|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
43-378 |
3.96e-163 |
|
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: 460.65 E-value: 3.96e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 43 FFSWLVVEIETDEGHIGIGNAGLCPdVTKKIIDSKLASLLIGENPLNTEYLFEKMYRSTVAYGRKGAVIAAISALDIALW 122
Cdd:cd03327 8 RVGWLFVEIETDDGTVGYANTTGGP-VACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGRKGIAMAAISAVDLALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 123 DIKGLAFNQPVFMLLGGRTKPQIETYYSRLYTRDLDSLQAEAAHYKAEGFTGMKLRCGYPLTDGLTGLKKNVEMVRVVRE 202
Cdd:cd03327 87 DLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEYLKEGYRGMKMRFGYGPSDGHAGLRKNVELVRAIRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 203 TVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQTGAL 282
Cdd:cd03327 167 AVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 283 DIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQMHNLHVVMSSFACPMAEYFPQTEIEVGNEMFWYIFDGEAIAENG 362
Cdd:cd03327 247 DILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQIYNYHFIMSEPNSPFAEYLPNSPDEVGNPLFYYIFLNEPVPVNG 326
|
330
....*....|....*.
gi 1823154876 363 KLQLDDsKPGMGLTLK 378
Cdd:cd03327 327 YFDLSD-KPGFGLELN 341
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
40-376 |
3.07e-111 |
|
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: 329.57 E-value: 3.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 40 AFRFFSWLVVEIETDEGHIGIGNA--GLCPDVTKKIIDSKLASLLIGENPLNTEYLFEKMYRSTVAYGRKGAVIAAISAL 117
Cdd:cd03316 20 AVTWRNLVLVRVTTDDGITGWGEAypGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLYRRLFWRGRGGVAMAAISAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 118 DIALWDIKGLAFNQPVFMLLGGRTKPQIETYYSRLYT-RDLDSLQAEAAHYKAEGFTGMKLRCGYPLTDGLtGLKKNVEM 196
Cdd:cd03316 100 DIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYdDSPEELAEEAKRAVAEGFTAVKLKVGGPDSGGE-DLREDLAR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 197 VRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDL 276
Cdd:cd03316 179 VRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 277 LQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG-----GQMHNLHVVMSSFACPMAEYFPQteievGNEMFWY 351
Cdd:cd03316 259 LEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGaggpiGLAASLHLAAALPNFGILEYHLD-----DLPLRED 333
|
330 340
....*....|....*....|....*
gi 1823154876 352 IFDGEAIAENGKLQLDDsKPGMGLT 376
Cdd:cd03316 334 LFKNPPEIEDGYVTVPD-RPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-385 |
2.37e-91 |
|
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: 278.63 E-value: 2.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 1 MKIRAVRTKLYQWngPVKTGDTIfatplsplhfqqdSQAAFRFFSWLVVEIETDEGHIGIGNA---GLCPDVTKKIIDSK 77
Cdd:COG4948 1 MKITDIEVYPVRL--PLKRPFTI-------------SRGTRTERDVVLVRVETDDGITGWGEAvpgGTGAEAVAAALEEA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 78 LASLLIGENPLNTEYLFEKMYRSTvaygrkGAVIAAISALDIALWDIKGLAFNQPVFMLLGGRTKPQIETYYSrLYTRDL 157
Cdd:COG4948 66 LAPLLIGRDPLDIEALWQRLYRAL------PGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYAT-LGIDTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 158 DSLQAEAAHYKAEGFTGMKLRCGYPltdgltGLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRW 237
Cdd:COG4948 139 EEMAEEAREAVARGFRALKLKVGGP------DPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 238 VEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG- 316
Cdd:COG4948 213 IEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCm 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823154876 317 -----GQMHNLHVVMSSFACPMAEYfpqteieVGNEMFWY-IFDGEAIAENGKLQLDDsKPGMGLTLKTEGLEQF 385
Cdd:COG4948 293 lesgiGLAAALHLAAALPNFDIVEL-------DGPLLLADdLVEDPLRIEDGYLTVPD-GPGLGVELDEDALARY 359
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
25-380 |
2.02e-76 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 241.56 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 25 ATPLSPLHFQQDSQAAF--RFFSWLVVEIETDEGHIGIG--NAGlcpDVTKKIIDSKLASLLIGENPLNTEYLFEKMYRS 100
