|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
27-379 |
1.16e-128 |
|
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: 374.26 E-value: 1.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 27 RIEHVKLSLAFLPLATPvsdakvltgrQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPN 106
Cdd:cd03316 1 KITDVETFVLRVPLPEP----------GGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 107 DIDKIYTKLLWAGASVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTSGGFLHTPlDQVLKNVAI 185
Cdd:cd03316 71 DIERLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGgKVRDRVRVYASGGGYDDSP-EELAEEAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 186 SRENGIGGIKLKVGQPNTA-----EDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDI 260
Cdd:cd03316 150 AVAEGFTAVKLKVGGPDSGgedlrEDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 261 EGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFA-----MEVHL 335
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAggpigLAASL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 751930672 336 HLAAAYPLEPWLEHFEWLNP----LFNEQLELRDGRMWVSERHGLGFT 379
Cdd:cd03316 310 HLAAALPNFGILEYHLDDLPlredLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
27-384 |
1.28e-100 |
|
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: 302.90 E-value: 1.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 27 RIEHVKLSLAFLPLATPvsdakvLTGRQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKE-IADNLLGEDP 105
Cdd:COG4948 2 KITDIEVYPVRLPLKRP------FTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGAEAVAAALEEaLAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 106 NDIDKIYTKLLwagasvGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTSGgfLHTPlDQVLKNVA 184
Cdd:COG4948 76 LDIEALWQRLY------RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGgKVRDRVPVYATLG--IDTP-EEMAEEAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 185 ISRENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHA 264
Cdd:COG4948 147 EAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 265 QLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAME------VHLHLA 338
Cdd:COG4948 227 ELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLEsgiglaAALHLA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 751930672 339 AAYPLEPWLEHFE---WLNPLFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:COG4948 307 AALPNFDIVELDGpllLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDA 355
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
187-384 |
2.13e-77 |
|
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: 238.23 E-value: 2.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 187 RENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQL 266
Cdd:pfam13378 11 EARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 267 AAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHF-----AMEVHLHLAAAY 341
Cdd:pfam13378 91 RRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSgggpiGLAASLHLAAAV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 751930672 342 PLEPWLEHFEWLNP----LFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:pfam13378 171 PNLLIQEYFLDPLLleddLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
63-328 |
6.85e-38 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 141.02 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 63 IIAEIRSRDGfeGVGFSYSKrAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPLDIALWDM 142
Cdd:PRK15440 59 LVVEVEAENG--QVGFAVST-AGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDLALWDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 143 KAKRAGLPLAKLL-GAHRDSVQCYNTSG--------GFL-------HTPLDqvlknvaisrenGIGGIKlkvgqpntaED 206
Cdd:PRK15440 136 LGKVRGLPVYKLLgGAVRDELQFYATGArpdlakemGFIggkmplhHGPAD------------GDAGLR---------KN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 207 IRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAAldtpIATGEMLTSfREH 286
Cdd:PRK15440 195 AAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN----APAGMMVTS-GEH 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 751930672 287 E-------QLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPH 328
Cdd:PRK15440 270 EatlqgfrTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
187-272 |
1.06e-29 |
|
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: 110.45 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 187 RENGIGGIKLKVGQPNtAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQL 266
Cdd:smart00922 13 AEAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAEL 91
|
....*.
