|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-386 |
0e+00 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. 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: 239442 [Multi-domain] Cd Length: 385 Bit Score: 602.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 2 RIQEVRERSIPLSRY-AGVAAATGGLSTSLVAVLTDIVRDGRRVVGYGHASVGRYAQGGLIRERFAPRLLGAPADSLASD 80
Cdd:cd03326 1 RIVAIREKAIPLSSPiANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLLAAAPDSLLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 81 DGSGIDPLRAWDLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLHRFLARRLGLaEDYPQRVPVYAGGGYPYPHD 160
Cdd:cd03326 81 AGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGR-GQADPRVPVYAAGGYYYPGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 161 DLGRLEEELRRFVDLGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDI 240
Cdd:cd03326 160 DLGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 241 CDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVRRERDVLVFDPVHCYGLPGYLAILDHLCARGWPRAAFRP 320
Cdd:cd03326 240 GDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599236 321 HAGYLFSLHLVAALRLGWAEATPSAFRPFDDFAGALPFSSGLAGLPQSPGIGFERQATLAGLFRKL 386
Cdd:cd03326 320 HGGHLMSLHIAAGLGLGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL 385
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-374 |
1.60e-44 |
|
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: 157.29 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 1 MRIQ--EVRERSIPLSRYAGVAAAT-GGLSTSLVAVLTDivrDGrrVVGYGHASVGRYAQGG---LIRERFAPRLLGAPA 74
Cdd:COG4948 1 MKITdiEVYPVRLPLKRPFTISRGTrTERDVVLVRVETD---DG--ITGWGEAVPGGTGAEAvaaALEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 75 DslasddgsgiDPLRAWDLMMRDEKPGGHgercvAVGALDMALWDAAAKAAGLPLHRFLarrlGLAedYPQRVPVYAGGG 154
Cdd:COG4948 76 L----------DIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLL----GGK--VRDRVPVYATLG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 155 YpyphDDLGRLEEELRRFVDLGYTHAKIKIGAAGLDQDRRRIdRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAPLG 233
Cdd:COG4948 135 I----DTPEEMAEEAREAVARGFRALKLKVGGPDPEEDVERV-RAVReAVGPDARLRVDANGAWTLEEAIRLLRALEDLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 234 LWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILDHLCARGW 313
Cdd:COG4948 210 LEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAV----DIVNIKLSKVGGLTEALRIAALAEAHGV 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599236 314 PraaFRPHA------GYLFSLHLVAALR-LGWAEATPSAFRPFDDFAGALPFSSGLAGLPQSPGIGFE 374
Cdd:COG4948 286 P---VMPHCmlesgiGLAAALHLAAALPnFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVE 350
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
164-374 |
7.18e-30 |
|
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: 114.58 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 164 RLEEELRRFVD-LGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICD 242
Cdd:pfam13378 1 ELAAEARRAVEaRGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 243 PHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILdHLC-ARGWPraaFRPH 321
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAV----DIVQPDVTRVGGITEALKIA-ALAeAFGVP---VAPH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 322 A-----GYLFSLHLVAAL-RLGWAEATPSAFRPFDD-FAGALPFSSGLAGLPQSPGIGFE 374
Cdd:pfam13378 153 SgggpiGLAASLHLAAAVpNLLIQEYFLDPLLLEDDlLTEPLEVEDGRVAVPDGPGLGVE 212
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
165-257 |
3.96e-15 |
|
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: 70.39 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 165 LEEELRRFVDLGYTHAKIKIGAaGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPH 244
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|...
