|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
6-383 |
0e+00 |
|
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: 523.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 6 KITSVSVDVFSFPSRRAVDSAGHAHPGEEKPVKMAMLRIACDEGSEGFSFGSPELIRPHIIESFVKKVLIGQNPMNREKI 85
Cdd:cd03329 1 KITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFGGRPVTDPALVDRFLKKVLIGQDPLDRERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 86 WQELAHWQRGSasqfTDRALALVEQALWDLAGRALKLPVHKLLGGYRDKVLAYGSTMCGDDLpGGLSTPDEYGQFAEKLV 165
Cdd:cd03329 81 WQDLWRLQRGL----TDRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYASTMVGDDL-EGLESPEAYADFAEECK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 166 KRGYKGIKLHTWMPPisfapDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAE 245
Cdd:cd03329 156 ALGYRAIKLHPWGPG-----VVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 246 SYAWLAANLDIPVLGPESIAGKYHSRASWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNGAANLAVVGA 325
Cdd:cd03329 231 SYRWLAEKLDIPILGTEHSRGALESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLHVIAA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1499501876 326 ISNCRWYERGLLHPFLEYDDVPAYLNTLVDPMDSDGFVHLSGQPGLGEDINFSYIETH 383
Cdd:cd03329 311 IRNTRYYERGLLHPSQKYDVYAGYLSVLDDPVDSDGFVHVPKGPGLGVEIDFDYIERN 368
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
6-372 |
2.09e-87 |
|
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: 268.71 E-value: 2.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 6 KITSVSVDVFSFPSRRavdsaghaHPGEEKPVKMAMLRIACDEGSEGFSFGSPELIRP---HIIESFVKKVLIGQNPMNR 82
Cdd:cd03316 1 KITDVETFVLRVPLPE--------PGGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSavaAAIEDLLAPLLIGRDPLDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 83 EKIWQELAHWQR-GSASQFTDRALALVEQALWDLAGRALKLPVHKLLGGY-RDKVLAYGSTMCGDDlpgglsTPDEYGQF 160
Cdd:cd03316 73 ERLWEKLYRRLFwRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKvRDRVRVYASGGGYDD------SPEELAEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 161 AEKLVKRGYKGIKLHTWMPPISFApDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMM 240
Cdd:cd03316 147 AKRAVAEGFTAVKLKVGGPDSGGE-DLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 241 EDSAESYAWLAANLDIPVLGPESIAGKYHSRAsWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNG---- 316
Cdd:cd03316 226 PDDLEGLARLRQATSVPIAAGENLYTRWEFRD-LLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGgpig 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1499501876 317 -AANLAVVGAISNCRWYERGLLHPFLEYDDVPAylntlvDPMDSDGFVHLSGQPGLG 372
Cdd:cd03316 305 lAASLHLAAALPNFGILEYHLDDLPLREDLFKN------PPEIEDGYVTVPDRPGLG 355
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
5-383 |
3.54e-75 |
|
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: 237.41 E-value: 3.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 5 MKITSVSVDVFSFPSRRAVDSAGHAHPGEEkpvkMAMLRIACDEGSEGFSFGSPELIRP----HIIESFVKKVLIGQNPM 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERD----VVLVRVETDDGITGWGEAVPGGTGAeavaAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 81 NREKIWQELAHWQRGSASqftdrALALVEQALWDLAGRALKLPVHKLLGG-YRDKVLAYGSTmcgddlpgGLSTPDEYGQ 159
Cdd:COG4948 77 DIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLLGGkVRDRVPVYATL--------GIDTPEEMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 160 FAEKLVKRGYKGIKLHTwmppisFAPDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPM 239
Cdd:COG4948 144 EAREAVARGFRALKLKV------GGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 240 MEDSAESYAWLAANLDIPVLGPESIagkyHSRASW---VTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNG 316
Cdd:COG4948 218 PAEDLEGLAELRRATPVPIAADESL----TSRADFrrlIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCML 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1499501876 317 ------AANLAVVGAISNCRWYErgLLHPFLEYDDVpaylntLVDPMD-SDGFVHLSGQPGLGEDINFSYIETH 383
Cdd:COG4948 294 esgiglAAALHLAAALPNFDIVE--LDGPLLLADDL------VEDPLRiEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
