|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
1-401 |
0e+00 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 790.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 1 MTLPKIKHVRAWFIGGataekgaGGGDYHDQGGNHWIDDHIATPMSKYRDYEQSRQSFGINVLGTLIVEVEAENGQTGFA 80
Cdd:PRK15440 1 MTLPKIKHVRAWFVGG-------GGADYHDQGANHWIDDHIATPMSKYPEYRQSRQSFGINVLGTLVVEVEAENGQVGFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 81 VSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGATMYYsGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAV 160
Cdd:PRK15440 74 VSTAGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYY-GRKGLVMNTISCVDLALWDLLGKVRGLPVYKLLGGAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 161 RDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACA 240
Cdd:PRK15440 153 RDELQFYATGARPDLAKEMGFIGGKMPLHHGPADGDAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 241 PFNLKWIEECLPPQQYEGYRELKRNAPAGMMVTSGEHHGTLQSFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSRG 319
Cdd:PRK15440 233 PYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGEHEATLQGFRTLLEMGcIDIIQPDVGWCGGLTELVKIAALAKARG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 320 QLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTLRPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCHLKRPY 399
Cdd:PRK15440 313 QLVVPHGSSVYSHHFVITRTNSPFSEFLMMSPDADTVVPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPY 392
|
..
gi 1478601324 400 SH 401
Cdd:PRK15440 393 SH 394
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
64-390 |
1.70e-179 |
|
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: 502.63 E-value: 1.70e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 64 GTLIVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGATMYYsGSGGLVMNTISCVDLALWDL 143
Cdd:cd03327 10 GWLFVEIETDDGTVGYANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAY-GRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 144 FGKVVGLPVYKLLGGAVRDEIQFYATGA-------RPDLAKEM---GFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKC 213
Cdd:cd03327 89 LGKIRGEPVYKLLGGRTRDKIPAYASGLyptdldeLPDEAKEYlkeGYRGMKMRFGYGPSDGHAGLRKNVELVRAIREAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 214 GPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNapAGMMVTSGEHHGTLQSFRTLAE-TGI 292
Cdd:cd03327 169 GYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKA--TGIPISTGEHEYTVYGFKRLLEgRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 293 DIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTLrPQFDPILLDEPVPVN 372
Cdd:cd03327 247 DILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQIYNYHFIMSEPNSPFAEYLPNSPDEVGN-PLFYYIFLNEPVPVN 325
|
330
....*....|....*...
gi 1478601324 373 GRIHKSvlDKPGFGVELN 390
Cdd:cd03327 326 GYFDLS--DKPGFGLELN 341
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
66-388 |
2.37e-82 |
|
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: 256.00 E-value: 2.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 66 LIVEVEAENGQTGFAVSTAGEMGCF---IVEKHLNRFIEGKCVSDIKLIHDQMLGATmYYSGSGGLVMNTISCVDLALWD 142
Cdd:cd03316 27 VLVRVTTDDGITGWGEAYPGGRPSAvaaAIEDLLAPLLIGRDPLDIERLWEKLYRRL-FWRGRGGVAMAAISAVDIALWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 143 LFGKVVGLPVYKLLGGAVRDEIQFYATGARPDL-----------AKEMGFIGGKMptHWGPHD-GDAGIRKDAAMVADMR 210
Cdd:cd03316 106 IKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDspeelaeeakrAVAEGFTAVKL--KVGGPDsGGEDLREDLARVRAVR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 211 EKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPagMMVTSGEHHGTLQSFRTLAET 290
Cdd:cd03316 184 EAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQATS--VPIAAGENLYTRWEFRDLLEA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 291 G-IDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHG-----SSVYSHHAVITFTNTPFSEFLMTSPdcstlrPQFDPIL 364
Cdd:cd03316 262 GaVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGaggpiGLAASLHLAAALPNFGILEYHLDDL------PLREDLF 335
|
330 340
....*....|....*....|....