Cdd:PRK15440 35 ATPMSKYPEYRQSRQSFgiNVLGTLVVEVEAENGQVGFAvsTAG---EMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 101 TVAYGRKGAVIAAISALDIALWDIKGLAFNQPVFMLLGGRTKPQIeTYYSRLYTRDLDslqaeaahyKAEGFTGMKLRCG 180
Cdd:PRK15440 112 TLYYGRKGLVMNTISCVDLALWDLLGKVRGLPVYKLLGGAVRDEL-QFYATGARPDLA---------KEMGFIGGKMPLH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 181 YPLTDGLTGLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQytDIP 260
Cdd:PRK15440 182 HGPADGDAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKR--NAP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 261 ----LSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQMHNLHVVMSSFACPMAEY 336
Cdd:PRK15440 260 agmmVTSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYSHHFVITRTNSPFSEF 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1823154876 337 F---PQTEIEVgnEMFWYIFDGEAIAENGKLQLDDS-KPGMGLTLKTE 380
Cdd:PRK15440 340 LmmsPDADTVV--PQFDPILLDEPVPVNGRIHKSVLdKPGFGVELNRD 385
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
46-377 |
1.48e-67 |
|
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: 217.58 E-value: 1.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 46 WLVVEIETDEGHIGIGNA---GLCPDVTKKIIDskLASLLIGENPLNTEYLFEKMYRStvAYGRKGAVI-AAISALDIAL 121
Cdd:cd03325 14 WLFVKIETDEGVVGWGEPtveGKARTVEAAVQE--LEDYLIGKDPMNIEHHWQVMYRG--GFYRGGPVLmSAISGIDQAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 122 WDIKGLAFNQPVFMLLGGRTKPQIETYYsRLYTRDLDSLQAEAAHYKAEGFTGMKLRCGYPL--TDGLTGLKKNVEMVRV 199
Cdd:cd03325 90 WDIKGKVLGVPVHQLLGGQVRDRVRVYS-WIGGDRPSDVAEAARARREAGFTAVKMNATEELqwIDTSKKVDAAVERVAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 200 VRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQT 279
Cdd:cd03325 169 LREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLED 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 280 GALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG-----GQMHNLHVVMSSFACPMAEYFPQTEIEVGNEMFWYIFD 354
Cdd:cd03325 249 GAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCplgpiALAASLHVDASTPNFLIQEQSLGIHYNEGDDLLDYLVD 328
|
330 340
....*....|....*....|....
gi 1823154876 355 GEAIA-ENGKLQLDDsKPGMGLTL 377
Cdd:cd03325 329 PEVFDmENGYVKLPT-GPGLGIEI 351
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
161-380 |
5.10e-62 |
|
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: 198.56 E-value: 5.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 161 QAEAAhYKAEGFTGMKLRCGYPltdgltGLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEE 240
Cdd:pfam13378 5 EARRA-VEARGFRAFKLKVGGP------DPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 241 LMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQMH 320
Cdd:pfam13378 78 PVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1823154876 321 -----NLHVVMSSFACPMAEYFpqteiEVGNEMFWYIFDGEAIAENGKLQLDDsKPGMGLTLKTE 380
Cdd:pfam13378 158 iglaaSLHLAAAVPNLLIQEYF-----LDPLLLEDDLLTEPLEVEDGRVAVPD-GPGLGVELDED 216
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
46-315 |
4.43e-56 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 188.57 E-value: 4.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 46 WLVVEIETDEGHIGIGNAglcpdvtkkIIDSK----------LASLLIGENPLNTEYLFEKMYRStvAYGRKGAVI-AAI 114
Cdd:PRK14017 15 WLFLKIETDEGIVGWGEP---------VVEGRartveaavheLADYLIGKDPRRIEDHWQVMYRG--GFYRGGPILmSAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 115 SALDIALWDIKGLAFNQPVFMLLGGRTKPQIETYysRLYTRDLDSLQAEAAHYKAE-GFTGMKLRCGYPLT--DGLTGLK 191
Cdd:PRK14017 84 AGIDQALWDIKGKALGVPVHELLGGLVRDRIRVY--SWIGGDRPADVAEAARARVErGFTAVKMNGTEELQyiDSPRKVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 192 KNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRY 271
Cdd:PRK14017 162 AAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1823154876 272 GFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPH 315
Cdd:PRK14017 242 DFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPH 285
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
47-337 |
4.34e-47 |
|
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: 164.49 E-value: 4.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 47 LVVEIETDEGHIG---IGNAGLCPDvtkkIIDSKLASLLIGENPLNTEYLFEKMYRStvaygRKGAVIAAISALDIALWD 123