gi 15599236 245 DFPTQAEVADIYP 257
Cdd:smart00922 84 DLEGLAELRRATP 96
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
84-298 |
2.66e-09 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 58.37 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 84 GIDPLRA---WDLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLHRFLArrlGLAEDypqRVPVYA--GGGYPyp 158
Cdd:PRK14017 54 GKDPRRIedhWQVMYRGGFYRGGPILMSAIAGIDQALWDIKGKALGVPVHELLG---GLVRD---RIRVYSwiGGDRP-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 159 hDDLGrleEELRRFVDLGYTHakIKIGAAG----LDqDRRRIDRAL-RV------LGDASRLAVDAMNRYDAEGAVDAAK 227
Cdd:PRK14017 126 -ADVA---EAARARVERGFTA--VKMNGTEelqyID-SPRKVDAAVaRVaavreaVGPEIGIGVDFHGRVHKPMAKVLAK 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599236 228 ALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGL 298
Cdd:PRK14017 199 ELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGV----DIIQPDLSHAGGI 265
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-386 |
0e+00 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. 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: 239442 [Multi-domain] Cd Length: 385 Bit Score: 602.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 2 RIQEVRERSIPLSRY-AGVAAATGGLSTSLVAVLTDIVRDGRRVVGYGHASVGRYAQGGLIRERFAPRLLGAPADSLASD 80
Cdd:cd03326 1 RIVAIREKAIPLSSPiANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLLAAAPDSLLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 81 DGSGIDPLRAWDLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLHRFLARRLGLaEDYPQRVPVYAGGGYPYPHD 160
Cdd:cd03326 81 AGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGR-GQADPRVPVYAAGGYYYPGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 161 DLGRLEEELRRFVDLGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDI 240
Cdd:cd03326 160 DLGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 241 CDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVRRERDVLVFDPVHCYGLPGYLAILDHLCARGWPRAAFRP 320
Cdd:cd03326 240 GDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599236 321 HAGYLFSLHLVAALRLGWAEATPSAFRPFDDFAGALPFSSGLAGLPQSPGIGFERQATLAGLFRKL 386
Cdd:cd03326 320 HGGHLMSLHIAAGLGLGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL 385
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-374 |
7.18e-51 |
|
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: 173.95 E-value: 7.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 2 RIQEVRERSIPLSRYAGVAAATGGLSTsLVAVLTDivrDGrrVVGYGHASVGR--YAQGGLIRERFAPRLLGAPADslas 79
Cdd:cd03316 1 KITDVETFVLRVPLPEPGGAVTWRNLV-LVRVTTD---DG--ITGWGEAYPGGrpSAVAAAIEDLLAPLLIGRDPL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 80 ddgsgiDPLRAWDLMMRDEKPGGHGERCV-AVGALDMALWDAAAKAAGLPLHRFLARRlglaedYPQRVPVYAGGGYPyp 158
Cdd:cd03316 71 ------DIERLWEKLYRRLFWRGRGGVAMaAISAVDIALWDIKGKAAGVPVYKLLGGK------VRDRVRVYASGGGY-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 159 HDDLGRLEEELRRFVDLGYTHAKIKIGA-----AGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLG 233
Cdd:cd03316 137 DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 234 LWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILDHLCARGW 313
Cdd:cd03316 217 LFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAV----DIIQPDVTKVGGITEAKKIAALAEAHGV 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599236 314 PRAafrPHA-----GYLFSLHLVAAL-RLGWAEATPSAFRPFDDFAGALP-FSSGLAGLPQSPGIGFE 374
Cdd:cd03316 293 RVA---PHGaggpiGLAASLHLAAALpNFGILEYHLDDLPLREDLFKNPPeIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-374 |
1.60e-44 |
|
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: 157.29 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 1 MRIQ--EVRERSIPLSRYAGVAAAT-GGLSTSLVAVLTDivrDGrrVVGYGHASVGRYAQGG---LIRERFAPRLLGAPA 74
Cdd:COG4948 1 MKITdiEVYPVRLPLKRPFTISRGTrTERDVVLVRVETD---DG--ITGWGEAVPGGTGAEAvaaALEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 75 DslasddgsgiDPLRAWDLMMRDEKPGGHgercvAVGALDMALWDAAAKAAGLPLHRFLarrlGLAedYPQRVPVYAGGG 154
Cdd:COG4948 76 L----------DIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLL----GGK--VRDRVPVYATLG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 155 YpyphDDLGRLEEELRRFVDLGYTHAKIKIGAAGLDQDRRRIdRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAPLG 233