156-376 |
4.63e-51 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 170.05 E-value: 4.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 156 EYGQFAEKLVKR-GYKGIKLHTwmppisFAPDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAW 234
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKV------GGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 235 FEEPMMEDSAESYAWLAANLDIPVLGPESIAGKyHSRASWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHG 314
Cdd:pfam13378 75 IEEPVPPDDLEGLARLRRATPVPIATGESLYSR-EDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499501876 315 NG-----AANLAVVGAISNCRWYERGLLHPFLEYDDVPaylntlVDPMDSDGFVHLSGQPGLGEDIN 376
Cdd:pfam13378 154 GGgpiglAASLHLAAAVPNLLIQEYFLDPLLLEDDLLT------EPLEVEDGRVAVPDGPGLGVELD 214
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
42-376 |
3.62e-45 |
|
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: 158.65 E-value: 3.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 42 LRIACDEGSEGF--SFGSPelIRPHIIESFVKKVLIGQNPMNREKIWQEL----AHWQRGSASQftdRALALVEQALWDL 115
Cdd:cd03327 14 VEIETDDGTVGYanTTGGP--VACWIVDQHLARFLIGKDPSDIEKLWDQMyratLAYGRKGIAM---AAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 116 AGRALKLPVHKLLGG-YRDKVLAYGSTMCGDDLPgglSTPDEygqfAEKLVKRGYKGIKlhtwMPPISFAPDP----RMD 190
Cdd:cd03327 89 LGKIRGEPVYKLLGGrTRDKIPAYASGLYPTDLD---ELPDE----AKEYLKEGYRGMK----MRFGYGPSDGhaglRKN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 191 VQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIAGKYHS 270
Cdd:cd03327 158 VELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 271 RaSWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNGAANLAVVGAISNCrwyergllhPFLEY------- 343
Cdd:cd03327 238 K-RLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQIYNYHFIMSEPNS---------PFAEYlpnspde 307
|
330 340 350
....*....|....*....|....*....|....
gi 1499501876 344 DDVPAYLNTLVD-PMDSDGFVHLSGQPGLGEDIN 376
Cdd:cd03327 308 VGNPLFYYIFLNePVPVNGYFDLSDKPGFGLELN 341
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
106-334 |
6.27e-37 |
|
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: 133.61 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 106 ALVEQALWDLAGRALKLPVH-KLLGGYRDKVLAYGStmcgddlpgglstpdeygqfaeklvkrgykgiklhtwmppisfa 184
Cdd:cd00308 45 SGIDMALWDLAAKALGVPLAeLLGGGSRDRVPAYGS-------------------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 185 pdprmdVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESi 264
Cdd:cd00308 81 ------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADES- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499501876 265 AGKYHSRASWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNG------AANLAVVGAISNCRWYER 334
Cdd:cd00308 154 VTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLessigtAAALHLAAALPNDRAIET 229
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
42-376 |
9.75e-33 |
|
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: 125.52 E-value: 9.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 42 LRIACDEGSEGFSFGSPELiRPHIIESFVKKV---LIGQNPMNREKIWQEL--AHWQRGSAsqFTDRALALVEQALWDLA 116
Cdd:cd03325 17 VKIETDEGVVGWGEPTVEG-KARTVEAAVQELedyLIGKDPMNIEHHWQVMyrGGFYRGGP--VLMSAISGIDQALWDIK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 117 GRALKLPVHKLLGGY-RDKVLAYGSTmcgddlpgGLSTPDEYGQFAEKLVKRGYKGIKLH--TWMPPISFAPDPRMDVQA 193
Cdd:cd03325 94 GKVLGVPVHQLLGGQvRDRVRVYSWI--------GGDRPSDVAEAARARREAGFTAVKMNatEELQWIDTSKKVDAAVER 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 194 CAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIAGKYHSRAS 273
Cdd:cd03325 166 VAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 274 wVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHG-----NGAANLAVVGAISNCRWYERGLLHPFLEYDDVPA 348
Cdd:cd03325 246 -LEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCplgpiALAASLHVDASTPNFLIQEQSLGIHYNEGDDLLD 324
|
330 340
....*....|....*....|....*...