gi 751930672 267 AAALDT 272
Cdd:smart00922 92 RRATPI 97
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
38-324 |
2.27e-25 |
|
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 low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 104.92 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 38 LPLATPVSDAKVltgrqkPLTEVAIIIAEIRSRDGFEGVG--FSYSKRAGGQGIYAHAKEI-----ADNLLGE--DPNDI 108
Cdd:TIGR01928 5 EPFKSPFKTSKG------TLNHRDCLIIELIDDKGNAGFGevVAFQTPWYTHETIATVKHIiedffEPNINKEfeHPSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 109 DKIYTKLLwaGASVGRSGmavqaispLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGgflHTPLDQVLKNVAISRE 188
Cdd:TIGR01928 79 LELVRSLK--GTPMAKAG--------LEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSG---LANDEQMLKQIESLKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 189 NGIGGIKLKVgQPNTAEDIRRLtavREALGPDFPLMVDANQQWDRETAIRMgRKMEQFNLIWIEEPLDAYDIEGHAQLAA 268
Cdd:TIGR01928 146 TGYKRIKLKI-TPQIMHQLVKL---RRLRFPQIPLVIDANESYDLQDFPRL-KELDRYQLLYIEEPFKIDDISMLDELAK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 751930672 269 ALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRK 324
Cdd:TIGR01928 221 GTITPICLDESITSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAK 276
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
27-379 |
1.16e-128 |
|
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: 374.26 E-value: 1.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 27 RIEHVKLSLAFLPLATPvsdakvltgrQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPN 106
Cdd:cd03316 1 KITDVETFVLRVPLPEP----------GGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 107 DIDKIYTKLLWAGASVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTSGGFLHTPlDQVLKNVAI 185
Cdd:cd03316 71 DIERLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGgKVRDRVRVYASGGGYDDSP-EELAEEAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 186 SRENGIGGIKLKVGQPNTA-----EDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDI 260
Cdd:cd03316 150 AVAEGFTAVKLKVGGPDSGgedlrEDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 261 EGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFA-----MEVHL 335
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAggpigLAASL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 751930672 336 HLAAAYPLEPWLEHFEWLNP----LFNEQLELRDGRMWVSERHGLGFT 379
Cdd:cd03316 310 HLAAALPNFGILEYHLDDLPlredLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
27-384 |
1.28e-100 |
|
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: 302.90 E-value: 1.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 27 RIEHVKLSLAFLPLATPvsdakvLTGRQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKE-IADNLLGEDP 105
Cdd:COG4948 2 KITDIEVYPVRLPLKRP------FTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGAEAVAAALEEaLAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 106 NDIDKIYTKLLwagasvGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTSGgfLHTPlDQVLKNVA 184
Cdd:COG4948 76 LDIEALWQRLY------RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGgKVRDRVPVYATLG--IDTP-EEMAEEAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 185 ISRENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHA 264
Cdd:COG4948 147 EAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 265 QLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAME------VHLHLA 338
Cdd:COG4948 227 ELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLEsgiglaAALHLA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 751930672 339 AAYPLEPWLEHFE---WLNPLFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:COG4948 307 AALPNFDIVELDGpllLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDA 355
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
187-384 |
2.13e-77 |
|
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: 238.23 E-value: 2.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 187 RENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQL 266
Cdd:pfam13378 11 EARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 267 AAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHF-----AMEVHLHLAAAY 341
Cdd:pfam13378 91 RRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSgggpiGLAASLHLAAAV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 751930672 342 PLEPWLEHFEWLNP----LFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:pfam13378 171 PNLLIQEYFLDPLLleddLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
58-381 |
4.17e-62 |
|
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: 203.33 E-value: 4.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 58 TEVAIIIAEIRSRDGFegVGFsYSKRAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPLDI 137
Cdd:cd03327 7 TRVGWLFVEIETDDGT--VGY-ANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGRKGIAMAAISAVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 138 ALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTsgGFLHTPLDQVLKNVAISRENGIGGIKLKV------GQPNTAEDIRRL 210
Cdd:cd03327 84 ALWDLLGKIRGEPVYKLLGgRTRDKIPAYAS--GLYPTDLDELPDEAKEYLKEGYRGMKMRFgygpsdGHAGLRKNVELV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 211 TAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLI 290
Cdd:cd03327 162 RAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 291 LGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLAAAYPLEPWLEHF-----EWLNPLFnEQLEL-- 363
Cdd:cd03327 242 EGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQIYNYHFIMSEPNSPFAEYLpnspdEVGNPLF-YYIFLne 320
|
330 340
....*....|....*....|.