gi 1478601324 365 LDEPVPVNGRIHksVLDKPGFGVE 388
Cdd:cd03316 336 KNPPEIEDGYVT--VPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
65-392 |
3.01e-62 |
|
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: 204.29 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 65 TLIVEVEAENGQTGFavstaGEMGCF---------IVEKHLNRFIEGKCVSDIKLIHDQMlgatmyYSGSGGlVMNTISC 135
Cdd:COG4948 31 VVLVRVETDDGITGW-----GEAVPGgtgaeavaaALEEALAPLLIGRDPLDIEALWQRL------YRALPG-NPAAKAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 136 VDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDL---------AKEMGF----IGGkmpthwgphdGDAGIRKD 202
Cdd:COG4948 99 VDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPeemaeeareAVARGFralkLKV----------GGPDPEED 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 203 AAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVtsGEHHGTLQ 282
Cdd:COG4948 169 VERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAA--DESLTSRA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 283 SFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHG---SSV---YSHHAVITFTNTPFSEFlmtspdcST 355
Cdd:COG4948 247 DFRRLIEAGaVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCmleSGIglaAALHLAAALPNFDIVEL-------DG 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 1478601324 356 LRPQFDPILLDEPVPVNGRIHksVLDKPGFGVELNRD 392
Cdd:COG4948 320 PLLLADDLVEDPLRIEDGYLT--VPDGPGLGVELDED 354
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
195-392 |
2.69e-41 |
|
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: 145.02 E-value: 2.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 195 GDAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVts 274
Cdd:pfam13378 23 GGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIAT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 275 GEHHGTLQSFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPH-----GSSVYSHHAVITFTNTPFSEFLM 348
Cdd:pfam13378 101 GESLYSREDFRRLLEAGaVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHsgggpIGLAASLHLAAAVPNLLIQEYFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1478601324 349 TSPdcstlrPQFDPILLDEPVPVNGRIHksVLDKPGFGVELNRD 392
Cdd:pfam13378 181 DPL------LLEDDLLTEPLEVEDGRVA--VPDGPGLGVELDED 216
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
96-390 |
7.31e-36 |
|
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: 134.38 E-value: 7.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 96 LNRFIEGKCVSDIKLiHDQMLGATMYYSGsGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFY--ATGARP 173
Cdd:cd03325 47 LEDYLIGKDPMNIEH-HWQVMYRGGFYRG-GPVLMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYswIGGDRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 174 D-------LAKEMGFIGGKM----PTHWgpHDGDAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPF 242
Cdd:cd03325 125 SdvaeaarARREAGFTAVKMnateELQW--IDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 243 NLKWIEECLPPQQYEGYRELKR--NAPagmmVTSGEHHGTLQSFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSRG 319
Cdd:cd03325 203 RLLFIEEPVLPENVEALAEIAArtTIP----IATGERLFSRWDFKELLEDGaVDIIQPDISHAGGITELKKIAAMAEAYD 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478601324 320 QLVVPHG-----SSVYSHHAVITFTNTPFSEflMTSPDCSTLRPQFDPILLDEPVP--VNGRIhkSVLDKPGFGVELN 390
Cdd:cd03325 279 VALAPHCplgpiALAASLHVDASTPNFLIQE--QSLGIHYNEGDDLLDYLVDPEVFdmENGYV--KLPTGPGLGIEID 352
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
65-389 |
4.44e-34 |
|
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: 129.84 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 65 TLI-VEVEAeNGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGAtMYYSGSGGLVMNTISCVDLALWDL 143
Cdd:cd03328 29 TLVlVEVRA-GGRTGLGYTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRA-VRNAGRPGVAAMAISAVDIALWDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 144 FGKVVGLPVYKLLGgAVRDEIQFYATG---ARPD----------LAKEMGFIGGKMPTHWgphdgdagiRKDAAMVADMR 210
Cdd:cd03328 107 KARLLGLPLARLLG-RAHDSVPVYGSGgftSYDDdrlreqlsgwVAQGIPRVKMKIGRDP---------RRDPDRVAAAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 211 EKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVTSGEHHGTLQSFRTLAET 290
Cdd:cd03328 177 RAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAGMDIAAGEYAYTLAYFRRLLEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 291 G-IDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTspdcstlRPQFDPILLD-EP 368
Cdd:cd03328 257 HaVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVPRLRHLEWFHD-------HVRIERMLFDgAP 329
|
330 340
....*....|....*....|.