Cdd:cd03329 35 ALLTIETDEGAKGhafGGRPVTDPA----LVDRFLKKVLIGQDPLDRERLWQDLWRL-----QRGLTDRGLGLVDIALWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 124 IKGLAFNQPVFMLLGGrTKPQIETYYSRLYTRD---LDSLQA---EAAHYKAEGFTGMKLrcgYPLTDGLtgLKKNVEMV 197
Cdd:cd03329 106 LAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDlegLESPEAyadFAEECKALGYRAIKL---HPWGPGV--VRRDLKAC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 198 RVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHeyTRYGFH--- 274
Cdd:cd03329 180 LAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEH--SRGALEsra 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1823154876 275 DLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQMHNLHVVMssfACPMAEYF 337
Cdd:cd03329 258 DWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLHVIA---AIRNTRYY 317
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
48-385 |
8.07e-44 |
|
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: 155.68 E-value: 8.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 48 VVEIETDEGHIGIGNAGLC--PDVTKKIIDSKLASLLIGENPLNTEYLFEKMYRStvAYGRKGAVI-AAISALDIALWDI 124
Cdd:cd03322 18 TLKITTDQGVTGLGDATLNgrELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRG--AYWRRGPVTmNAIAAVDMALWDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 125 KGLAFNQPVFMLLGGRTKPQIETYySRLYTRDLDSLQAEAAHYKAEGFTGMKLRCgypltdgltglkknVEMVRVVRETV 204
Cdd:cd03322 96 KGKAAGMPLYQLLGGKSRDGIMVY-SHASGRDIPELLEAVERHLAQGYRAIRVQL--------------PKLFEAVREKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 205 GDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGE-----HEYTrygfhDLLQT 279
Cdd:cd03322 161 GFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEvfnsiWDWQ-----NLIQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 280 GALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG-------GQMHNLHVVMSSFACPMAEYFPQTE--IEVgnemfw 350
Cdd:cd03322 236 RLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGptdlspvGMAAALHLDLWVPNFGIQEYMRHAEetLEV------ 309
|
330 340 350
....*....|....*....|....*....|....*
gi 1823154876 351 yiFDGEAIAENGKLQLDDsKPGMGLTLKTEGLEQF 385
Cdd:cd03322 310 --FPHSVRFEDGYLHPGE-EPGLGVEIDEKAAAKF 341
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
48-378 |
1.62e-40 |
|
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: 146.79 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 48 VVEIETDeGHIGIGNAgLCPDVTKKIIDSKLASLLIGENPLNTEYLFEKMYRSTVAYGRKGAVIAAISALDIALWDIKGL 127
Cdd:cd03328 32 LVEVRAG-GRTGLGYT-YADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAMAISAVDIALWDLKAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 128 AFNQPVFMLLgGRTKPQIETYYSRLYTR-DLDSLQAEAAHYKAEGFTGMKLRCGypltdglTGLKKNVEMVRVVRETVGD 206
Cdd:cd03328 110 LLGLPLARLL-GRAHDSVPVYGSGGFTSyDDDRLREQLSGWVAQGIPRVKMKIG-------RDPRRDPDRVAAARRAIGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 207 DVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYT--DIPLSGGEHEYTRYGFHDLLQTGALDI 284
Cdd:cd03328 182 DAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGpaGMDIAAGEYAYTLAYFRRLLEAHAVDV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 285 FQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQMHNLHVVMSSFACPMAEYF-PQTEIEvgnEMFwyiFDGEAIAENGK 363
Cdd:cd03328 262 LQADVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVPRLRHLEWFhDHVRIE---RML---FDGAPDPSGGA 335
|
330
....*....|....*
gi 1823154876 364 LQLDDSKPGMGLTLK 378
Cdd:cd03328 336 LRPDLSRPGLGLELR 350
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
30-336 |
4.16e-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: 133.99 E-value: 4.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 30 PLHFQQDSQAAFR---FFSWLVVEIETDEGHIGIGNAglcpdvtkkiidsklaslligenplnteylfekmyrstvaygr 106
Cdd:cd00308 7 RLPTSRPFYLAGGtadTNDTVLVKLTTDSGVVGWGEV------------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 107 kgaviaaISALDIALWDIKGLAFNQPVFMLLGGRTKPQIETYYSrlytrdldslqaeaahykaegftgmklrcgypltdg 186