gi 751930672 364 ---RDGRMWVSERHGLGFTLS 381
Cdd:cd03327 321 pvpVNGYFDLSDKPGFGLELN 341
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
27-386 |
5.78e-61 |
|
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: 200.79 E-value: 5.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 27 RIEHVKLSLAFLPLATPVSDAkVLTGRQKPLtevaiIIAEIRSRDGFEGVG--FSYSKRAGgQGIYAHAKEIADNLLGED 104
Cdd:cd03321 2 LITGLRARAVNVPMQYPVHTS-VGTVATAPL-----VLIDLATDEGVTGHSylFTYTPAAL-KSLKQLLDDMAALLVGEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 105 --PNDIDKIYTK---LLwagasvGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGgflhtpLDQV 179
Cdd:cd03321 75 laPAELERALAKrfrLL------GYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHG------LDGA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 180 lkNVAISR-----ENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEP 254
Cdd:cd03321 143 --KLATERavtaaEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 255 LDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVH 334
Cdd:cd03321 221 TLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEIS 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 751930672 335 LHLAAAYPLEPWLEHFEWLNPLFNEQLELRDGRMWVSERHGLGFTLSEQARR 386
Cdd:cd03321 301 AHLLAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVR 352
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
59-352 |
2.00e-56 |
|
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: 188.78 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 59 EVAIIIAEIRSrDGFEGVGFSYSKRAGGQGIYAHakeIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPLDIA 138
Cdd:cd03328 27 ATTLVLVEVRA-GGRTGLGYTYADAAAAALVDGL---LAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAMAISAVDIA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 139 LWDMKAKRAGLPLAKLLGAHRDSVQCYNtSGGFLHTPLDQVLKNVAISRENGIGGIKLKVGQpNTAEDIRRLTAVREALG 218
Cdd:cd03328 103 LWDLKARLLGLPLARLLGRAHDSVPVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGR-DPRRDPDRVAAARRAIG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 219 PDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQL--AAALDTPIATGEMLTSFREHEQLILGNACD 296
Cdd:cd03328 181 PDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVreRGPAGMDIAAGEYAYTLAYFRRLLEAHAVD 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 751930672 297 FVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLAAAYPLepwLEHFEW 352
Cdd:cd03328 261 VLQADVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVPR---LRHLEW 313
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
28-348 |
4.98e-46 |
|
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: 161.80 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 28 IEHVKLSLAFLPLATPVSDAKVLTGRQKPLTEVAIIiaEIRSRDGFEGVGFsyskrAGGQGIYAHAKE--IADNLLGEDP 105
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALL--TIETDEGAKGHAF-----GGRPVTDPALVDrfLKKVLIGQDP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 106 NDIDKIYTKLL-WAGasvgrsGMAVQAISPLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTS-----GGFLHTPldQV 179
Cdd:cd03329 75 LDRERLWQDLWrLQR------GLTDRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYASTmvgddLEGLESP--EA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 180 LKNVAIS-RENGIGGIKLKV-GQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDA 257
Cdd:cd03329 147 YADFAEEcKALGYRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 258 YDIEGHAQLAAALDTPIATGEMLTSFREH-EQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLH 336
Cdd:cd03329 227 ASISSYRWLAEKLDIPILGTEHSRGALESrADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLH 306
|
330
....*....|..