gi 1499501876 349 YLNTLVDPMDSDGFVHLSGQPGLGEDIN 376
Cdd:cd03325 325 YLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
41-380 |
1.28e-28 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 114.99 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 41 MLRIACDEGSEGFsfGSPELI-RPHIIESFVKKV---LIGQNPMNREKIWQEL--AHWQRGSASQFTdrALALVEQALWD 114
Cdd:PRK14017 17 FLKIETDEGIVGW--GEPVVEgRARTVEAAVHELadyLIGKDPRRIEDHWQVMyrGGFYRGGPILMS--AIAGIDQALWD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 115 LAGRALKLPVHKLLGG-YRDKVLAYgSTMCGDDlpgglstPDEYGQFAEKLVKRGYKGIKLHTwMPPISFAPDPRmDVQA 193
Cdd:PRK14017 93 IKGKALGVPVHELLGGlVRDRIRVY-SWIGGDR-------PADVAEAARARVERGFTAVKMNG-TEELQYIDSPR-KVDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 194 C----AAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIagkyH 269
Cdd:PRK14017 163 AvarvAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERL----F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 270 SRasW-----VTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGN-G----AANLAVVGAISNCRWYERGL-LH 338
Cdd:PRK14017 239 SR--WdfkrvLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPlGpialAACLQVDAVSPNAFIQEQSLgIH 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1499501876 339 pfleYDDVPAYLNTLVDPMD---SDGFVHLSGQPGLGEDINFSYI 380
Cdd:PRK14017 317 ----YNQGADLLDYVKNKEVfayEDGFVAIPTGPGLGIEIDEAKV 357
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
6-376 |
2.65e-28 |
|
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: 113.69 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 6 KITSVSVDVFSfPSRRAVdsaghahpgeekpvkmaMLRIACDEGSEGF---SFGSPELIRPHIIESFVKKVLIGQNPMNR 82
Cdd:cd03322 1 KITAIEVIVTC-PGRNFV-----------------TLKITTDQGVTGLgdaTLNGRELAVKAYLREHLKPLLIGRDANRI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 83 EKIWQEL---AHWQRGSAsqfTDRALALVEQALWDLAGRALKLPVHKLLGGY-RDKVLAYGSTmCGDDLPGGLstpdeyg 158
Cdd:cd03322 63 EDIWQYLyrgAYWRRGPV---TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKsRDGIMVYSHA-SGRDIPELL------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 159 QFAEKLVKRGYKGIKLHTwmppisfapdPRMdvqaCAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEP 238
Cdd:cd03322 132 EAVERHLAQGYRAIRVQL----------PKL----FEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 239 MMEDSAESYAWLAANLDIPVlgpeSIAGKYHSRASW---VTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHgn 315
Cdd:cd03322 198 TPAENQEAFRLIRQHTATPL----AVGEVFNSIWDWqnlIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWH-- 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1499501876 316 GAANLAVVGAISNCR---WYERGLLHPFLEYDDvpaylNTL----VDPMDSDGFVHLSGQPGLGEDIN 376
Cdd:cd03322 272 GPTDLSPVGMAAALHldlWVPNFGIQEYMRHAE-----ETLevfpHSVRFEDGYLHPGEEPGLGVEID 334
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
6-376 |
4.15e-27 |
|
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: 110.48 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 6 KITSVSVDVFSFPSRRAVDSAGHAHpgeeKPVKMAMLRIACDEGSEG-----------FSFGSPELIRPhIIESFVKKVL 74
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTM----HTQSLVLVRLTTSDGVVGigeattpggpaWGGESPETIKA-IIDRYLAPLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 75 IGQNPMNREKIWQELAHWQRGSASqftdrALALVEQALWDLAGRALKLPVHKLLGG-YRDKV-----LAYGSTmcGDDLp 148
Cdd:cd03318 76 IGRDATNIGAAMALLDRAVAGNLF-----AKAAIEMALLDAQGRRLGLPVSELLGGrVRDSLpvawtLASGDT--ERDI- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 149 gglstpDEygqfAEKLVKRG-YKGIKLHTWmppisfAPDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGREL 227
Cdd:cd03318 148 ------AE----AEEMLEAGrHRRFKLKMG------ARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 228 QKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIAGkYHSRASWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFG 307
Cdd:cd03318 212 EAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSG-PADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAG 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499501876 308 MGCevHGN--------GAANLAVVGAISNCRWyerG--LLHPFLEYDDVpaylnTLVDPMDSDGFVHLSGQPGLGEDIN 376