gi 1478601324 369 VPVNGRIHKSvLDKPGFGVEL 389
Cdd:cd03328 330 DPSGGALRPD-LSRPGLGLEL 349
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
41-392 |
1.14e-33 |
|
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: 129.05 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 41 IATPMSKYRDYEQSRQSFGINVLGTLIVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGAtm 120
Cdd:cd03329 10 FEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQDLWRL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 121 yysgSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGaVRDEIQFYATGARPDLA----------------KEMGFIGG 184
Cdd:cd03329 88 ----QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLeglespeayadfaeecKALGYRAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 185 KMPThWGPhdgdAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKR 264
Cdd:cd03329 163 KLHP-WGP----GVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 265 NAPAGMMVTsgEH-HGTLQSFRTLA-ETGIDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTP 342
Cdd:cd03329 238 KLDIPILGT--EHsRGALESRADWVlAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLHVIAAIRNTR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1478601324 343 FSEFLMTSPDCSTLRPQFDPILLDEPVPVNGRIHksVLDKPGFGVELNRD 392
Cdd:cd03329 316 YYERGLLHPSQKYDVYAGYLSVLDDPVDSDGFVH--VPKGPGLGVEIDFD 363
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
132-346 |
1.01e-30 |
|
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: 117.43 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 132 TISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARpdlakemgfiggkmpthwgphdgdagirkdaamVADMRE 211
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSIER---------------------------------VRAVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 212 KCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVTsgEHHGTL-QSFRTLAET 290
Cdd:cd00308 90 AFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAAD--ESVTTVdDALEALELG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478601324 291 GIDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSV------YSHHAVITFTNTPFSEF 346
Cdd:cd00308 168 AVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEssigtaAALHLAAALPNDRAIET 229
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
119-325 |
1.81e-28 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 114.99 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 119 TMYYSG---SGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYA--TGARP----DLAK---EMGFIGGKM 186
Cdd:PRK14017 66 VMYRGGfyrGGPILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSwiGGDRPadvaEAARarvERGFTAVKM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 187 ----PTHWgpHDGDAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYREL 262
Cdd:PRK14017 146 ngteELQY--IDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1478601324 263 KRNAPagMMVTSGEHHGTLQSFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPH 325
Cdd:PRK14017 224 AAQTS--IPIATGERLFSRWDFKRVLEAGgVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPH 285
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
68-399 |
1.39e-27 |
|
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: 112.15 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 68 VEVEAENGQTGFAVSTAGEMGCFI---VEKHLNRFIEGKcvsDIKLIHD--QMLGATMYYSgSGGLVMNTISCVDLALWD 142
Cdd:cd03322 19 LKITTDQGVTGLGDATLNGRELAVkayLREHLKPLLIGR---DANRIEDiwQYLYRGAYWR-RGPVTMNAIAAVDMALWD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 143 LFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMpthwgpHDGDAGIRKDA-AMVADMREKCGPDFWLML 221
Cdd:cd03322 95 IKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHL------AQGYRAIRVQLpKLFEAVREKFGFEFHLLH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 222 DCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVtsGEHHGTLQSFRTL-AETGIDIMQPDVG 300
Cdd:cd03322 169 DVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAV--GEVFNSIWDWQNLiQERLIDYIRTTVS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 301 WCGGLTTLVEIAALAKSRGQLVVPHGS---SVYSHHAVITFT----NTPFSEFLMTSPDCSTLRPQfdpilldEPVPVNG 373
Cdd:cd03322 247 HAGGITPARKIADLASLYGVRTGWHGPtdlSPVGMAAALHLDlwvpNFGIQEYMRHAEETLEVFPH-------SVRFEDG 319
|
330 340
....*....|....*....|....*.
gi 1478601324 374 RIHKSvlDKPGFGVELNRDCHLKRPY 399
Cdd:cd03322 320 YLHPG--EEPGLGVEIDEKAAAKFPY 343
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
114-392 |
3.48e-20 |
|
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: 91.00 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 114 QMLGATMYYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRdEIQFY---------ATGARPDLAKEMGFIGG 184
Cdd:cd03321 82 RALAKRFRLLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR-PVQAYdshgldgakLATERAVTAAEEGFHAV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 185 KMPThwgphdGDAGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKR 264
Cdd:cd03321 161 KTKI------GYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIAS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 265 --NAPAGMmvtsGEH-HGTLQSFRTLAETGIDIMQPDVGWCGGLTTLVEIAALAKSRGqlvvphgssvyshhavITFTNT 341
Cdd:cd03321 235 alRTPVQM----GENwLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAG----------------IPMSSH 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1478601324 342 PFSEF----LMTSPDCSTLR--PQFDPIlLDEPVPV-NGRIHKSvlDKPGFGVELNRD 392
Cdd:cd03321 295 LFQEIsahlLAVTPTAHWLEyvDWAGAI-LEPPLKFeDGNAVIP--DEPGNGIIWREK 349
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
175-267 |
8.35e-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: 80.79 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 175 LAKEMGFIGGKMptHWGPHDGDagirkDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQ 254
Cdd:smart00922 11 AVAEAGFRAVKV--KVGGGPLE-----DLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|...