gi 751930672 337 LAAAYPLEPWLE 348
Cdd:cd03329 307 VIAAIRNTRYYE 318
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
70-328 |
2.16e-44 |
|
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: 158.66 E-value: 2.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 70 RDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPNDI----DKIYTKLL------WAGASVGRSGMAVQAISPldiAL 139
Cdd:cd03324 42 AAGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIvadmGKFWRRLTsdsqlrWIGPEKGVIHLATAAVVN---AV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 140 WDMKAKRAGLPLAKLLG------------------------------------------AHRDSVQCYNTSGGFLHTPLD 177
Cdd:cd03324 119 WDLWAKAEGKPLWKLLVdmtpeelvscidfryitdaltpeealeilrrgqpgkaareadLLAEGYPAYTTSAGWLGYSDE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 178 QVLKNVAISRENGIGGIKLKVGQpNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDA 257
Cdd:cd03324 199 KLRRLCKEALAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSP 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 751930672 258 YDIEGHAQLAAALDT---PIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPH 328
Cdd:cd03324 278 DDILGHAAIRKALAPlpiGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPH 351
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
94-381 |
4.41e-44 |
|
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: 156.33 E-value: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 94 KEIADNLLGEDPNDIDKIYTKL----LWAGASVGRSgmavqAISPLDIALWDMKAKRAGLPLAKLLGAH-RDSVQCYNTS 168
Cdd:cd03325 45 QELEDYLIGKDPMNIEHHWQVMyrggFYRGGPVLMS-----AISGIDQALWDIKGKVLGVPVHQLLGGQvRDRVRVYSWI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 169 GGflhTPLDQVLKNVAISRENGIGGIKLK-------VGQPNTAED-IRRLTAVREALGPDFPLMVDANQQWDRETAIRMG 240
Cdd:cd03325 120 GG---DRPSDVAEAARARREAGFTAVKMNateelqwIDTSKKVDAaVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 241 RKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAK 320
Cdd:cd03325 197 KELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEA 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751930672 321 HGRKLAPH-----FAMEVHLHLAAAYP----------LEPWLEHFEWLNPLFNEQLELRDGRMWVSERHGLGFTLS 381
Cdd:cd03325 277 YDVALAPHcplgpIALAASLHVDASTPnfliqeqslgIHYNEGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
131-348 |
5.85e-44 |
|
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: 152.48 E-value: 5.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 131 AISPLDIALWDMKAKRAGLPLA-KLLGAHRDSVQCYNTsggflhtpldqvlknvaisrengiggiklkvgqpntaedIRR 209
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAeLLGGGSRDRVPAYGS---------------------------------------IER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 210 LTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQL 289
Cdd:cd00308 84 VRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751930672 290 ILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPH------FAMEVHLHLAAAYPLEPWLE 348
Cdd:cd00308 164 LELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHgtlessIGTAAALHLAAALPNDRAIE 228
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
100-386 |
2.31e-41 |
|
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: 149.51 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 100 LLGEDPNDIDKIYtKLLWAGASVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCYNTSGGflhTPLDQ 178
Cdd:cd03322 54 LIGRDANRIEDIW-QYLYRGAYWRRGPVTMNAIAAVDMALWDIKGKAAGMPLYQLLGgKSRDGIMVYSHASG---RDIPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 179 VLKNVAISRENGIGGIKlkvgqpntAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAY 258
Cdd:cd03322 130 LLEAVERHLAQGYRAIR--------VQLPKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 259 DIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFA-------M 331
Cdd:cd03322 202 NQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdlspvgM 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 751930672 332 EVHLHLAAAYP---LEPWLEHFEWLNPLFNEQLELRDGRMWVSERHGLGFTLSEQARR 386
Cdd:cd03322 282 AAALHLDLWVPnfgIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAA 339
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
63-328 |
6.85e-38 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 141.02 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 63 IIAEIRSRDGfeGVGFSYSKrAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGASVGRSGMAVQAISPLDIALWDM 142
Cdd:PRK15440 59 LVVEVEAENG--QVGFAVST-AGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDLALWDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 143 KAKRAGLPLAKLL-GAHRDSVQCYNTSG--------GFL-------HTPLDqvlknvaisrenGIGGIKlkvgqpntaED 206