Cdd:cd00308 44 -------ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS------------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 187 ltglkknVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEH 266
Cdd:cd00308 81 -------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADES 153
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823154876 267 EYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHGGQM------HNLHVVMSSFACPMAEY 336
Cdd:cd00308 154 VTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEssigtaAALHLAAALPNDRAIET 229
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
49-377 |
2.59e-32 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 125.41 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 49 VEIETDEGHIGIGNAGLCP---DVTKKIIDsKLASLLIGENPLNTEYLFEKMYRStvAYGRKGAV-IAAISALDIALWDI 124
Cdd:PRK15072 20 LKITTDDGVTGLGDATLNGrelAVASYLQD-HVCPLLIGRDAHRIEDIWQYLYRG--AYWRRGPVtMSAIAAVDMALWDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 125 KGLAFNQPVFMLLGGRTKPQIETyYSRLYTRDLDSLQAEAAHYKAEGFTGMKLRCGYPLTDGLTGLKKN----------- 193
Cdd:PRK15072 97 KAKAAGMPLYQLLGGASREGVMV-YGHANGRDIDELLDDVARHLELGYKAIRVQCGVPGLKTTYGVSKGkglayepatkg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 194 -----------------VEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMlPDEIQNFAKL-KQ 255
Cdd:PRK15072 176 llpeeelwstekylrfvPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDPT-PAENQEAFRLiRQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 256 YTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG-------GQMHNLHVVMSS 328
Cdd:PRK15072 255 HTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGptdlspvCMAAALHFDLWV 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1823154876 329 FACPMAEYFPQTEIEvgNEMF--WYIFdgeaiaENGKLQLDDsKPGMGLTL 377
Cdd:PRK15072 335 PNFGIQEYMGHSEET--LEVFphSYTF------EDGYLHPGD-APGLGVDF 376
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
105-332 |
1.08e-28 |
|
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: 112.82 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 105 GRKGAVIAAISALDIALWDIKGLAFNQPVFmLLGGRTKPQIETYYSrLYTRDLDSLQAEAAHYKAEGFTGMKLRCGYPLt 184
Cdd:cd03315 36 GLVGWAEATKAAVDMALWDLWGKRLGVPVY-LLLGGYRDRVRVAHM-LGLGEPAEVAEEARRALEAGFRTFKLKVGRDP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 185 dgltglKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGG 264
Cdd:cd03315 113 ------ARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMAD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1823154876 265 EHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIPHG---GQMHNLHVVMSSFACP 332
Cdd:cd03315 187 ESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSmieSGLGTLANAHLAAALR 257
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-385 |
1.33e-28 |
|
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: 114.50 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 1 MKIRAVRTKLYQ--WNGPVKTGDTIFATplSPLhfqqdsqaafrffswLVVEIETDEGHIG------IGNAGLCPdvTKK 72
Cdd:cd03321 1 VLITGLRARAVNvpMQYPVHTSVGTVAT--APL---------------VLIDLATDEGVTGhsylftYTPAALKS--LKQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 73 IIDSkLASLLIGEN--PLNTEYLFEKMYRstvAYGRKGAVIAAISALDIALWDIKGLAFNQPVFMLLGGRTKPqIETYYS 150
Cdd:cd03321 62 LLDD-MAALLVGEPlaPAELERALAKRFR---LLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRP-VQAYDS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 151 RLYtrDLDSLQAEAAHYKA-EGFTGMKLRCGYPLtdgltgLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKA 229
Cdd:cd03321 137 HGL--DGAKLATERAVTAAeEGFHAVKTKIGYPT------ADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 230 LEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHG 309
Cdd:cd03321 209 LDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAG 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823154876 310 VEVIPHGGQMHNLHVVMSSFACPMAEYfpqteievgneMFWY--IFDGEAIAENGKLQLDDsKPGMGLTLKTEGLEQF 385
Cdd:cd03321 289 IPMSSHLFQEISAHLLAVTPTAHWLEY-----------VDWAgaILEPPLKFEDGNAVIPD-EPGNGIIWREKAVRKY 354
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
47-312 |
1.72e-25 |
|
