|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
3-444 |
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: 907.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 3 TSTPIVKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIPGGEKILATLNDAKALVEGQPIGEYKNLL 82
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 83 KKIQQTFADRDSGGRGNQTFDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGEGQQRSEVEVLGYLFFIGDRKQTSLDY 162
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 163 ATTPQHNHDWYKVRHEKALTPEAVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDE 242
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 243 AIALGKHLKGVLAYAEDPCGAEQGYSSREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWTLEGSVR 322
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 323 VSQLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGKVTAIDTHWIWQEGtDQLTKAPLEIKDGKIQVPTAPGLGVELDW 402
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 496858145 403 DRINQAHELYKLKGLGARNDADAMQFLIPNWSFNNKKPCLVR 444
Cdd:TIGR03247 400 DAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
7-413 |
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: 646.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 7 IVKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIPGGEKIL-ATLNDAKALVEGQPIGEYKNLLKKI 85
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGAEALeALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 86 QQTFADRDSGGRGNQTFDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGEGQqRSEVEVLGYLFFIGDRKQTSLDYAtt 165
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 166 pqhnhdWYKVRHEKALTPEAVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDEAIA 245
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 246 LGKHLKGVLAYAEDPCGAeqgyssREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWT-LEGSVRVS 324
Cdd:cd03323 232 LAKELEGVLAYLEDPCGG------REGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 325 QLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGKVTAIDTHWIWQEGtDQLTKAPLEIKDGKIQVPTAPGLGVELDWDR 404
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
....*....
gi 496858145 405 INQAHELYK 413
Cdd:cd03323 385 LAKAHELYQ 393
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
8-408 |
7.57e-79 |
|
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: 248.58 E-value: 7.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 8 VKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIP----GGEKILATLNDA-KALVEGQPIGEYKNLL 82
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEAlAPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 83 KKIQQtfadrdsggrgnqtfDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgylffigdrkqtsldY 162
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPV----------------Y 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 163 ATTPqhnhdwykvrhekALTPEAVQRLAEASYDRyGFKDFKLKGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLD 241
Cdd:COG4948 131 ATLG-------------IDTPEEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 242 EAIALGKHLKGV-LAYAEDPCGAEQGyssrEIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFW-TLEG 319
Cdd:COG4948 197 EAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 320 SVRVSQLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGkVTAIDTHWIWQEgTDQLTKAPLEIKDGKIQVPTAPGLGVE 399
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDGPLLL-ADDLVEDPLRIEDGYLTVPDGPGLGVE 350
|
....*....
gi 496858145 400 LDWDRINQA 408
Cdd:COG4948 351 LDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
185-404 |
1.97e-51 |
|
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: 172.75 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 185 AVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDPCG 262
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 263 AEQgyssREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWT-LEGSVRVSQLCNMYNLTWGSHSNNH 341
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496858145 342 FdISLAMFTHVAAAAVGKVTAIDTHWIWQEgTDQLTKAPLEIKDGKIQVPTAPGLGVELDWDR 404
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLL-EDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
183-282 |
2.99e-16 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 73.85 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 183 PEAVQRLAEASYDRYGFKDFKLKGGVLqGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDP 260
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGGG-PLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEP 79
|
90 100
....*....|....*....|..