Cdd:PRK15440 136 LGKVRGLPVYKLLgGAVRDELQFYATGArpdlakemGFIggkmplhHGPAD------------GDAGLR---------KN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 207 IRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAAldtpIATGEMLTSfREH 286
Cdd:PRK15440 195 AAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN----APAGMMVTS-GEH 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 751930672 287 E-------QLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPH 328
Cdd:PRK15440 270 EatlqgfrTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
121-322 |
1.90e-36 |
|
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: 133.62 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 121 SVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGGflhTPLDQVLKNVAISRENGIGGIKLKVGq 200
Cdd:cd03315 34 DDGLVGWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGL---GEPAEVAEEARRALEAGFRTFKLKVG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 201 PNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEML 280
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 751930672 281 TSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHG 322
Cdd:cd03315 190 FTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALG 231
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
38-343 |
2.99e-35 |
|
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: 133.67 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 38 LPLATPVSDAKVLTGRQKpLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAH------AKEIADNLLGEDPNDID-- 109
Cdd:cd03326 10 IPLSSPIANAYVDFSGLT-TSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRErfiprlLAAAPDSLLDDAGGNLDpa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 110 KIYtKLLWAGASVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLGAH------RDSVQCYnTSGGFLHTPLDQVLKNV 183
Cdd:cd03326 89 RAW-AAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRygrgqaDPRVPVY-AAGGYYYPGDDLGRLRD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 184 AISR--ENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIE 261
Cdd:cd03326 167 EMRRylDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 262 GHAQLAAALDTPIATGEMLTSFREHEQLILGNAC----DFVQPDAPRVGGISPFLKIMDLAAKHG---RKLAPHFAMEVH 334
Cdd:cd03326 247 LQAELADHYDGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGwsrRRFFPHGGHLMS 326
|
....*....
gi 751930672 335 LHLAAAYPL 343
Cdd:cd03326 327 LHIAAGLGL 335
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
62-386 |
5.76e-35 |
|
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: 132.44 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 62 IIIAEIRSRDGFEGVGfsyskRAGGQGIYAH-------AKEIADN-----LLGEDPNDIDKIYTKLlwAGASVGRSgmav 129
Cdd:cd03318 30 LVLVRLTTSDGVVGIG-----EATTPGGPAWggespetIKAIIDRylaplLIGRDATNIGAAMALL--DRAVAGNL---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 130 QAISPLDIALWDMKAKRAGLPLAKLLG-AHRDS--VQCYNTSGGFLHTpLDQVLKNVAISRENGIggiKLKVGQPNTAED 206
Cdd:cd03318 99 FAKAAIEMALLDAQGRRLGLPVSELLGgRVRDSlpVAWTLASGDTERD-IAEAEEMLEAGRHRRF---KLKMGARPPADD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 207 IRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREH 286
Cdd:cd03318 175 LAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 287 EQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGrkLAPHFAM--------EVHLHLAAAYPLEPWleHFEWLNPLF- 357
Cdd:cd03318 255 FELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAG--IALYGGTmlessigtAASAHLFATLPSLPF--GCELFGPLLl 330
|
330 340 350
....*....|....*....|....*....|....
gi 751930672 358 -----NEQLELRDGRMWVSERHGLGFTLSEQARR 386
Cdd:cd03318 331 aedllEEPLAYRDGELHVPTGPGLGVRLDEDKVR 364
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
127-384 |
1.03e-33 |
|
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: 128.51 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 127 MAVQAispLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGgfLHTPLDQVLKNVAISRENGIGGIKLKVgQPNtaED 206
Cdd:cd03317 94 MAKAG---LEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIG--IQDDVEQLLKQIERYLEEGYKRIKLKI-KPG--WD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 207 IRRLTAVREALgPDFPLMVDANQQWDRETAIRMgRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREH 286
Cdd:cd03317 166 VEPLKAVRERF-PDIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAEDA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 287 EQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGrklaPHF----AME------VHLHLAA----AYP--LEPWLEHF 350
Cdd:cd03317 244 RKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHG----IPVwcggMLEsgigraHNVALASlpnfTYPgdISASSRYF 319
|
250 260 270
....*....|....*....|....*....|....