Cdd:COG4948 135 I----DTPEEMAEEAREAVARGFRALKLKVGGPDPEEDVERV-RAVReAVGPDARLRVDANGAWTLEEAIRLLRALEDLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 234 LWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILDHLCARGW 313
Cdd:COG4948 210 LEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAV----DIVNIKLSKVGGLTEALRIAALAEAHGV 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599236 314 PraaFRPHA------GYLFSLHLVAALR-LGWAEATPSAFRPFDDFAGALPFSSGLAGLPQSPGIGFE 374
Cdd:COG4948 286 P---VMPHCmlesgiGLAAALHLAAALPnFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVE 350
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
164-374 |
7.18e-30 |
|
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: 114.58 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 164 RLEEELRRFVD-LGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICD 242
Cdd:pfam13378 1 ELAAEARRAVEaRGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 243 PHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILdHLC-ARGWPraaFRPH 321
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAV----DIVQPDVTRVGGITEALKIA-ALAeAFGVP---VAPH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 322 A-----GYLFSLHLVAAL-RLGWAEATPSAFRPFDD-FAGALPFSSGLAGLPQSPGIGFE 374
Cdd:pfam13378 153 SgggpiGLAASLHLAAAVpNLLIQEYFLDPLLLEDDlLTEPLEVEDGRVAVPDGPGLGVE 212
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
27-335 |
8.08e-24 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. 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: 239444 [Multi-domain] Cd Length: 352 Bit Score: 100.95 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 27 STSLVAVltDIVRDGRRVVGY--GHASVGRYAQGGLirerfAPRLLGAPAdslasddgsgIDPLRAWDLMMRD-EKPGGH 103
Cdd:cd03328 27 ATTLVLV--EVRAGGRTGLGYtyADAAAAALVDGLL-----APVVEGRDA----------LDPPAAWEAMQRAvRNAGRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 104 GERCVAVGALDMALWDAAAKAAGLPLHRFLARrlglaedYPQRVPVYAGGGYPYPHDDlgRLEEELRRFVDLGYTHAKIK 183
Cdd:cd03328 90 GVAAMAISAVDIALWDLKARLLGLPLARLLGR-------AHDSVPVYGSGGFTSYDDD--RLREQLSGWVAQGIPRVKMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 184 IGAAGlDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVADIYPG--PIG 261
Cdd:cd03328 161 IGRDP-RRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAgmDIA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599236 262 AGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILDHLCARGWPRAAfrpHAGYLFSLHLVAALR 335
Cdd:cd03328 240 AGEYAYTLAYFRRLLEAHAV----DVLQADVTRCGGVTGFLQAAALAAAHHVDLSA---HCAPALHAHVACAVP 306
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
44-333 |
1.70e-19 |
|
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: 88.54 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 44 VVGYGHASVGRYAQGgLIRERFAPRLLGApadslasddgsgiDPLR---AWDLMMRDEKP-GGHGERCVAVGALDMALWD 119
Cdd:cd03327 22 TVGYANTTGGPVACW-IVDQHLARFLIGK-------------DPSDiekLWDQMYRATLAyGRKGIAMAAISAVDLALWD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 120 AAAKAAGLPLHRFLARRLglaedyPQRVPVYAGGGYPyphDDLGRLEEELRRFVDLGYTHAKIKI------GAAGLDQDR 193
Cdd:cd03327 88 LLGKIRGEPVYKLLGGRT------RDKIPAYASGLYP---TDLDELPDEAKEYLKEGYRGMKMRFgygpsdGHAGLRKNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 194 RRIdRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEA 272
Cdd:cd03327 159 ELV-RAIReAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599236 273 R-LLDlyggvRRERDVLVFDPVHCYGLPGYLAILDHLCARGWPRAafrPHAGYLFSLHLVAA 333
Cdd:cd03327 238 KrLLE-----GRAVDILQPDVNWVGGITELKKIAALAEAYGVPVV---PHASQIYNYHFIMS 291
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
111-282 |
4.94e-16 |
|
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: 77.38 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 111 GALDMALWDAAAKAAGLPLHRFLARrlglaedYPQRVPVyaggGYPYPHDDLGRLEEELRRFVDLGYTHAKIKIGAaGLD 190
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGG-------YRDRVRV----AHMLGLGEPAEVAEEARRALEAGFRTFKLKVGR-DPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 191 QDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLA 270
Cdd:cd03315 114 RDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPH 193
|
170
....*....|..