Cdd:cd03318 291 IAL--YGGtmlessigTAASAHLFATLPSLPF---GceLFGPLLLAEDL-----LEEPLAYRDGELHVPTGPGLGVRLD 359
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
106-312 |
1.68e-24 |
|
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: 101.26 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 106 ALVEQALWDLAGRALKLPVHKLLGGYRDKV-LAYgstMCGddlpggLSTPDEYGQFAEKLVKRGYKGIKLHTwmppisfA 184
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGYRDRVrVAH---MLG------LGEPAEVAEEARRALEAGFRTFKLKV-------G 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 185 PDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESI 264
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1499501876 265 AGKYHSRASwVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEV 312
Cdd:cd03315 190 FTPHDAFRE-LALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMV 236
|
|
| 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 ... |
70-312 |
3.80e-23 |
|
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: 98.41 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 70 VKKVLIGQNPMNrEKIWQELAHWQRGSASqftdrALALVEQALWDLAGRALKLPVHKLLGGYRDKVLAYGSTMcgddlpg 149
Cdd:cd03319 64 VRPALIGGDPRL-EKLLEALQELLPGNGA-----ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTI------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 150 GLSTPDEYGQFAEKLVKRGYKGIKlhtwmppISFAPDPRMDVQACAAVREAVgPDVALMLDGYHWYSRTDALYIGRELQK 229
Cdd:cd03319 131 SIDTPEAMAAAAKKAAKRGFPLLK-------IKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 230 LDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIagkyHSRAS---WVTNKACDI----------LRagvagvggigPC 296
Cdd:cd03319 203 LGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESC----FSAADaarLAGGGAYDGiniklmktggLT----------EA 268
|
250
....*....|....*.
gi 1499501876 297 LKVAHLAESFGMGCEV 312
Cdd:cd03319 269 LRIADLARAAGLKVMV 284
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
65-372 |
5.71e-23 |
|
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: 98.64 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 65 IIESFVKKVLIGQNPMNREKIWQELAHWQR-----GSASQftdrALALVEQALWDLAGRALKLPVHKLLGGYRDKVLAYG 139
Cdd:cd03328 55 LVDGLLAPVVEGRDALDPPAAWEAMQRAVRnagrpGVAAM----AISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 140 StmcgddlpGGLST-PDEygQFAEKL---VKRGYKGIKLHTwmppisfAPDPRMDVQACAAVREAVGPDVALMLDGYHWY 215
Cdd:cd03328 131 S--------GGFTSyDDD--RLREQLsgwVAQGIPRVKMKI-------GRDPRRDPDRVAAARRAIGPDAELFVDANGAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 216 SRTDALYIGRELQKLDFAWFEEPMmedSAESYAWLAANLDIPVLGPESIAGKYHSRASWVTN----KACDILRAGVAGVG 291
Cdd:cd03328 194 SRKQALALARAFADEGVTWFEEPV---SSDDLAGLRLVRERGPAGMDIAAGEYAYTLAYFRRlleaHAVDVLQADVTRCG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 292 GIGPCLKVAHLAESFGMGCEVHGNGAANLAVVGAISNCRWYERGLLHPFLE---YDDVPAYLNTLVDPMDSdgfvhlsgQ 368
Cdd:cd03328 271 GVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVPRLRHLEWFHDHVRIErmlFDGAPDPSGGALRPDLS--------R 342
|
....
gi 1499501876 369 PGLG 372
Cdd:cd03328 343 PGLG 346
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
5-238 |
5.51e-22 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 96.52 E-value: 5.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 5 MKITSVSVDVFSfPSRRAVdsaghahpgeekpvkmaMLRIACDEGSEGF---SFGSPEL-----IRPHIIESfvkkvLIG 76
Cdd:PRK15072 1 MKIVDAEVIVTC-PGRNFV-----------------TLKITTDDGVTGLgdaTLNGRELavasyLQDHVCPL-----LIG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 77 QNPMNREKIWQEL---AHWQRGSAsqfTDRALALVEQALWDLAGRALKLPVHKLLGG-YRDKVLAYGSTmCGDDLPgglS 152
Cdd:PRK15072 58 RDAHRIEDIWQYLyrgAYWRRGPV---TMSAIAAVDMALWDIKAKAAGMPLYQLLGGaSREGVMVYGHA-NGRDID---E 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 153 TPDEYGQFAEKlvkrGYKGIKLHTWMPPIS----FAPDPRMD------------------------VQACAAVREAVGPD 204
Cdd:PRK15072 131 LLDDVARHLEL----GYKAIRVQCGVPGLKttygVSKGKGLAyepatkgllpeeelwstekylrfvPKLFEAVRNKFGFD 206
|
250 260 270
....*....|....*....|....*....|....