gi 751930672 351 EwlNPLFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:cd03317 320 E--EDIITPPFELENGIISVPTGPGIGVTVDREA 351
|
|
| 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 ... |
58-341 |
1.68e-33 |
|
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: 127.30 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 58 TEVAIIIAEIRSrDGFEGVG-FSYSKRAGGQ---GIYAHAKEIADNLLGEDPNdIDKIYTKLlwAGASVGRSGmavqAIS 133
Cdd:cd03319 23 TEAENVIVEIEL-DGITGYGeAAPTPRVTGEtveSVLAALKSVRPALIGGDPR-LEKLLEAL--QELLPGNGA----ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 134 PLDIALWDMKAKRAGLPLAKL-LGAHRDSVQCYNTSGgfLHTPLDQVLKNVAIsRENGIGGIKLKVGQpNTAEDIRRLTA 212
Cdd:cd03319 95 AVDIALWDLEAKLLGLPLYQLwGGGAPRPLETDYTIS--IDTPEAMAAAAKKA-AKRGFPLLKIKLGG-DLEDDIERIRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 213 VREALgPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILG 292
Cdd:cd03319 171 IREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLAGG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 751930672 293 NACDFVQPDAPRVGGISPFLKIMDLAAKHGRK------LAPHFAMEVHLHLAAAY 341
Cdd:cd03319 250 GAYDGINIKLMKTGGLTEALRIADLARAAGLKvmvgcmVESSLSIAAAAHLAAAK 304
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
100-384 |
4.71e-33 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 127.72 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 100 LLGEDPNDIDKIYtKLLWAGASVGRSGMAVQAISPLDIALWDMKAKRAGLPLAKLLG-AHRDSVQCY-NTSGGFLHTPLD 177
Cdd:PRK15072 55 LIGRDAHRIEDIW-QYLYRGAYWRRGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGgASREGVMVYgHANGRDIDELLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 178 QVLKNV-----AISRENGIGGIK----LKVGQPNTAEDIRR---------------------LTAVREALGPDFPLMVDA 227
Cdd:PRK15072 134 DVARHLelgykAIRVQCGVPGLKttygVSKGKGLAYEPATKgllpeeelwstekylrfvpklFEAVRNKFGFDLHLLHDV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 228 NQqwdRETAI---RMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPR 304
Cdd:PRK15072 214 HH---RLTPIeaaRLGKSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTH 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 305 VGGISPFLKIMDLAAKHGRKLAPHFA-------MEVHLHLAAAYP---LEPWLEHFEWLNPLFNEQLELRDGRMWVSERH 374
Cdd:PRK15072 291 AGGITHLRRIADFAALYQVRTGSHGPtdlspvcMAAALHFDLWVPnfgIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAP 370
|
330
....*....|
gi 751930672 375 GLGFTLSEQA 384
Cdd:PRK15072 371 GLGVDFDEKL 380
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
91-342 |
1.46e-31 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 123.47 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 91 AHAKEIADNLLGEDPNDIDKIYTKLLWAGasVGRSG-MAVQAISPLDIALWDMKAKRAGLPLAKLLGAH-RDSVQCYNTS 168
Cdd:PRK14017 43 AAVHELADYLIGKDPRRIEDHWQVMYRGG--FYRGGpILMSAIAGIDQALWDIKGKALGVPVHELLGGLvRDRIRVYSWI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 169 GGflHTPLDqVLKNVAISRENGIGGIKLK-------VGQPNTAED-IRRLTAVREALGPDFPLMVDANQQWDRETAIRMG 240
Cdd:PRK14017 121 GG--DRPAD-VAEAARARVERGFTAVKMNgteelqyIDSPRKVDAaVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 241 RKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAK 320
Cdd:PRK14017 198 KELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEA 277
|
250 260
....*....|....*....|....*..