gi 15599236 271 EARLLDLYGGVR 282
Cdd:cd03315 194 DAFRELALGAAD 205
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
102-341 |
9.27e-16 |
|
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: 75.83 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 102 GHGErcvAVGALDMALWDAAAKAAGLPLHRFLarrLGLAEDypqRVPVYAgggypyphddlgrleeelrrfvdlgythak 181
Cdd:cd00308 39 GWGE---VISGIDMALWDLAAKALGVPLAELL---GGGSRD---RVPAYG------------------------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 182 ikigaagldqDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIG 261
Cdd:cd00308 80 ----------SIERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 262 AGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGLPGYLAILDHLCARGWPraaFRPHAGYLFS------LHLVAALR 335
Cdd:cd00308 150 ADESVTTVDDALEALELGAV----DILQIKPTRVGGLTESRRAADLAEAFGIR---VMVHGTLESSigtaaaLHLAAALP 222
|
....*..
gi 15599236 336 -LGWAEA 341
Cdd:cd00308 223 nDRAIET 229
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
165-257 |
3.96e-15 |
|
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: 70.39 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 165 LEEELRRFVDLGYTHAKIKIGAaGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPH 244
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|...
gi 15599236 245 DFPTQAEVADIYP 257
Cdd:smart00922 84 DLEGLAELRRATP 96
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
63-261 |
6.29e-13 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta 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: 239440 [Multi-domain] Cd Length: 415 Bit Score: 69.68 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 63 ERFAPRLLGAPADSLASDDGSgidplrAWDLMMRD--------EKPGGHgercVAVGALDMALWDAAAKAAGLPLHRFLA 134
Cdd:cd03324 66 EALAHLVVGRDLESIVADMGK------FWRRLTSDsqlrwigpEKGVIH----LATAAVVNAVWDLWAKAEGKPLWKLLV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 135 -------------RRLG-----------LAEDYPQ---RVPVYAGGGYP----------YPHDDLGRLeeeLRRFVDLGY 177
Cdd:cd03324 136 dmtpeelvscidfRYITdaltpeealeiLRRGQPGkaaREADLLAEGYPayttsagwlgYSDEKLRRL---CKEALAQGF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 178 THAKIKIGAAgLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVAD-IY 256
Cdd:cd03324 213 THFKLKVGAD-LEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKaLA 291
|
....*
gi 15599236 257 PGPIG 261
Cdd:cd03324 292 PLPIG 296
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-374 |
3.24e-12 |
|
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: 67.12 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 1 MRIQEVRERSIPLSRYAGVAAATGGLSTSLVaVLTDIVRDGRRVvgyGHASVGRY------AQGGLIRErFAPRLLGAPA 74
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPL-VLIDLATDEGVT---GHSYLFTYtpaalkSLKQLLDD-MAALLVGEPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 75 DSLASDdgsgidplRAwdLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLhrflARRLGLAedyPQRVPVYAGGG 154