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: 104.96 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 47 LVVEIETDeGHIGIGNAGLCPDVTKKIIDSKLASL------LIGENPLNT---EYLFEKMYRSTvaygrkgaviAAISAL 117
Cdd:cd03319 28 VIVEIELD-GITGYGEAAPTPRVTGETVESVLAALksvrpaLIGGDPRLEkllEALQELLPGNG----------AARAAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 118 DIALWDIKGLAFNQPVFMLLGGRTKPQIETYysrlYTRDLDSL---QAEAAHYKAEGFTGMKLRCGypltdglTGLKKNV 194
Cdd:cd03319 97 DIALWDLEAKLLGLPLYQLWGGGAPRPLETD----YTISIDTPeamAAAAKKAAKRGFPLLKIKLG-------GDLEDDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 195 EMVRVVRETVGdDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEHEYTRYGFH 274
Cdd:cd03319 166 ERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1823154876 275 DLLQTGALDIFqfdtN----RVGGFTEAQKICNMALVHGVEV 312
Cdd:cd03319 245 RLAGGGAYDGI----NiklmKTGGLTEALRIADLARAAGLKV 282
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
49-317 |
2.16e-23 |
|
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: 100.88 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 49 VEIETD----EGH-----IGIGNaglcpDVTKKIIDSkLASLLIGENPLNTEYLFEKMYRSTVAYGR-------KGAVIA 112
Cdd:cd03324 36 VVLRTDaaglKGHgltftIGRGN-----EIVCAAIEA-LAHLVVGRDLESIVADMGKFWRRLTSDSQlrwigpeKGVIHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 113 AISALDIALWDIKGLAFNQPVFMLLGGRTKPQIE-----TYYSRLYTRD--LDSLQ-------AEAAHYKAEGF------ 172
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVscidfRYITDALTPEeaLEILRrgqpgkaAREADLLAEGYpaytts 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 173 ------TGMKLR--CGYPLTDGLTGLKKNV--------EMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLR 236
Cdd:cd03324 190 agwlgySDEKLRrlCKEALAQGFTHFKLKVgadleddiRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 237 WVEELMLPDEIQNFAKLKQ---YTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVI 313
Cdd:cd03324 270 WIEEPTSPDDILGHAAIRKalaPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVC 349
|
....
gi 1823154876 314 PHGG 317
Cdd:cd03324 350 PHAG 353
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
112-380 |
4.57e-21 |
|
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: 93.61 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 112 AAISALDIALWDIKGLAFNQPVFMLLG---GRTK--PQIETYYSRLY---TRDLDSLQAEAAHYKAEGFTGMKLRCGYpl 183
Cdd:cd03326 108 VAVGALDMAVWDAVAKIAGLPLYRLLArryGRGQadPRVPVYAAGGYyypGDDLGRLRDEMRRYLDRGYTVVKIKIGG-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 184 tdglTGLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSG 263
Cdd:cd03326 186 ----APLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIAT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 264 GEHEYTRYGFHDLLQTGAL----DIFQFDTNRVGGFTEAQKICNMALVHGVE---VIPHGGQMHNLHVVmSSFACPMAEY 336
Cdd:cd03326 262 GENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGWSrrrFFPHGGHLMSLHIA-AGLGLGGNES 340
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1823154876 337 FPQTEIEVGNemfwyiFDGEAIAENGKLQLDDSkPGMGLTLKTE 380
Cdd:cd03326 341 YPDVFQPFGG------FADGCKVENGYVRLPDA-PGIGFEGKAE 377
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
21-138 |
2.46e-19 |
|
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: 82.90 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 21 DTIFATPLSPLHFQQDSQAAFRFFSWLVVEIETDEGHIGIGNA---GLCPDVTKKIIDSKLASLLIGENPLNTEYLFEKM 97
Cdd:pfam02746 3 EVFVVDVGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEAtsyGGRAETIKAILDDHLAPLLIGRDAANISDLWQLM 82
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1823154876 98 YRStvAYGrkgaVIAAISALDIALWDIKGLAFNQPVFMLLG 138
Cdd:pfam02746 83 YRA--ALG----NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
22-384 |
1.00e-18 |
|
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: 86.60 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 22 TIFATPLSPLHFQ----QDSQaafrffSWLVVEIETDEGHIGIGNA---------GLCPDVTKKIIDSKLASLLIGENPL 88
Cdd:cd03318 8 TIVDLPTRRPHQFagttMHTQ------SLVLVRLTTSDGVVGIGEAttpggpawgGESPETIKAIIDRYLAPLLIGRDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 89 NTEYLFEKMYRSTVAYgrkgavIAAISALDIALWDIKGLAFNQPVFMLLGGRTKPQIETYYSrLYTRDLDSLQAEAAHYK 168
