|
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: 796.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 1 MTLPKIKQVRAWFTGGataekgaGGGDYHDQGANHWIDDHIATPMSKYRDYEQSRQSFGINVLGTLVVEVEAENGQTGFA 80
Cdd:PRK15440 1 MTLPKIKHVRAWFVGG-------GGADYHDQGANHWIDDHIATPMSKYPEYRQSRQSFGINVLGTLVVEVEAENGQVGFA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 81 VSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSATLYYsGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAV 160
Cdd:PRK15440 74 VSTAGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYY-GRKGLVMNTISCVDLALWDLLGKVRGLPVYKLLGGAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 161 RDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACA 240
Cdd:PRK15440 153 RDELQFYATGARPDLAKEMGFIGGKMPLHHGPADGDAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 241 PYNLKWIEECLPPQQYESYRELKRNAPVGMMVTSGEHHGTLQSFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSRG 319
Cdd:PRK15440 233 PYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGEHEATLQGFRTLLEMGcIDIIQPDVGWCGGLTELVKIAALAKARG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 320 QLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMRPQFDPILLNEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPY 399
Cdd:PRK15440 313 QLVVPHGSSVYSHHFVITRTNSPFSEFLMMSPDADTVVPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCNLKRPY 392
|
..
gi 999851465 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 |
0e+00 |
|
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: 506.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 64 GTLVVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSATLYYsGSGGLVMNTISCVDLALWDL 143
Cdd:cd03327 10 GWLFVEIETDDGTVGYANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAY-GRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 144 FGKVVGLPVYKLLGGAVRDEIQFYATGA-------RPDLAKEM---GFIGGKMPTHWGPHDGDAGIRKDAAMVADMREKC 213
Cdd:cd03327 89 LGKIRGEPVYKLLGGRTRDKIPAYASGLyptdldeLPDEAKEYlkeGYRGMKMRFGYGPSDGHAGLRKNVELVRAIREAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 214 GEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNApvGMMVTSGEHHGTLQSFRTLSE-TGI 292
Cdd:cd03327 169 GYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKAT--GIPISTGEHEYTVYGFKRLLEgRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 293 DIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMrPQFDPILLNEPVPVN 372
Cdd:cd03327 247 DILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQIYNYHFIMSEPNSPFAEYLPNSPDEVGN-PLFYYIFLNEPVPVN 325
|
330
....*....|....*...
gi 999851465 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 |
1.35e-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: 256.77 E-value: 1.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 66 LVVEVEAENGQTGFAVSTAGEMGCF---IVEKHLNRFIEGKCVSDIKLIHDQMLSATlYYSGSGGLVMNTISCVDLALWD 142
Cdd:cd03316 27 VLVRVTTDDGITGWGEAYPGGRPSAvaaAIEDLLAPLLIGRDPLDIERLWEKLYRRL-FWRGRGGVAMAAISAVDIALWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 143 LFGKVVGLPVYKLLGGAVRDEIQFYATGARPDL-----------AKEMGFIGGKMptHWGPHD-GDAGIRKDAAMVADMR 210
Cdd:cd03316 106 IKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDspeelaeeakrAVAEGFTAVKL--KVGGPDsGGEDLREDLARVRAVR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 211 EKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGmmVTSGEHHGTLQSFRTLSET 290
Cdd:cd03316 184 EAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQATSVP--IAAGENLYTRWEFRDLLEA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 291 G-IDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHG-----SSVYSHHAVITFTNTPFSEFLMTSPdcstmrPQFDPIL 364
Cdd:cd03316 262 GaVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGaggpiGLAASLHLAAALPNFGILEYHLDDL------PLREDLF 335
|
330 340
....*....|....*....|....
