMLNAVDIPLADPHfWT--LSGAVRVAQLCDDWGLTWGCHSNNHFDIS 346
Cdd:cd03327 214 --YAELKKATGIPISTgEHEYTVYgfKRL---LEGRAVDILQPDVN-WVggITELKKIAALAEAYGVPVVPHASQIYNYH 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 882683 347 LAMFTHVGAAAPGNPTAIDTHWIWQEGDcrLTQNPLEIKNGKIAVPDAPGLGVELD 402
Cdd:cd03327 288 FIMSEPNSPFAEYLPNSPDEVGNPLFYY--IFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
124-408 |
1.30e-06 |
|
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: 50.09 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGPGKQReaitvlgylfyigdrtktdLPYVENTPGNHEWYQLRHqkamnSEAVVRLAEASQDRyGFKDF 203
Cdd:cd03329 108 GKYLGLPVHRLLGGYREK-------------------IPAYASTMVGDDLEGLES-----PEAYADFAEECKAL-GYRAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLKGGVLPG-EQEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCgAEQGFSGREVMAEFRR- 279
Cdd:cd03329 163 KLHPWGPGVvRRDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLGRALEELgFFWYEDPL-REASISSYRWLAEKLDi 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 280 ---ATGLPVATNMIATNWremghaVMLNAVDIPLADPHF-WTLSGAVRVAQLCDDWGLTWGCHSNNhfdislAMFTHVGA 355
Cdd:cd03329 242 pilGTEHSRGALESRADW------VLAGATDFLRADVNLvGGITGAMKTAHLAEAFGLDVELHGNG------AANLHVIA 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882683 356 AAPgnptaiDTHW-----------IWQEGDCRLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQK 408
Cdd:cd03329 310 AIR------NTRYyergllhpsqkYDVYAGYLSVLDDPVDSDGFVHVPKGPGLGVEIDFDYIER 367
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
124-409 |
2.25e-06 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 49.51 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGpGKQREAITVlgYLFYIGDRtktdlpyventpgnhewyqlrhqkamnSEAVVRLAEASQDRyGFKDF 203
Cdd:PRK14017 95 GKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARVER-GFTAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLKGgvlPGE-QEIDTVRALKK---RF--------PDARITVDPNGAWLLDEAISLCKGLNDV-LTYAEDPCGAEQgfsg 270
Cdd:PRK14017 144 KMNG---TEElQYIDSPRKVDAavaRVaavreavgPEIGIGVDFHGRVHKPMAKVLAKELEPYrPMFIEEPVLPEN---- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 271 REVMAEFRRATGLPVAT-NMIATNWrEMGHAVMLNAVDIPLADP-HFWTLSGAVRVAQLCDDWGLTWGCHsNNHFDISLA 348
Cdd:PRK14017 217 AEALPEIAAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLGPIALA 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 882683 349 MFTHVGAAAPgNPT----AIDTHwiWQEG----DCRLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQKA 409
Cdd:PRK14017 295 ACLQVDAVSP-NAFiqeqSLGIH--YNQGadllDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRER 360
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
124-423 |
2.56e-06 |
|
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: 49.36 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 124 GKALNVPVCELLGpGKQREAITVLGYlfyigdRTKTDLPYVENTPGNHEWYQLRHQKAMnseaVVRLAEASQDRYGFkDF 203
Cdd:cd03322 97 GKAAGMPLYQLLG-GKSRDGIMVYSH------ASGRDIPELLEAVERHLAQGYRAIRVQ----LPKLFEAVREKFGF-EF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 204 KLkggvlpgeqeidtvralkkrFPDARITVDPNgawlldEAISLCKGLNDV-LTYAEDPCGAEQgfsgREVMAEFRRATG 282
Cdd:cd03322 165 HL--------------------LHDVHHRLTPN------QAARFGKDVEPYrLFWMEDPTPAEN----QEAFRLIRQHTA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882683 283 LPVATNMIATNWREMGHAVMLNAVD-IPLADPHFWTLSGAVRVAQLCDDWGLTWGCH-----------SNNHFDISLAMF 350
Cdd:cd03322 215 TPLAVGEVFNSIWDWQNLIQERLIDyIRTTVSHAGGITPARKIADLASLYGVRTGWHgptdlspvgmaAALHLDLWVPNF 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882683 351 thvgaaapgnptAIDTHWIWQEGDCRLTQNPLEIKNGKIAVPDAPGLGVELDWEQVQKAHEAYKRLPGGARND 423
Cdd:cd03322 295 ------------GIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPVARLED 355
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
214-286 |
1.39e-05 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 1.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 882683 214 QEIDTVRALKKRF-PDARITVDPNGAWLLDEAISLCKGLN--DVLTYAEDPCgaeqgfSGREVMAEFRRATGLPVA 286
Cdd:PRK02901 119 DDVARVNAVRDALgPDGRVRVDANGGWSVDEAVAAARALDadGPLEYVEQPC------ATVEELAELRRRVGVPIA 188
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
199-244 |
2.31e-03 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 40.00 E-value: 2.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 882683 199 GFKDFKLKGGVLPGEQEIDTVRALKKRFP-DARITVDPNGAWLLDEA 244
Cdd:PRK02714 133 GYRTFKWKIGVDPLEQELKIFEQLLERLPaGAKLRLDANGGLSLEEA 179
|
|
| |