gi 496858145 261 CGAEQGyssrEIMAEFKRATGL 282
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
115-405 |
5.57e-07 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 51.44 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 115 ESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgYLFFIGDRkqtsldyattpqhnhdwykvrhekaltPEAVQRLAEASY 194
Cdd:PRK14017 87 DQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 195 DRyGFKDFKLKG-GVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLD--------EAIALGKHLKGV-LAYAEDPCGAE 264
Cdd:PRK14017 137 ER-GFTAVKMNGtEELQYIDSPRKVDAAVARVAAVREAVGPEIGIGVDfhgrvhkpMAKVLAKELEPYrPMFIEEPVLPE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 265 QGYSSREImaefKRATGLPTAT-NMIATDWrEMSHSIQLQAVDIPLADP-HFWTLEGSVRVSQLCNMYNLTWGSHsNNHF 342
Cdd:PRK14017 216 NAEALPEI----AAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLG 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 343 DISLAMFTHVAAA---AVGKVTAIDTHWiwQEGTDQL----TKAPLEIKDGKIQVPTAPGLGVELDWDRI 405
Cdd:PRK14017 290 PIALAACLQVDAVspnAFIQEQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGIEIDEAKV 357
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glucar-dehydr |
TIGR03247 |
glucarate dehydratase; Glucarate dehydratase converts D-glucarate (and L-idarate, a ... |
3-444 |
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: 907.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 3 TSTPIVKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIPGGEKILATLNDAKALVEGQPIGEYKNLL 82
Cdd:TIGR03247 1 ATTPVVTEMRVIPVAGHDSMLLNLSGAHAPFFTRNIVILTDSSGNTGVGEVPGGEKIRATLEDARPLVVGKPLGEYQNVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 83 KKIQQTFADRDSGGRGNQTFDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGEGQQRSEVEVLGYLFFIGDRKQTSLDY 162
Cdd:TIGR03247 81 NDVRATFADRDAGGRGLQTFDLRTTIHAVTAIESALLDLLGQHLGVPVAALLGEGQQRDEVEMLGYLFFIGDRKRTSLPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 163 ATTPQHNHDWYKVRHEKALTPEAVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDE 242
Cdd:TIGR03247 161 RSGPQDDDDWFRLRHEEALTPEAVVRLAEAAYDRYGFRDFKLKGGVLRGEEEIEAVTALAKRFPQARITLDPNGAWSLDE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 243 AIALGKHLKGVLAYAEDPCGAEQGYSSREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWTLEGSVR 322
Cdd:TIGR03247 241 AIALCKDLKGVLAYAEDPCGAEQGYSGREVMAEFRRATGLPTATNMIATDWRQMGHALQLQAVDIPLADPHFWTMQGSVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 323 VSQLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGKVTAIDTHWIWQEGtDQLTKAPLEIKDGKIQVPTAPGLGVELDW 402
Cdd:TIGR03247 321 VAQMCHDWGLTWGSHSNNHFDISLAMFTHVAAAAPGKITAIDTHWIWQDG-QRLTKEPLEIKGGKIQVPDKPGLGVEIDM 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 496858145 403 DRINQAHELYKLKGLGARNDADAMQFLIPNWSFNNKKPCLVR 444
Cdd:TIGR03247 400 DAVDAAHELYQKHGLGARDDAIAMQYLIPGWTFDNKRPCLVR 441
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
7-413 |
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: 646.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 7 IVKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIPGGEKIL-ATLNDAKALVEGQPIGEYKNLLKKI 85
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGAEALeALLEAARSLVGGDVFGAYLAVLESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 86 QQTFADRDSGGRGNQTFDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGEGQqRSEVEVLGYLFFIGDRKQTSLDYAtt 165
Cdd:cd03323 81 RVAFADRDAGGRGLQTFDLRTTVHVVTAFEVALLDLLGQALGVPVADLLGGGQ-RDSVPFLAYLFYKGDRHKTDLPYP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 166 pqhnhdWYKVRHEKALTPEAVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDEAIA 245
Cdd:cd03323 158 ------WFRDRWGEALTPEGVVRLARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 246 LGKHLKGVLAYAEDPCGAeqgyssREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWT-LEGSVRVS 324
Cdd:cd03323 232 LAKELEGVLAYLEDPCGG------REGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGgMRGSVRVA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 325 QLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGKVTAIDTHWIWQEGtDQLTKAPLEIKDGKIQVPTAPGLGVELDWDR 404
Cdd:cd03323 306 QVCETWGLGWGMHSNNHLGISLAMMTHVAAAAPGLITACDTHWIWQDG-QVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
....*....