gi 751930672 321 HGRKLAPH-----FAMEVHLHLAAAYP 342
Cdd:PRK14017 278 YDVALAPHcplgpIALAACLQVDAVSP 304
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
187-272 |
1.06e-29 |
|
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: 110.45 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 187 RENGIGGIKLKVGQPNtAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQL 266
Cdd:smart00922 13 AEAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAEL 91
|
....*.
gi 751930672 267 AAALDT 272
Cdd:smart00922 92 RRATPI 97
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
38-324 |
2.27e-25 |
|
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 low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 104.92 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 38 LPLATPVSDAKVltgrqkPLTEVAIIIAEIRSRDGFEGVG--FSYSKRAGGQGIYAHAKEI-----ADNLLGE--DPNDI 108
Cdd:TIGR01928 5 EPFKSPFKTSKG------TLNHRDCLIIELIDDKGNAGFGevVAFQTPWYTHETIATVKHIiedffEPNINKEfeHPSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 109 DKIYTKLLwaGASVGRSGmavqaispLDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGgflHTPLDQVLKNVAISRE 188
Cdd:TIGR01928 79 LELVRSLK--GTPMAKAG--------LEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSG---LANDEQMLKQIESLKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 189 NGIGGIKLKVgQPNTAEDIRRLtavREALGPDFPLMVDANQQWDRETAIRMgRKMEQFNLIWIEEPLDAYDIEGHAQLAA 268
Cdd:TIGR01928 146 TGYKRIKLKI-TPQIMHQLVKL---RRLRFPQIPLVIDANESYDLQDFPRL-KELDRYQLLYIEEPFKIDDISMLDELAK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 751930672 269 ALDTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRK 324
Cdd:TIGR01928 221 GTITPICLDESITSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAK 276
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
177-345 |
4.72e-22 |
|
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: 94.63 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 177 DQVLKNVAISRENGIGGIKLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLD 256
Cdd:cd03320 84 AAALGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 257 AYDIEGHAQLAAAldTPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKImdLAAKHGRKLAPHF------- 329
Cdd:cd03320 164 PDDLAELRRLAAG--VPIALDESLRRLDDPLALAAAGALGALVLKPALLGGPRALLEL--AEEARARGIPAVVssaless 239
|
170
....*....|....*..
gi 751930672 330 -AMEVHLHLAAAYPLEP 345
Cdd:cd03320 240 iGLGALAHLAAALPPLP 256
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
63-384 |
6.74e-21 |
|
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: 93.54 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 63 IIAEIRSRDGFEGVGFSYskraGGQGIYAHAKEIADNLLGEDPNDIDK-IYTKLLWAGASVGRSG---------MAVQAI 132
Cdd:cd03323 31 NIVELTDDNGNTGVGESP----GGAEALEALLEAARSLVGGDVFGAYLaVLESVRVAFADRDAGGrglqtfdlrTTVHVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 133 SPLDIALWDMKAKRAGLPLAKLLG-AHRDSV-------------------QCYNTSGGFLHTPlDQVLKNVAISREN-GI 191
Cdd:cd03323 107 TAFEVALLDLLGQALGVPVADLLGgGQRDSVpflaylfykgdrhktdlpyPWFRDRWGEALTP-EGVVRLARAAIDRyGF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 192 GGIKLKVGQPNTAEDIRRLTAVREALgPDFPLMVDANQQWDRETAIRMGRKMEQFnLIWIEEPldAYDIEGHAQLAAALD 271
Cdd:cd03323 186 KSFKLKGGVLPGEEEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDP--CGGREGMAEFRRATG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 272 TPIATGEMLTSFREHEQLILGNACDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPH--------FAMEVhlHLAAAYPL 343
Cdd:cd03323 262 LPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHsnnhlgisLAMMT--HVAAAAPG 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 751930672 344 E--PWLEHFEWLNP--LFNEQLELRDGRMWVSERHGLGFTLSEQA 384
Cdd:cd03323 340 LitACDTHWIWQDGqvITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
63-156 |
2.09e-11 |
|
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold similarity with enolase N-terminal domain.