gi 999851465 365 LNEPVPVNGRIHksVLDKPGFGVE 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 |
4.87e-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: 203.52 E-value: 4.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 65 TLVVEVEAENGQTGFavstaGEMGCF---------IVEKHLNRFIEGKCVSDIKLIHDQMLSAtlyysgsGGLVMNTISC 135
Cdd:COG4948 31 VVLVRVETDDGITGW-----GEAVPGgtgaeavaaALEEALAPLLIGRDPLDIEALWQRLYRA-------LPGNPAAKAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 136 VDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDL---------AKEMGF----IGGkmpthwgphdGDAGIRKD 202
Cdd:COG4948 99 VDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPeemaeeareAVARGFralkLKV----------GGPDPEED 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 203 AAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVtsGEHHGTLQ 282
Cdd:COG4948 169 VERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAA--DESLTSRA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 283 SFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHG---SSV---YSHHAVITFTNTPFSEFlmtspdcST 355
Cdd:COG4948 247 DFRRLIEAGaVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCmleSGIglaAALHLAAALPNFDIVEL-------DG 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 999851465 356 MRPQFDPILLNEPVPVNGRIHksVLDKPGFGVELNRD 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 |
2.46e-40 |
|
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: 142.70 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 195 GDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVts 274
Cdd:pfam13378 23 GGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIAT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 275 GEHHGTLQSFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPH-----GSSVYSHHAVITFTNTPFSEflm 348
Cdd:pfam13378 101 GESLYSREDFRRLLEAGaVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHsgggpIGLAASLHLAAAVPNLLIQE--- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 999851465 349 tspDCSTMRPQFDPILLNEPVPVNGRIHksVLDKPGFGVELNRD 392
Cdd:pfam13378 178 ---YFLDPLLLEDDLLTEPLEVEDGRVA--VPDGPGLGVELDED 216
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
96-390 |
7.64e-35 |
|
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: 131.68 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 96 LNRFIEGKCVSDIKLiHDQMLSATLYYSGsGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFY--ATGARP 173
Cdd:cd03325 47 LEDYLIGKDPMNIEH-HWQVMYRGGFYRG-GPVLMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYswIGGDRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 174 D-------LAKEMGFIGGKM----PTHWgpHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPY 242
Cdd:cd03325 125 SdvaeaarARREAGFTAVKMnateELQW--IDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 243 NLKWIEECLPPQQYESYRELKR--NAPVGmmvtSGEHHGTLQSFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSRG 319
Cdd:cd03325 203 RLLFIEEPVLPENVEALAEIAArtTIPIA----TGERLFSRWDFKELLEDGaVDIIQPDISHAGGITELKKIAAMAEAYD 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 999851465 320 QLVVPHG-----SSVYSHHAVITFTNTPFSEflMTSPDCSTMRPQFDPILLNEPVP--VNGRIhkSVLDKPGFGVELN 390
Cdd:cd03325 279 VALAPHCplgpiALAASLHVDASTPNFLIQE--QSLGIHYNEGDDLLDYLVDPEVFdmENGYV--KLPTGPGLGIEID 352
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
41-392 |
1.21e-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: 128.67 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 41 IATPMSKYRDYEQSRQSFGINVLGTLVVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSAtl 120
Cdd:cd03329 10 FEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQDLWRL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 121 yysgSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGaVRDEIQFYATGARPDLA----------------KEMGFIGG 184
Cdd:cd03329 88 ----QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLeglespeayadfaeecKALGYRAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 185 KMPThWGPhdgdAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKR 264
Cdd:cd03329 163 KLHP-WGP----GVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 265 NAPVGMMVTsgEH-HGTLQSFRTL-SETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTP 342
Cdd:cd03329 238 KLDIPILGT--EHsRGALESRADWvLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLHVIAAIRNTR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 999851465 343 FSEFLMTSPDCSTMRPQFDPILLNEPVPVNGRIHksVLDKPGFGVELNRD 392
Cdd:cd03329 316 YYERGLLHPSQKYDVYAGYLSVLDDPVDSDGFVH--VPKGPGLGVEIDFD 363
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
65-389 |
1.16e-32 |
|
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: 125.99 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 65 TLV-VEVEAeNGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSAtLYYSGSGGLVMNTISCVDLALWDL 143
Cdd:cd03328 29 TLVlVEVRA-GGRTGLGYTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRA-VRNAGRPGVAAMAISAVDIALWDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 144 FGKVVGLPVYKLLGgAVRDEIQFYATG---ARPD----------LAKEMGFIGGKMPTHWgphdgdagiRKDAAMVADMR 210
Cdd:cd03328 107 KARLLGLPLARLLG-RAHDSVPVYGSGgftSYDDdrlreqlsgwVAQGIPRVKMKIGRDP---------RRDPDRVAAAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 211 EKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVTSGEHHGTLQSFRTLSET 290
Cdd:cd03328 177 RAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAGMDIAAGEYAYTLAYFRRLLEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 291 G-IDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMTSPDCSTMrpQFDpillNEPV 369
Cdd:cd03328 257 HaVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACAVPRLRHLEWFHDHVRIERM--LFD----GAPD 330
|
330 340
....*....|....*....|
gi 999851465 370 PVNGRIHKSvLDKPGFGVEL 389
Cdd:cd03328 331 PSGGALRPD-LSRPGLGLEL 349
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
132-346 |
3.28e-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: 115.89 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 132 TISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARpdlakemgfiggkmpthwgphdgdagirkdaamVADMRE 211
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSIER---------------------------------VRAVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 212 KCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVTsgEHHGTL-QSFRTLSET 290
Cdd:cd00308 90 AFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAAD--ESVTTVdDALEALELG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 999851465 291 GIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHGSSV------YSHHAVITFTNTPFSEF 346
Cdd:cd00308 168 AVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEssigtaAALHLAAALPNDRAIET 229
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
67-399 |
1.93e-29 |
|
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: 117.16 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 67 VVEVEAENGQTGFAVSTAGEMGCFI---VEKHLNRFIEGKcvsDIKLIHD--QMLSATLYYSgSGGLVMNTISCVDLALW 141
Cdd:cd03322 18 TLKITTDQGVTGLGDATLNGRELAVkayLREHLKPLLIGR---DANRIEDiwQYLYRGAYWR-RGPVTMNAIAAVDMALW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 142 DLFGKVVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMpthwgpHDGDAGIRKDA-AMVADMREKCGEDFWLM 220
Cdd:cd03322 94 DIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHL------AQGYRAIRVQLpKLFEAVREKFGFEFHLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 221 LDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVtsGEHHGTLQSFRTL-SETGIDIMQPDV 299
Cdd:cd03322 168 HDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAV--GEVFNSIWDWQNLiQERLIDYIRTTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 300 GWCGGLTTLVEIAAIAKSRGQLVVPHGS---SVYSHHAVITFT----NTPFSEFLMTSPDCSTMRPQfdpillnEPVPVN 372
Cdd:cd03322 246 SHAGGITPARKIADLASLYGVRTGWHGPtdlSPVGMAAALHLDlwvpNFGIQEYMRHAEETLEVFPH-------SVRFED 318
|
330 340
....*....|....*....|....*..