gi 1499501876 205 VALMLDGYHWYSRTDALYIGRELQKLDFAWFEEP 238
Cdd:PRK15072 207 LHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDP 240
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
104-372 |
5.96e-21 |
|
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: 92.93 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 104 ALALVEQALWDLAGRALKLPVHKLLGGYRDKVLAYGStmcgDDLPGGLSTPDEygqfAEKLVKRGYKGIKLHtwmppISF 183
Cdd:cd03321 100 AAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDS----HGLDGAKLATER----AVTAAEEGFHAVKTK-----IGY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 184 aPDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPES 263
Cdd:cd03321 167 -PTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGEN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 264 IAGKYHSRASwVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNGAANLAVVGAISNCRWYER-----GLLH 338
Cdd:cd03321 246 WLGPEEMFKA-LSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVTPTAHWLEYvdwagAILE 324
|
250 260 270
....*....|....*....|....*....|....
gi 1499501876 339 PFLEYddvpaylntlvdpmdSDGFVHLSGQPGLG 372
Cdd:cd03321 325 PPLKF---------------EDGNAVIPDEPGNG 343
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
154-256 |
1.62e-19 |
|
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: 82.71 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 154 PDEYGQFAEKLVK-RGYKGIKLHTwmppisfAPDPRMDVQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDF 232
Cdd:smart00922 1 PEELAEAARRAVAeAGFRAVKVKV-------GGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGL 73
|
90 100
....*....|....*....|....
gi 1499501876 233 AWFEEPMMEDSAESYAWLAANLDI 256
Cdd:smart00922 74 EWIEEPVPPDDLEGLAELRRATPI 97
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
44-376 |
1.81e-18 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 86.32 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 44 IACDEGSEGFSFGSPELIRPHIIESFVKKVLIGQNPMNREKIWQELAHwqrgsASQFTDR------ALALVEQALWDLAG 117
Cdd:PRK15440 63 VEAENGQVGFAVSTAGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLN-----ATLYYGRkglvmnTISCVDLALWDLLG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 118 RALKLPVHKLLGG-YRDKVLAYGSTmcgddlpgglSTPDeygqFAEKLvkrGYKGIKLHTWMPPISFAPDPRMDVQACAA 196
Cdd:PRK15440 138 KVRGLPVYKLLGGaVRDELQFYATG----------ARPD----LAKEM---GFIGGKMPLHHGPADGDAGLRKNAAMVAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 197 VREAVGPDVALMLDGyhWYSrTDALYIGR---ELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLgpesIAGKYHSRAS 273
Cdd:PRK15440 201 MREKVGDDFWLMLDC--WMS-LDVNYATKlahACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMM----VTSGEHEATL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 274 W-----VTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNGAANLAVVGAISNCRWYERGLLHPflEYDDV-P 347
Cdd:PRK15440 274 QgfrtlLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYSHHFVITRTNSPFSEFLMMSP--DADTVvP 351
|
330 340 350
....*....|....*....|....*....|..
gi 1499501876 348 AYLNTLVD-PMDSDGFVHLSG--QPGLGEDIN 376
Cdd:PRK15440 352 QFDPILLDePVPVNGRIHKSVldKPGFGVELN 383
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
64-382 |
3.82e-16 |
|
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: 78.82 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 64 HIIESFVKKVLIGQNPMNREKIWQELAHWQRGSAsqftdrALALVEQALWDLAGRALKLPVHKLLGGYRDKVlaygstmc 143
Cdd:cd03317 61 HILKDYLLPLLLGREFSHPEEVSERLAPIKGNNM------AKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSI-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 144 gddlPGGLS-----TPDEYGQFAEKLVKRGYKGIKLHTwmppisfapDPRMDVQACAAVREAVgPDVALMLDGYHWYSRT 218
Cdd:cd03317 127 ----PVGVSigiqdDVEQLLKQIERYLEEGYKRIKLKI---------KPGWDVEPLKAVRERF-PDIPLMADANSAYTLA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 219 DALYIgRELQKLDFAWFEEPMMEDSAESYAWLAANLDIPVLGPESIAGKYHSRASwVTNKACDILRAGVAGVGGIGPCLK 298
Cdd:cd03317 193 DIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAEDARKA-IELGACKIINIKPGRVGGLTEALK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 299 VAHLAESFGMGCEVHG---NG---AANLAVV--------GAIS-NCRWYERGLLHPFLEYDdvpaylntlvdpmdsDGFV 363
Cdd:cd03317 271 IHDLCQEHGIPVWCGGmleSGigrAHNVALAslpnftypGDISaSSRYFEEDIITPPFELE---------------NGII 335
|
330
....*....|....*....