gi 1478601324 255 QYEGYRELKRNAP 267
Cdd:smart00922 84 DLEGLAELRRATP 96
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
126-399 |
1.44e-15 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 77.64 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 126 GGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFY--ATGAR-PDL------AKEMGF--------IGGkMPT 188
Cdd:PRK15072 79 GPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYghANGRDiDELlddvarHLELGYkairvqcgVPG-LKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 189 HWGPHDGDAGIRKDAA---------------------MVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWI 247
Cdd:PRK15072 158 TYGVSKGKGLAYEPATkgllpeeelwstekylrfvpkLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 248 EECLPPQQYEGYRELKRNAPAGMMVtsGEHHGTLQSFRTL-AETGIDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHG 326
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAV--GEVFNSIWDCKQLiEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 327 SSVYSH-------HAVITFTNTPFSEFLMTSPDCSTLRPQ---FDpilldepvpvNGRIHKSvlDKPGFGVELNRDCHLK 396
Cdd:PRK15072 316 PTDLSPvcmaaalHFDLWVPNFGIQEYMGHSEETLEVFPHsytFE----------DGYLHPG--DAPGLGVDFDEKLAAK 383
|
...
gi 1478601324 397 RPY 399
Cdd:PRK15072 384 YPY 386
|
|
| 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 ... |
66-319 |
1.15e-13 |
|
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: 71.07 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 66 LIVEVEAEnGQTGF--AVSTA---GEM--GCFIVEKHLNRFIEGKCVSDIKLIhdQMLGATMYYSGSGglvmntISCVDL 138
Cdd:cd03319 28 VIVEIELD-GITGYgeAAPTPrvtGETveSVLAALKSVRPALIGGDPRLEKLL--EALQELLPGNGAA------RAAVDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 139 ALWDLFGKVVGLPVYKLLGGAVRDEIQFYAT------GARPDLAKEM---GF------IGGkmpthwgphdgdaGIRKDA 203
Cdd:cd03319 99 ALWDLEAKLLGLPLYQLWGGGAPRPLETDYTisidtpEAMAAAAKKAakrGFpllkikLGG-------------DLEDDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 204 AMVADMREKCgPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMVTSGEHhgTLQS 283
Cdd:cd03319 166 ERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCF--SAAD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1478601324 284 FRTLAET----GIDI--MQpdvgwCGGLTTLVEIAALAKSRG 319
Cdd:cd03319 243 AARLAGGgaydGINIklMK-----TGGLTEALRIADLARAAG 279
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
136-394 |
4.60e-12 |
|
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: 67.03 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 136 VDLALWDLFGKVVGLPVYKLLGGAVRDE-----IQFYATGARP----DLAK---EM------GFIGGKMPThwgphdGDA 197
Cdd:cd03326 113 LDMAVWDAVAKIAGLPLYRLLARRYGRGqadprVPVYAAGGYYypgdDLGRlrdEMrryldrGYTVVKIKI------GGA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 198 GIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELkRNAPAGMMVTsGEH 277
Cdd:cd03326 187 PLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAEL-ADHYDGPIAT-GEN 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 278 HGTLQSFRTLAETG-----IDIMQPDVGWCGGLTTLVEIAALAKSRG---QLVVPHGSSVYSHHAVI----------TFT 339
Cdd:cd03326 265 LFSLQDARNLLRYGgmrpdRDVLQFDPGLSYGLPEYLRMLDVLEAHGwsrRRFFPHGGHLMSLHIAAglglggnesyPDV 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1478601324 340 NTPFSEFlmtsPDCSTLRpqfdpilldepvpvNGRIhkSVLDKPGFGVELNRDCH 394
Cdd:cd03326 345 FQPFGGF----ADGCKVE--------------NGYV--RLPDAPGIGFEGKAELA 379
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
66-397 |
6.28e-11 |
|
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: 63.49 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 66 LIVEVEAENGQTGF--AVSTAG--------EMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGAtmyysgsggLVMNTI-- 133
Cdd:cd03318 31 VLVRLTTSDGVVGIgeATTPGGpawggespETIKAIIDRYLAPLLIGRDATNIGAAMALLDRA---------VAGNLFak 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 134 SCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPD------LAKEMGFIGG----KMPTHWGPHdgdagiRKDA 203
Cdd:cd03318 102 AAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDterdiaEAEEMLEAGRhrrfKLKMGARPP------ADDL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 204 AMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMM----VTSGEHHG 279