Cdd:cd03321 76 APAELE--------RA--LAKRFRLLGYTGLVRMAAAGIDMAAWDALAKVHGLPL----AKLLGGN---PRPVQAYDSHG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 155 YpyphDDLGRLEEELRRFVDLGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGL 234
Cdd:cd03321 139 L----DGAKLATERAVTAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 235 WWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVRrerdvlvfdpvhcYGLPGYLAILDhlcARGWP 314
Cdd:cd03321 215 TWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACD-------------LVMPDLMKIGG---VTGWL 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599236 315 RAAFRPHA-GYLFSLHLVAALRLGWAEATPSA-FRPFDDFAGA-----LPFSSGLAGLPQSPGIGFE 374
Cdd:cd03321 279 RASALAEQaGIPMSSHLFQEISAHLLAVTPTAhWLEYVDWAGAileppLKFEDGNAVIPDEPGNGII 345
|
|
| 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 ... |
5-275 |
1.22e-11 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 64.90 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 5 EVRERSIPLsryAGVAAATGGLSTSLVAVLTDIVRDGrrVVGYGHASVGRYAQGglireRFAPRLLGAPADSLASDDGSG 84
Cdd:cd03319 3 SLRPERLPL---KRPFTIARGSRTEAENVIVEIELDG--ITGYGEAAPTPRVTG-----ETVESVLAALKSVRPALIGGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 85 IDPLRAWDLMmrdekpgghGERCVAVG----ALDMALWDAAAKAAGLPLHRFlarrLGLAedyPQRVPVYAgggYPYPHD 160
Cdd:cd03319 73 PRLEKLLEAL---------QELLPGNGaaraAVDIALWDLEAKLLGLPLYQL----WGGG---APRPLETD---YTISID 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 161 DLGRLEEELRRFVDLGYTHAKIKIGaAGLDQDRRRIDRALRVLGDAsRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDI 240
Cdd:cd03319 134 TPEAMAAAAKKAAKRGFPLLKIKLG-GDLEDDIERIRAIREAAPDA-RLRVDANQGWTPEEAVELLRELAELGVELIEQP 211
|
250 260 270
....*....|....*....|....*....|....*
gi 15599236 241 CDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLL 275
Cdd:cd03319 212 VPAGDDDGLAYLRDKSPLPIMADESCFSAADAARL 246
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
84-268 |
2.14e-11 |
|
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: 64.65 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 84 GIDPLRA---WDLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLHRFLArrlGLAEDYpQRVPVYAGGgypyphD 160
Cdd:cd03325 53 GKDPMNIehhWQVMYRGGFYRGGPVLMSAISGIDQALWDIKGKVLGVPVHQLLG---GQVRDR-VRVYSWIGG------D 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 161 DLGRLEEELRRFVDLGYThaKIKIGAAGLDQ---DRRRIDRALR-------VLGDASRLAVDAMNRYDAEGAVDAAKALA 230
Cdd:cd03325 123 RPSDVAEAARARREAGFT--AVKMNATEELQwidTSKKVDAAVErvaalreAVGPDIDIGVDFHGRVSKPMAKDLAKELE 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 15599236 231 PLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFS 268
Cdd:cd03325 201 PYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFS 238
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
5-374 |
2.91e-10 |
|
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: 61.26 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 5 EVRERSIPLSR--YAGVAAATGGLSTSLVAVLTDIVRDGRRvvgyGHASVGRYAQGGLIRERF-APRLLGApadslasdd 81
Cdd:cd03329 6 EVTVFEYPTQPvsFDGGHHHPGPAGTRKLALLTIETDEGAK----GHAFGGRPVTDPALVDRFlKKVLIGQ--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 82 gsgiDPL---RAWDLMMRDEKpgghGERCVAVGALDMALWDAAAKAAGLPLHRFLArrlglaeDYPQRVPVYAGggyPYP 158