gi 496858145 405 INQAHELYK 413
Cdd:cd03323 385 LAKAHELYQ 393
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
8-408 |
7.57e-79 |
|
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: 248.58 E-value: 7.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 8 VKSIRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEIP----GGEKILATLNDA-KALVEGQPIGEYKNLL 82
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVpggtGAEAVAAALEEAlAPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 83 KKIQQtfadrdsggrgnqtfDLRTTIHVVTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgylffigdrkqtsldY 162
Cdd:COG4948 83 QRLYR---------------ALPGNPAAKAAVDMALWDLLGKALGVPVYQLLG-GKVRDRVPV----------------Y 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 163 ATTPqhnhdwykvrhekALTPEAVQRLAEASYDRyGFKDFKLKGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLD 241
Cdd:COG4948 131 ATLG-------------IDTPEEMAEEAREAVAR-GFRALKLKVGGPDPEEDVERVRAVREAVgPDARLRVDANGAWTLE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 242 EAIALGKHLKGV-LAYAEDPCGAEQGyssrEIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFW-TLEG 319
Cdd:COG4948 197 EAIRLLRALEDLgLEWIEQPLPAEDL----EGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 320 SVRVSQLCNMYNLTWGSHSNNHFDISLAMFTHVAAAAVGkVTAIDTHWIWQEgTDQLTKAPLEIKDGKIQVPTAPGLGVE 399
Cdd:COG4948 273 ALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPN-FDIVELDGPLLL-ADDLVEDPLRIEDGYLTVPDGPGLGVE 350
|
....*....
gi 496858145 400 LDWDRINQA 408
Cdd:COG4948 351 LDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
185-404 |
1.97e-51 |
|
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: 172.75 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 185 AVQRLAEASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDPCG 262
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 263 AEQgyssREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWT-LEGSVRVSQLCNMYNLTWGSHSNNH 341
Cdd:pfam13378 81 PDD----LEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGgITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496858145 342 FdISLAMFTHVAAAAVGKVTAIDTHWIWQEgTDQLTKAPLEIKDGKIQVPTAPGLGVELDWDR 404
Cdd:pfam13378 157 P-IGLAASLHLAAAVPNLLIQEYFLDPLLL-EDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
8-399 |
9.09e-49 |
|
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: 170.10 E-value: 9.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 8 VKSIRAIPVAGHDSMllnlsgAHGPYFTRNILI--IEDNSGNIGVGEIPGGEKILATLN----DAKALVEGQPIGEYKNL 81
Cdd:cd03316 2 ITDVETFVLRVPLPE------PGGAVTWRNLVLvrVTTDDGITGWGEAYPGGRPSAVAAaiedLLAPLLIGRDPLDIERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 82 LKKIQQTFADRDSGGrgnqtfdlrTTIHVVTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgylffigdrkqtsld 161
Cdd:cd03316 76 WEKLYRRLFWRGRGG---------VAMAAISAVDIALWDIKGKAAGVPVYKLLG-GKVRDRVRV---------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 162 YATTPQHNHDwykvrhekaltPEAVQRLAEASYDRyGFKDFKLKGGVLQGEQE-----AEAVTAIARRF-PEARVTLDPN 235
Cdd:cd03316 130 YASGGGYDDS-----------PEELAEEAKRAVAE-GFTAVKLKVGGPDSGGEdlredLARVRAVREAVgPDVDLMVDAN 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 236 GAWFLDEAIALGKHL-KGVLAYAEDPCGAEQgyssREIMAEFKRATGLPTAT-NMIAT--DWREMshsIQLQAVDIPLAD 311
Cdd:cd03316 198 GRWDLAEAIRLARALeEYDLFWFEEPVPPDD----LEGLARLRQATSVPIAAgENLYTrwEFRDL---LEAGAVDIIQPD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 312 PHFWT-LEGSVRVSQLCNMYNLTWGSHSNNHfDISLAMFTHVAAAaVGKVTAIDTHWIWQEGTDQLTKAPLEIKDGKIQV 390
Cdd:cd03316 271 VTKVGgITEAKKIAALAEAHGVRVAPHGAGG-PIGLAASLHLAAA-LPNFGILEYHLDDLPLREDLFKNPPEIEDGYVTV 348
|
....*....