gi 1499501876 364 HLSGQPGLGEDINFSYIET 382
Cdd:cd03317 336 SVPTGPGIGVTVDREALKK 354
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
36-129 |
1.21e-13 |
|
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: 66.73 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 36 PVKMAM----------LRIACDEG----SEGFSFGSPELIRPHIIESFVKKVLIGQNPMNREKIWQELAHWQRGSASqft 101
Cdd:pfam02746 15 PIQMAFgtvqqqslviVRIETSEGvvgiGEATSYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALGNMS--- 91
|
90 100
....*....|....*....|....*...
gi 1499501876 102 drALALVEQALWDLAGRALKLPVHKLLG 129
Cdd:pfam02746 92 --AKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
6-258 |
9.55e-07 |
|
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: 50.42 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 6 KITSVSVDVFSFPSRRAVDSAGHAHPGEEKPVkmAMLRIACDE-GSEG----FSFG--------SPELIRPHIIESFVKK 72
Cdd:cd03324 2 KITALEVRDVRFPTSLELDGSDAMNPDPDYSA--AYVVLRTDAaGLKGhgltFTIGrgneivcaAIEALAHLVVGRDLES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 73 VLigqnpMNREKIWQELAH-----WQrGSASQFTDRALALVEQALWDLAGRALKLPVHKLLGG-------------YRDK 134
Cdd:cd03324 80 IV-----ADMGKFWRRLTSdsqlrWI-GPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDmtpeelvscidfrYITD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 135 VL-----------------AYGSTMCGDDLPGGLSTPDEYGQFAEKL-------VKRGYKGIKLHTwmppisfAPDPRMD 190
Cdd:cd03324 154 ALtpeealeilrrgqpgkaAREADLLAEGYPAYTTSAGWLGYSDEKLrrlckeaLAQGFTHFKLKV-------GADLEDD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1499501876 191 VQACAAVREAVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEPMMEDSAESYAWLA---ANLDIPV 258
Cdd:cd03324 227 IRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRkalAPLPIGV 297
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
101-316 |
2.03e-06 |
|
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: 49.24 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 101 TDRALALVEQALWDLAGRALKLPVHKLLGGY-RDKV--LAY----GSTMCGDdlPGGLSTPDEYGQ---------FAEKL 164
Cdd:cd03323 102 TVHVVTAFEVALLDLLGQALGVPVADLLGGGqRDSVpfLAYlfykGDRHKTD--LPYPWFRDRWGEaltpegvvrLARAA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 165 VKR-GYKGIKLHTWMppisFAPDprMDVQACAAVREAVgPDVALMLDGYHWYSRTDALYIGRELQKLdFAWFEEP----- 238
Cdd:cd03323 180 IDRyGFKSFKLKGGV----LPGE--EEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDPcggre 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499501876 239 -MMEDSAESYAWLAANLdipvlgpesIAGKYHSRASWVTNKACDILRAGVAGVGGIGPCLKVAHLAESFGMGCEVHGNG 316
Cdd:cd03323 252 gMAEFRRATGLPLATNM---------IVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNN 321
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|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
102-238 |
1.25e-05 |
|
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: 47.00 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 102 DRALAL--VEQALWDLAGRALKLPVHKLL------GGYRDKVLAY---GSTMCGDDLpGGLStpDEYGQFAEklvkRGYK 170
Cdd:cd03326 105 ERAVAVgaLDMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVYaagGYYYPGDDL-GRLR--DEMRRYLD----RGYT 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499501876 171 GIKLHtwmppISFAP--DPRMDVQACAAVreaVGPDVALMLDGYHWYSRTDALYIGRELQKLDFAWFEEP 238
Cdd:cd03326 178 VVKIK-----IGGAPldEDLRRIEAALDV---LGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP 239
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