Cdd:cd03329 73 ----DPLdreRLWQDLWRLQR----GLTDRGLGLVDIALWDLAGKYLGLPVHRLLG-------GYREKIPAYAS---TMV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 159 HDDLGRLE--EELRRF----VDLGYTHAKIKIGAAGLDQDRRRIDRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAP 231
Cdd:cd03329 135 GDDLEGLEspEAYADFaeecKALGYRAIKLHPWGPGVVRRDLKACLAVReAVGPDMRLMHDGAHWYSRADALRLGRALEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 232 LGLWWFEDICDPHDFPTQAEVADIYPGPIGAGE----ALFSLAEARLldlyggvRRERDVLVFDPVHCYGLPGYLAILdH 307
Cdd:cd03329 215 LGFFWYEDPLREASISSYRWLAEKLDIPILGTEhsrgALESRADWVL-------AGATDFLRADVNLVGGITGAMKTA-H 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599236 308 LCargwprAAFRP----HAGYLFSLHLVAALRLG-WAE-ATPSAFRPFDDFAGALPF------SSGLAGLPQSPGIGFE 374
Cdd:cd03329 287 LA------EAFGLdvelHGNGAANLHVIAAIRNTrYYErGLLHPSQKYDVYAGYLSVlddpvdSDGFVHVPKGPGLGVE 359
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
44-383 |
9.11e-10 |
|
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: 59.76 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 44 VVGYGHASV-GR-YAQGGLIRERFAPRLLGAPADSLASddgsgidplrAWDLMMRdekpGGHGER----CVAVGALDMAL 117
Cdd:cd03322 27 VTGLGDATLnGReLAVKAYLREHLKPLLIGRDANRIED----------IWQYLYR----GAYWRRgpvtMNAIAAVDMAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 118 WDAAAKAAGLPLHRFLArrlGLAEDypqrvpvyagGGYPYPH---DDLGRLEEELRRFVDLGYTHAKIKIgaagldqdrR 194
Cdd:cd03322 93 WDIKGKAAGMPLYQLLG---GKSRD----------GIMVYSHasgRDIPELLEAVERHLAQGYRAIRVQL---------P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 195 RIDRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEAR 273
Cdd:cd03322 151 KLFEAVReKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 274 LLDlyggVRRERDVLVFDPVHCYGLPGYLAILDhLCA-----RGWPRAAFRPHAGYLFSLHL-VAALRLGWAEATPSAFR 347
Cdd:cd03322 231 NLI----QERLIDYIRTTVSHAGGITPARKIAD-LASlygvrTGWHGPTDLSPVGMAAALHLdLWVPNFGIQEYMRHAEE 305
|
330 340 350
....*....|....*....|....*....|....*.
gi 15599236 348 PFDDFAGALPFSSGLAGLPQSPGIGFERQATLAGLF 383
Cdd:cd03322 306 TLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
12-272 |
9.71e-10 |
|
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: 59.64 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 12 PLSRYAGVAAATGGLSTSLVAVLTDivRDGrrVVGYGHA-SVGRYAQGG--------LIRERFAPRLLGAPADslasddg 82
Cdd:cd03318 13 PTRRPHQFAGTTMHTQSLVLVRLTT--SDG--VVGIGEAtTPGGPAWGGespetikaIIDRYLAPLLIGRDAT------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 83 sgiDPLRAWDLMMRDEKpgghGERCvAVGALDMALWDAAAKAAGLPLHRFLARRLglaedyPQRVPVyaggGYPYPHDDL 162
Cdd:cd03318 82 ---NIGAAMALLDRAVA----GNLF-AKAAIEMALLDAQGRRLGLPVSELLGGRV------RDSLPV----AWTLASGDT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 163 GRLEEELRRFVDLGYTHA-KIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDIC 241
Cdd:cd03318 144 ERDIAEAEEMLEAGRHRRfKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPV 223
|
250 260 270
....*....|....*....|....*....|.