gi 496858145 391 PTAPGLGVE 399
Cdd:cd03316 349 PDRPGLGVE 357
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
11-365 |
1.77e-42 |
|
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: 149.79 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 11 IRAIPVAGHDSMLLNLSGAHGPYFTRNILIIEDNSGNIGVGEipggekilatlndakalvegqpigeyknllkkiqqtfa 90
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 91 drdsggrgnqtfdlrttihVVTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVLGYLffigdrkqtsldyattpqhnh 170
Cdd:cd00308 43 -------------------VISGIDMALWDLAAKALGVPLAELLG-GGSRDRVPAYGSI--------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 171 dwykvrhekaltpeavqrlaeasydrygfkdfklkggvlqgeqeaEAVTAIARRFP-EARVTLDPNGAWFLDEAIALGKH 249
Cdd:cd00308 82 ---------------------------------------------ERVRAVREAFGpDARLAVDANGAWTPKEAIRLIRA 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 250 L-KGVLAYAEDPCGAEQgyssREIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDIPLADPHFWT-LEGSVRVSQLC 327
Cdd:cd00308 117 LeKYGLAWIEEPCAPDD----LEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGgLTESRRAADLA 192
|
330 340 350
....*....|....*....|....*....|....*...
gi 496858145 328 NMYNLTWGSHSNNHFDISLAMFTHVaAAAVGKVTAIDT 365
Cdd:cd00308 193 EAFGIRVMVHGTLESSIGTAAALHL-AAALPNDRAIET 229
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
113-405 |
3.47e-21 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 94.31 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 113 AYESALLDLLGKHLNVNVASLLGeGQQRSEVEVLgylffigdrkqTSLDYATTPqhnhdwykvrhekALTPEAVQRLAEA 192
Cdd:cd03318 103 AIEMALLDAQGRRLGLPVSELLG-GRVRDSLPVA-----------WTLASGDTE-------------RDIAEAEEMLEAG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 193 SYDRygfkdFKLKGGVLQGEQEAEAVTAIARRFP-EARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDPCGAEQgyssR 270
Cdd:cd03318 158 RHRR-----FKLKMGARPPADDLAHVEAIAKALGdRASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVPREN----L 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 271 EIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVDI-PLADPHFWTLEGSVRVSQLCNMYNLtwGSHSNNHFD--ISLA 347
Cdd:cd03318 229 DGLARLRSRNRVPIMADESVSGPADAFELARRGAADVfSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTMLEssIGTA 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496858145 348 MFTHVaAAAVGKVT----AIDTHWIwqegTDQLTKAPLEIKDGKIQVPTAPGLGVELDWDRI 405
Cdd:cd03318 307 ASAHL-FATLPSLPfgceLFGPLLL----AEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
183-282 |
2.99e-16 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 73.85 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 183 PEAVQRLAEASYDRYGFKDFKLKGGVLqGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDP 260
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGGG-PLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRALEALDELgLEWIEEP 79
|
90 100
....*....|....*....|..