Pssm-ID: 397046 [Multi-domain] Cd Length: 117 Bit Score: 60.56 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 63 IIAEIRSRDGFEGVG--FSYSKRAGGQGIYAHAkEIADNLLGEDPNDID----KIYTKLLWAGAsvgrsgmavqAISPLD 136
Cdd:pfam02746 29 VIVRIETSEGVVGIGeaTSYGGRAETIKAILDD-HLAPLLIGRDAANISdlwqLMYRAALGNMS----------AKAAID 97
|
90 100
....*....|....*....|
gi 751930672 137 IALWDMKAKRAGLPLAKLLG 156
Cdd:pfam02746 98 MALWDLKAKVLNLPLADLLG 117
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
185-342 |
4.75e-09 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 57.29 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 185 ISRENGIGGIKLKVGQP--NTAEDIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKM-EQFNLIWIEEPLDAydIE 261
Cdd:PRK02901 97 LARFPGCRTAKVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT--VE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 262 GHAQLAAALDTPIATGEmltSFREHEQLI----LGnACDFVQPDAPRVGGISPFLKI---MDLAAKHGRKLAPHFAMEVH 334
Cdd:PRK02901 175 ELAELRRRVGVPIAADE---SIRRAEDPLrvarAG-AADVAVLKVAPLGGVRAALDIaeqIGLPVVVSSALDTSVGIAAG 250
|
....*...
gi 751930672 335 LHLAAAYP 342
Cdd:PRK02901 251 LALAAALP 258
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
135-348 |
3.12e-08 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 56.02 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 135 LDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSG-----GFLH---TPLDQVLKNVAISREnGIGGIKLKVGQ-PNTAE 205
Cdd:PLN02980 1043 LEMAILNAIAVRHGSSLLNILDPYQKDENGSEQSHsvqicALLDsngSPLEVAYVARKLVEE-GFSAIKLKVGRrVSPIQ 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 206 DIRRLTAVREALGPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYD--IEGHAQLAaaldTPIATGEMLTSF 283
Cdd:PLN02980 1122 DAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDEDdlIKFCEETG----LPVALDETIDKF 1197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751930672 284 REHeqlILGNACDFVQP-------DAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLAAAYPLEPWLE 348
Cdd:PLN02980 1198 EEC---PLRMLTKYTHPgivavviKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFASYLE 1266
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
114-259 |
1.29e-05 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 46.66 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 114 KLLWAGAsvgrsgmavqAISPLDIALWDMKAKRAGLPLAKLLGAHRDsVQCYNTSGGFLHTPlDQVLKNVAISRENGIGG 193
Cdd:PRK15129 80 KLLPAGA----------ARNAVDCALWDLAARQQQQSLAQLIGITLP-ETVTTAQTVVIGTP-EQMANSASALWQAGAKL 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751930672 194 IKLKVGQPNTAEdirRLTAVREALgPDFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDAYD 259
Cdd:PRK15129 148 LKVKLDNHLISE---RMVAIRSAV-PDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQD 209
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
195-288 |
1.54e-03 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 40.38 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751930672 195 KLKVGQPNTAEDIRRLTAVREALGPDFPLMVDANQQWDRETA---IRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALD 271
Cdd:PRK02714 138 KWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQ 217
|
90
....*....|....*..
gi 751930672 272 TPIATGEMLTSFREHEQ 288
Cdd:PRK02714 218 TPIALDESVANLAQLQQ 234
|
|
| |