Cdd:cd03318 176 AHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMadesVSGPADAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 280 TLQSFRTLAETGIDIMQpdvgwCGGLTTLVEIAALAKSRGqlVVPHG-----SSV---YSHHAVITFTNTPF-SEFLMTS 350
Cdd:cd03318 256 ELARRGAADVFSLKIAK-----SGGLRRAQKVAAIAEAAG--IALYGgtmleSSIgtaASAHLFATLPSLPFgCELFGPL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1478601324 351 pdcstlrpQFDPILLDEPVPV-NGRIHksVLDKPGFGVELNRDcHLKR 397
Cdd:cd03318 329 --------LLAEDLLEEPLAYrDGELH--VPTGPGLGVRLDED-KVRR 365
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
136-323 |
9.18e-10 |
|
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: 58.89 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 136 VDLALWDLFGKVVGLPVYKLLGGaVRDEIQF-YATGARP-----DLAK---EMGFIGGKMPThwGPHDGdagirKDAAMV 206
Cdd:cd03315 48 VDMALWDLWGKRLGVPVYLLLGG-YRDRVRVaHMLGLGEpaevaEEARralEAGFRTFKLKV--GRDPA-----RDVAVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 207 ADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEECLPPQQYEGYRELKRNAPAGMMvtSGEHHGTLQ-SFR 285
Cdd:cd03315 120 AALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIM--ADESAFTPHdAFR 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 1478601324 286 TLAETGIDIMQPDVGWCGGLTTLVEIAALAKSRGQLVV 323
Cdd:cd03315 198 ELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVM 235
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
127-329 |
1.31e-08 |
|
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: 56.20 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 127 GLVMNtiscvdlALWDLFGKVVGLPVYKLLGGAVRDE----IQF-YATGA-RPDLA-------------KEMGFIGGKMP 187
Cdd:cd03324 112 AAVVN-------AVWDLWAKAEGKPLWKLLVDMTPEElvscIDFrYITDAlTPEEAleilrrgqpgkaaREADLLAEGYP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 188 TH-----W-GPHDG----------DAGIR----KDAAMVAD-------MREKCGPDFWLMLDCWMSQDVNYATKLAHACA 240
Cdd:cd03324 185 AYttsagWlGYSDEklrrlckealAQGFThfklKVGADLEDdirrcrlAREVIGPDNKLMIDANQRWDVPEAIEWVKQLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 241 PFNLKWIEECLPPQQYEGYRELKRN-APAGMMVTSGEHHGTLQSFRTLAETG-IDIMQPDVGWCGGLTTLVEIAALAKSR 318
Cdd:cd03324 265 EFKPWWIEEPTSPDDILGHAAIRKAlAPLPIGVATGEHCQNRVVFKQLLQAGaIDVVQIDSCRLGGVNENLAVLLMAAKF 344
|
250
....*....|.
gi 1478601324 319 GQLVVPHGSSV 329
Cdd:cd03324 345 GVPVCPHAGGV 355
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
67-392 |
2.10e-07 |
|
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: 52.71 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 67 IVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGATMYYSGSGG--------LVMNTISCVDL 138
Cdd:cd03323 32 IVELTDDNGNTGVGESPGGAEALEALLEAARSLVGGDVFGAYLAVLESVRVAFADRDAGGRglqtfdlrTTVHVVTAFEV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 139 ALWDLFGKVVGLPVYKLLGGAVRDEIQFYA----TGAR-------------------PD----LAKEM----GFIGGKMP 187
Cdd:cd03323 112 ALLDLLGQALGVPVADLLGGGQRDSVPFLAylfyKGDRhktdlpypwfrdrwgealtPEgvvrLARAAidryGFKSFKLK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 188 ThwGPHDGDAGIrkdAAMVAdMREKCgPDFWLMLD---CW-MSQDVNYATKLAHAcapfnLKWIEEclPPQQYEGYRELK 263
Cdd:cd03323 192 G--GVLPGEEEI---EAVKA-LAEAF-PGARLRLDpngAWsLETAIRLAKELEGV-----LAYLED--PCGGREGMAEFR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 264 RNA----PAGMMVTSGEHHGtlqsfRTLAETGIDIMQPDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSvyshHAVIT-- 337
Cdd:cd03323 258 RATglplATNMIVTDFRQLG-----HAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNN----HLGISla 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478601324 338 -FTN----TPFSEFlmtspDCSTLRPQFD-PILLDEPVP-VNGRIHksVLDKPGFGVELNRD 392
Cdd:cd03323 329 mMTHvaaaAPGLIT-----ACDTHWIWQDgQVITGEPLRiKDGKVA--VPDKPGLGVELDRD 383
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
67-157 |
1.04e-06 |
|
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: 47.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478601324 67 IVEVEAENGQTG----FAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLGATMYysgsgglVMNTISCVDLALWD 142
Cdd:pfam02746 30 IVRIETSEGVVGigeaTSYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALG-------NMSAKAAIDMALWD 102
|
90
....*....|....*
gi 1478601324 143 LFGKVVGLPVYKLLG 157
Cdd:pfam02746 103 LKAKVLNLPLADLLG 117
|
|
| |