gi 496858145 261 CGAEQGyssrEIMAEFKRATGL 282
Cdd:smart00922 80 VPPDDL----EGLAELRRATPI 97
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
113-407 |
6.00e-14 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 72.90 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 113 AYESALLDLLGKHLNVNVASLLGeGQQRSEVEVLGYLFfIGDrkqTSLDYAttpqhnhdwykvrhekaltpEAVQRLAEa 192
Cdd:TIGR02534 102 AVDTALHDAQARRLGVPVSELLG-GRVRDSVDVTWTLA-SGD---TDRDIA--------------------EAEERIEE- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 193 sydrYGFKDFKLKGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLK-GVLAYAEDPCGAEQgyssR 270
Cdd:TIGR02534 156 ----KRHRSFKLKIGARDPADDVAHVVAIAKALgDRASVRVDVNAAWDERTALHYLPQLAdAGVELIEQPTPAEN----R 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 271 EIMAEFKRATGLPTATNMIATDWREMSHSIQLQAVD-IPLADPHFWTLEGSVRVSQLCNMYNLTWGSHSNNHFDISLAMF 349
Cdd:TIGR02534 228 EALARLTRRFNVPIMADESVTGPADALAIAKASAADvFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIAS 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 496858145 350 THvAAAAVGKVTAIDTHWIWQEGTDQLTKAPLEIKDGKIQVPTAPGLGVELDWDRINQ 407
Cdd:TIGR02534 308 AH-FFATFPALSFGTELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNF 364
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
113-333 |
5.09e-12 |
|
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: 65.83 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 113 AYESALLDLLGKHLNVNVASLLgeGQQRSEVEVlGYLFFIGDrkqtsldyattpqhnhdwykvrhekaltPEAVQRLAEA 192
Cdd:cd03315 47 AVDMALWDLWGKRLGVPVYLLL--GGYRDRVRV-AHMLGLGE----------------------------PAEVAEEARR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 193 sYDRYGFKDFKLKGGvLQGEQEAEAVTAIARRFP-EARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDPCGAEQgyssR 270
Cdd:cd03315 96 -ALEAGFRTFKLKVG-RDPARDVAVVAALREAVGdDAELRVDANRGWTPKQAIRALRALEDLgLDYVEQPLPADD----L 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496858145 271 EIMAEFKRATGLPTATN---MIATDWREMSHSIQLQAVDIPLADPHFwtLEGSVRVSQLCNMYNLT 333
Cdd:cd03315 170 EGRAALARATDTPIMADesaFTPHDAFRELALGAADAVNIKTAKTGG--LTKAQRVLAVAEALGLP 233
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
183-285 |
2.58e-11 |
|
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: 63.82 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 183 PEAVQRLAEASYDRyGFKDFKLKGGVLQGEQEAEAVTAIARRFPE-ARVTLDPNGAWFLDEAIALGKHL-KGVLAYAEDP 260
Cdd:cd03320 83 DAAALGEAKAAYGG-GYRTVKLKVGATSFEEDLARLRALREALPAdAKLRLDANGGWSLEEALAFLEALaAGRIEYIEQP 161
|
90 100
....*....|....*....|....*
gi 496858145 261 CgaeqgySSREIMAEFKRATGLPTA 285
Cdd:cd03320 162 L------PPDDLAELRRLAAGVPIA 180
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
111-401 |
3.93e-10 |
|
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: 61.19 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 111 VTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgYLFFIGDRkqtsldyattpqhnhdwykvrhekaltPEAVQRLA 190
Cdd:cd03325 82 ISGIDQALWDIKGKVLGVPVHQLLG-GQVRDRVRV--YSWIGGDR---------------------------PSDVAEAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 191 EASYDRyGFKDFKLKG-GVLQGEQEAEAVTAIARRF--------PEARVTLDPNGAWFLDEAIALGKHLKGV-LAYAEDP 260
Cdd:cd03325 132 RARREA-GFTAVKMNAtEELQWIDTSKKVDAAVERVaalreavgPDIDIGVDFHGRVSKPMAKDLAKELEPYrLLFIEEP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 261 CGAEQgyssREIMAEFKRATGLPTATN--MIATdwREMSHSIQLQAVDIPLAD-PHFWTLEGSVRVSQLCNMYNLTWGSH 337
Cdd:cd03325 211 VLPEN----VEALAEIAARTTIPIATGerLFSR--WDFKELLEDGAVDIIQPDiSHAGGITELKKIAAMAEAYDVALAPH 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496858145 338 sNNHFDISLAMFTHVAAAA--------VGKVTAIDTHWIWQEGTDqltKAPLEIKDGKIQVPTAPGLGVELD 401
Cdd:cd03325 285 -CPLGPIALAASLHVDASTpnfliqeqSLGIHYNEGDDLLDYLVD---PEVFDMENGYVKLPTGPGLGIEID 352
|
|
| 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 ... |
35-283 |
1.63e-09 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 58.74 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 35 TRNILI-IEDnSGNIGVGEIPG-----GE---KILATLNDAKALVEGQPIgEYKNLLKKIQqTFADRDSGGRgnqtfdlr 105
Cdd:cd03319 25 AENVIVeIEL-DGITGYGEAAPtprvtGEtveSVLAALKSVRPALIGGDP-RLEKLLEALQ-ELLPGNGAAR-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 106 ttihvvTAYESALLDLLGKHLNVNVASLLGEGQQRSEVevlgylffigdrkqT----SLDyattpqhnhdwykvrhekal 181
Cdd:cd03319 94 ------AAVDIALWDLEAKLLGLPLYQLWGGGAPRPLE--------------TdytiSID-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 182 TPEAVQRLAEAsYDRYGFKDFKLKGGvLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDEAIALGKHL--KGVlAYAED 259
Cdd:cd03319 134 TPEAMAAAAKK-AAKRGFPLLKIKLG-GDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELaeLGV-ELIEQ 210
|
250 260
....*....|....*....|....