Cdd:cd03318 82 NIGAAMALLDRAVAGN------LFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWT-LASGDTERDIAEAEEML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 169 AEGFTG-MKLRCGY-PLTDgltglkkNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVEELMLPDE 246
Cdd:cd03318 155 EAGRHRrFKLKMGArPPAD-------DLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPREN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 247 IQNFAKLKQYTDIPLSGGEHEYTRYGFHDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEviPHGGQMHNlHVVM 326
Cdd:cd03318 228 LDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIA--LYGGTMLE-SSIG 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1823154876 327 SSFACPMAEYFPQteIEVGNEMF--WYIFDG---EAIA-ENGKLQLDDSkPGMGLTLKTEGLEQ 384
Cdd:cd03318 305 TAASAHLFATLPS--LPFGCELFgpLLLAEDlleEPLAyRDGELHVPTG-PGLGVRLDEDKVRR 365
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
160-259 |
3.11e-18 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 79.25 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 160 LQAEAAHYKAEGFTGMKLRCGYPLTDgltglkkNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRWVE 239
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGGGPLE-------DLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIE 77
|
90 100
....*....|....*....|
gi 1823154876 240 ELMLPDEIQNFAKLKQYTDI 259
Cdd:smart00922 78 EPVPPDDLEGLAELRRATPI 97
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
47-383 |
1.07e-08 |
|
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: 56.47 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 47 LVVEIETDEGHIGIGN--AGLCPDVT-------KKIIDSKLASLLIGEnPLNTEYLFEKMYRSTvaygrKGAVIAAiSAL 117
Cdd:cd03317 27 LIVELTDEEGITGYGEvvAFEGPFYTeetnataWHILKDYLLPLLLGR-EFSHPEEVSERLAPI-----KGNNMAK-AGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 118 DIALWDIKGLAFNQPVFMLLGGrTKPQIETYYSRLYTRDLDSLQAEAAHYKAEGFTGMKLRcgypltdgltgLK--KNVE 195
Cdd:cd03317 100 EMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQLLKQIERYLEEGYKRIKLK-----------IKpgWDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 196 MVRVVRETVGDdVDIMLEAYMGFNFPYAKQLlKALEPYNLRWVEELMLPDEIQNFAKLKQYTDIPLSGGEH----EYTRy 271
Cdd:cd03317 168 PLKAVRERFPD-IPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESiqsaEDAR- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 272 gfhDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEVIpHGGQM-------HNLHVV-MSSFACP--MAeyfpqte 341
Cdd:cd03317 245 ---KAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVW-CGGMLesgigraHNVALAsLPNFTYPgdIS------- 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1823154876 342 ievGNEMFWY--IFDGEAIAENGKLQLdDSKPGMGLTLKTEGLE 383
Cdd:cd03317 314 ---ASSRYFEedIITPPFELENGIISV-PTGPGIGVTVDREALK 353
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
43-180 |
1.85e-05 |
|
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: 46.55 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 43 FFSWLVVEIETDEGHIGIGNaglCPDVTKKIidSKL----ASLLIGENPLNTEYLFEKMYRSTVAYGRKG---------A 109
Cdd:cd03323 27 FFTRNIVELTDDNGNTGVGE---SPGGAEAL--EALleaaRSLVGGDVFGAYLAVLESVRVAFADRDAGGrglqtfdlrT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 110 VIAAISALDIALWDIKGLAFNQPVFMLLGGRTKPQIET--YYSRLYTRDLDSL--------------------QAEAAhY 167
Cdd:cd03323 102 TVHVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPFlaYLFYKGDRHKTDLpypwfrdrwgealtpegvvrLARAA-I 180
|
170
....*....|...
gi 1823154876 168 KAEGFTGMKLRCG 180
Cdd:cd03323 181 DRYGFKSFKLKGG 193
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
158-313 |
3.43e-05 |
|
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: 44.94 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 158 DSLQAEAAHYKAEGFTGMKLRCGypltdgLTGLKKNVEMVRVVRETVGDDVDIMLEAYMGFNFPYAKQLLKALEPYNLRW 237
Cdd:cd03320 84 AAALGEAKAAYGGGYRTVKLKVG------ATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823154876 238 VEELMLPDEIQNFAKLKQYTDIPL-----SGGEHEytrygfhDLLQTGALDIFQFDTNRVGGFTEAQKICNMALVHGVEV 312
Cdd:cd03320 158 IEQPLPPDDLAELRRLAAGVPIALdeslrRLDDPL-------ALAAAGALGALVLKPALLGGPRALLELAEEARARGIPA 230
|
.
gi 1823154876 313 I 313
Cdd:cd03320 231 V 231
|
|
| |