gi 15599236 242 DPHDFPTQAEVADIYPGPIGAGEALFSLAEA 272
Cdd:cd03318 224 PRENLDGLARLRSRNRVPIMADESVSGPADA 254
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
84-298 |
2.66e-09 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 58.37 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 84 GIDPLRA---WDLMMRDEKPGGHGERCVAVGALDMALWDAAAKAAGLPLHRFLArrlGLAEDypqRVPVYA--GGGYPyp 158
Cdd:PRK14017 54 GKDPRRIedhWQVMYRGGFYRGGPILMSAIAGIDQALWDIKGKALGVPVHELLG---GLVRD---RIRVYSwiGGDRP-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 159 hDDLGrleEELRRFVDLGYTHakIKIGAAG----LDqDRRRIDRAL-RV------LGDASRLAVDAMNRYDAEGAVDAAK 227
Cdd:PRK14017 126 -ADVA---EAARARVERGFTA--VKMNGTEelqyID-SPRKVDAAVaRVaavreaVGPEIGIGVDFHGRVHKPMAKVLAK 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599236 228 ALAPLGLWWFEDICDPHDFPTQAEVADIYPGPIGAGEALFSLAEARLLDLYGGVrrerDVLVFDPVHCYGL 298
Cdd:PRK14017 199 ELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGV----DIIQPDLSHAGGI 265
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
167-288 |
2.98e-08 |
|
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: 54.19 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 167 EELRRFVDLGYTHAKIKIGAAGLDQDRRRIDRALRVLGDASRLAVDAmNR-YDAEGAVDAAKALAPLGLWWFEDICDPHD 245
Cdd:cd03320 88 GEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDA-NGgWSLEEALAFLEALAAGRIEYIEQPLPPDD 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 15599236 246 FPTQAEVAdiYPGPIGAGEAL------FSLAEARLLDLY-------GGVRRERDVL 288
Cdd:cd03320 167 LAELRRLA--AGVPIALDESLrrlddpLALAAAGALGALvlkpallGGPRALLELA 220
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
109-251 |
3.52e-04 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 42.20 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 109 AVGALDMALWDAAAKAAGLPLHRFLArrlGLAEDypqRVPVY--AGGGypyphdDLGRLEEELRRFVDLGYTHAKIKIGA 186
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLG---GASRE---GVMVYghANGR------DIDELLDDVARHLELGYKAIRVQCGV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 187 AGLD------QDRR---------------------------RIDRALR-VLGDASRLAVDAMNRYDAEGAVDAAKALAPL 232
Cdd:PRK15072 153 PGLKttygvsKGKGlayepatkgllpeeelwstekylrfvpKLFEAVRnKFGFDLHLLHDVHHRLTPIEAARLGKSLEPY 232
|
170
....*....|....*....
gi 15599236 233 GLWWFEDicdphdfPTQAE 251
Cdd:PRK15072 233 RLFWLED-------PTPAE 244
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
89-257 |
6.41e-04 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 41.64 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 89 RAWDLMMRDEKPGGHGERCV-AVGALDMALWDAAAKAAGLPLHRFLArrlGLAEDYPQrvpVYAGGGYPyphdDLGRlee 167
Cdd:PRK15440 103 LIWDQMLNATLYYGRKGLVMnTISCVDLALWDLLGKVRGLPVYKLLG---GAVRDELQ---FYATGARP----DLAK--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599236 168 elrrfvDLGYTHAKIKI------GAAGLDQDRRRIDRALRVLGDASRLAVDAMNRYDAEGAVDAAKALAPLGLWWFEDIC 241
Cdd:PRK15440 170 ------EMGFIGGKMPLhhgpadGDAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECL 243
|
170
....*....|....*.
gi 15599236 242 DPHDFPTQAEVADIYP 257
Cdd:PRK15440 244 PPDDYWGYRELKRNAP 259
|
|
| |