gi 496858145 260 PCGAEQgyssREIMAEFKRATGLP 283
Cdd:cd03319 211 PVPAGD----DDGLAYLRDKSPLP 230
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
29-406 |
3.33e-09 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 58.40 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 29 AHGPYFTRNILIIE--DNSGNIGVGEIPGGEK---ILATLNDAKALVEGQPIGEYKNLLKKIQQTFADRDSGGRGNQTfd 103
Cdd:cd03317 17 SFGTLNEREFLIVEltDEEGITGYGEVVAFEGpfyTEETNATAWHILKDYLLPLLLGREFSHPEEVSERLAPIKGNNM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 104 lrttihVVTAYESALLDLLGKHLNVNVASLLGegQQRSEVEV---LGylffIGDRKQTsldyattpqhnhdwykvrheka 180
Cdd:cd03317 95 ------AKAGLEMAVWDLYAKAQGQSLAQYLG--GTRDSIPVgvsIG----IQDDVEQ---------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 181 lTPEAVQRLAEASYDRygfkdFKLKggvLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLDEAialgKHLKGV----LAY 256
Cdd:cd03317 141 -LLKQIERYLEEGYKR-----IKLK---IKPGWDVEPLKAVRERFPDIPLMADANSAYTLADI----PLLKRLdeygLLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 257 AEDPCGAEQGYSSREIMAEFK----------------RATGLPTAT--NM-IAtdwREMSHSIQLQAVDI-PLADPHFWT 316
Cdd:cd03317 208 IEQPLAADDLIDHAELQKLLKtpicldesiqsaedarKAIELGACKiiNIkPG---RVGGLTEALKIHDLcQEHGIPVWC 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 317 leGSVRVSQLCNMYNLTWGSHSNNHF--DISlamfthvaaaavgkvtAIDTHWIwqegtDQLTKAPLEIKDGKIQVPTAP 394
Cdd:cd03317 285 --GGMLESGIGRAHNVALASLPNFTYpgDIS----------------ASSRYFE-----EDIITPPFELENGIISVPTGP 341
|
410
....*....|..
gi 496858145 395 GLGVELDWDRIN 406
Cdd:cd03317 342 GIGVTVDREALK 353
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
111-406 |
4.51e-09 |
|
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: 57.79 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 111 VTAYESALLDLLGKHLNVNVASLLGEGQQRsevevlgylffigdrkqtSLDYATTPQHNHDwykvrhEKALTPEAVQRLA 190
Cdd:cd03329 96 LGLVDIALWDLAGKYLGLPVHRLLGGYREK------------------IPAYASTMVGDDL------EGLESPEAYADFA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 191 EASYDRyGFKDFKLKG---GVLqgEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHLK--GVLAYaEDPCGAE 264
Cdd:cd03329 152 EECKAL-GYRAIKLHPwgpGVV--RRDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLGRALEelGFFWY-EDPLREA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 265 QGYSSREIMAEFK---RATGLPTATNMIATDWremshsIQLQAVDIPLADPHF-WTLEGSVRVSQLCNMYNLTWGSHSNN 340
Cdd:cd03329 228 SISSYRWLAEKLDipiLGTEHSRGALESRADW------VLAGATDFLRADVNLvGGITGAMKTAHLAEAFGLDVELHGNG 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496858145 341 hfdislAMFTHVAAA-------AVGkVTAIDTHWIWQEGTDQLTKAPLEiKDGKIQVPTAPGLGVELDWDRIN 406
Cdd:cd03329 302 ------AANLHVIAAirntryyERG-LLHPSQKYDVYAGYLSVLDDPVD-SDGFVHVPKGPGLGVEIDFDYIE 366
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
192-285 |
9.89e-09 |
|
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: 56.35 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 192 ASYDRYGFKDFKLKGGVLQGEQEAEAVTAIARRFPE-ARVTLDPNGAWFLDEAIALGKHL----KGVLAYAEDPCgaeqg 266
Cdd:TIGR01927 118 RSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDkAELRLDANGGLSPDEAQQFLKALdpnlRGRIAFLEEPL----- 192
|
90
....*....|....*....
gi 496858145 267 ySSREIMAEFKRATGLPTA 285
Cdd:TIGR01927 193 -PDADEMSAFSEATGTAIA 210
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
41-401 |
2.88e-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: 52.34 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 41 IEDNSGNIGVGEIPGGEKI-LATLNDAKALVEGQPIGEYKNLLKkiQQTFADRDSGGRGnqtfdlrTTIHVVTAYESALL 119
Cdd:cd03327 16 IETDDGTVGYANTTGGPVAcWIVDQHLARFLIGKDPSDIEKLWD--QMYRATLAYGRKG-------IAMAAISAVDLALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 120 DLLGKHLNVNVASLLGeGQQRSEVEVlgylffigdrkqtsldYATtpqhnhdwykvrheKALTPEAVQRLAEA-SYDRYG 198
Cdd:cd03327 87 DLLGKIRGEPVYKLLG-GRTRDKIPA----------------YAS--------------GLYPTDLDELPDEAkEYLKEG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 199 FKDFKL------KGGVLQGEQEAEAVTAIARRF-PEARVTLDPNGAWFLDEAIALGKHL-KGVLAYAEDPCGAEQ--GYs 268
Cdd:cd03327 136 YRGMKMrfgygpSDGHAGLRKNVELVRAIREAVgYDVDLMLDCYMSWNLNYAIKMARALeKYELRWIEEPLIPDDieGY- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 269 sreimAEFKRATGLPTAT-NMIATDW--REMshsIQLQAVDIPLADPHfWT--LEGSVRVSQLCNMYNLTWGSHSNNHFD 343
Cdd:cd03327 215 -----AELKKATGIPISTgEHEYTVYgfKRL---LEGRAVDILQPDVN-WVggITELKKIAALAEAYGVPVVPHASQIYN 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496858145 344 ISLAMFTHVAAAAVGKVTAIDthWIWQEGTDQLTKAPLEIKDGKIQVPTAPGLGVELD 401
Cdd:cd03327 286 YHFIMSEPNSPFAEYLPNSPD--EVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
115-405 |
5.57e-07 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 51.44 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 115 ESALLDLLGKHLNVNVASLLGeGQQRSEVEVlgYLFFIGDRkqtsldyattpqhnhdwykvrhekaltPEAVQRLAEASY 194
Cdd:PRK14017 87 DQALWDIKGKALGVPVHELLG-GLVRDRIRV--YSWIGGDR---------------------------PADVAEAARARV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 195 DRyGFKDFKLKG-GVLQGEQEAEAVTAIARRFPEARVTLDPNGAWFLD--------EAIALGKHLKGV-LAYAEDPCGAE 264
Cdd:PRK14017 137 ER-GFTAVKMNGtEELQYIDSPRKVDAAVARVAAVREAVGPEIGIGVDfhgrvhkpMAKVLAKELEPYrPMFIEEPVLPE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 265 QGYSSREImaefKRATGLPTAT-NMIATDWrEMSHSIQLQAVDIPLADP-HFWTLEGSVRVSQLCNMYNLTWGSHsNNHF 342
Cdd:PRK14017 216 NAEALPEI----AAQTSIPIATgERLFSRW-DFKRVLEAGGVDIIQPDLsHAGGITECRKIAAMAEAYDVALAPH-CPLG 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 343 DISLAMFTHVAAA---AVGKVTAIDTHWiwQEGTDQL----TKAPLEIKDGKIQVPTAPGLGVELDWDRI 405
Cdd:PRK14017 290 PIALAACLQVDAVspnAFIQEQSLGIHY--NQGADLLdyvkNKEVFAYEDGFVAIPTGPGLGIEIDEAKV 357
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
180-285 |
1.10e-05 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 180 ALTPEAVQRLAEASYdryGFKDFKLK----GGVLqgEQEAEAVTAI-ARRFPEARVTLDPNGAWFLDEAIALGKHLK--G 252
Cdd:PRK02901 87 AVDAAQVPEVLARFP---GCRTAKVKvaepGQTL--ADDVARVNAVrDALGPDGRVRVDANGGWSVDEAVAAARALDadG 161
|
90 100 110
....*....|....*....|....*....|...
gi 496858145 253 VLAYAEDPCgaeqgySSREIMAEFKRATGLPTA 285
Cdd:PRK02901 162 PLEYVEQPC------ATVEELAELRRRVGVPIA 188
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
107-401 |
4.21e-04 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 42.43 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 107 TIHVVTAYESALLDLLGKHLNVNVASLLGeGQQRSEVEVLGYlffigdrkQTSLDYATTPQHNHDWYKV--RHEKALTPe 184
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLG-GKSRDGIMVYSH--------ASGRDIPELLEAVERHLAQgyRAIRVQLP- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 185 avqRLAEASYDRYGFKDFKLKGGvlqgeqeaeavtaiarrfpEARVTldPNgawfldEAIALGKHLKGV-LAYAEDPCGA 263
Cdd:cd03322 151 ---KLFEAVREKFGFEFHLLHDV-------------------HHRLT--PN------QAARFGKDVEPYrLFWMEDPTPA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 264 EQGYSSREImaefKRATGLPTATNMIATDWREMSHSIQLQAVD-IPLADPHFWTLEGSVRVSQLCNMYNLTWGSH----- 337
Cdd:cd03322 201 ENQEAFRLI----RQHTATPLAVGEVFNSIWDWQNLIQERLIDyIRTTVSHAGGITPARKIADLASLYGVRTGWHgptdl 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 338 ------SNNHFDISLAMFthvaaaavgkvtAIDTHWIWQEGTDQLTKAPLEIKDGKIQVPTAPGLGVELD 401
Cdd:cd03322 277 spvgmaAALHLDLWVPNF------------GIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEID 334
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
179-405 |
1.06e-03 |
|
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: 40.93 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 179 KALTPEAVQRLAEasydryGFKDFKLKGGVLQGEQEAEAVTAIARRFPeARVTL--DPNGAWFLDEAIALGKHLKGV-LA 255
Cdd:cd03321 143 KLATERAVTAAEE------GFHAVKTKIGYPTADEDLAVVRSIRQAVG-DGVGLmvDYNQSLTVPEAIERGQALDQEgLT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496858145 256 YAEDPCGAEqgysSREIMAEFKRATGLPTatnMIATDW---REMSHSIQLQAVDIPLAD-PHFWTLEGSVRVSQLCNMYN 331
Cdd:cd03321 216 WIEEPTLQH----DYEGHARIASALRTPV---QMGENWlgpEEMFKALSAGACDLVMPDlMKIGGVTGWLRASALAEQAG 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496858145 332 LTWGSHSNNHFDISLAMFTHVAaaavgkvtaidtHWI-WQEGTDQLTKAPLEIKDGKIQVPTAPGLGVELDWDRI 405
Cdd:cd03321 289 IPMSSHLFQEISAHLLAVTPTA------------HWLeYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAV 351
|
|
| |