gi 999851465 373 GRIHKSvlDKPGFGVELNRDCNLKRPY 399
Cdd:cd03322 319 GYLHPG--EEPGLGVEIDEKAAAKFPY 343
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
121-325 |
1.79e-28 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 114.99 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 121 YYSGsGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYA--TGARP----DLAK---EMGFIGGKM----P 187
Cdd:PRK14017 72 FYRG-GPILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSwiGGDRPadvaEAARarvERGFTAVKMngteE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 188 THWgpHDGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAP 267
Cdd:PRK14017 151 LQY--IDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTS 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 999851465 268 VGmmVTSGEHHGTLQSFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPH 325
Cdd:PRK14017 229 IP--IATGERLFSRWDFKRVLEAGgVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPH 285
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
114-392 |
2.79e-19 |
|
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: 88.31 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 114 QMLSATLYYSGSGGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRdEIQFY---------ATGARPDLAKEMGFIGG 184
Cdd:cd03321 82 RALAKRFRLLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR-PVQAYdshgldgakLATERAVTAAEEGFHAV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 185 KMPThwgphdGDAGIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKR 264
Cdd:cd03321 161 KTKI------GYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIAS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 265 --NAPVGMmvtsGEH-HGTLQSFRTLSETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGqlvvphgssvyshhavITFTNT 341
Cdd:cd03321 235 alRTPVQM----GENwLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAG----------------IPMSSH 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 999851465 342 PFSEF----LMTSPDCSTMR--PQFDPIlLNEPVPV-NGRIHKSvlDKPGFGVELNRD 392
Cdd:cd03321 295 LFQEIsahlLAVTPTAHWLEyvDWAGAI-LEPPLKFeDGNAVIP--DEPGNGIIWREK 349
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
175-268 |
1.03e-17 |
|
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: 77.71 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 175 LAKEMGFIGGKMptHWGPHDGDagirkDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQ 254
Cdd:smart00922 11 AVAEAGFRAVKV--KVGGGPLE-----DLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|....
gi 999851465 255 QYESYRELKRNAPV 268
Cdd:smart00922 84 DLEGLAELRRATPI 97
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
126-399 |
1.41e-15 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 77.64 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 126 GGLVMNTISCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFY--ATGAR-PDL------AKEMGF--------IGGkMPT 188
Cdd:PRK15072 79 GPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYghANGRDiDELlddvarHLELGYkairvqcgVPG-LKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 189 HWGPHDGDAGIRKDAA---------------------MVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWI 247
Cdd:PRK15072 158 TYGVSKGKGLAYEPATkgllpeeelwstekylrfvpkLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 248 EECLPPQQYESYRELKRNAPVGMMVtsGEHHGTLQSFRTL-SETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVVPHG 326
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAV--GEVFNSIWDCKQLiEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 327 SSVYSH-------HAVITFTNTPFSEFLMTSPDCSTMRPQ---FDpillnepvpvNGRIHKSvlDKPGFGVELNRDCNLK 396
Cdd:PRK15072 316 PTDLSPvcmaaalHFDLWVPNFGIQEYMGHSEETLEVFPHsytFE----------DGYLHPG--DAPGLGVDFDEKLAAK 383
|
...
gi 999851465 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 |
2.03e-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: 70.30 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 66 LVVEVEAEnGQTGF--AVSTA---GEM--GCFIVEKHLNRFIEGKCVSDIKLIhdQMLSATLYYSGSGglvmntISCVDL 138
Cdd:cd03319 28 VIVEIELD-GITGYgeAAPTPrvtGETveSVLAALKSVRPALIGGDPRLEKLL--EALQELLPGNGAA------RAAVDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 139 ALWDLFGKVVGLPVYKLLGGAVRDEIQFYAT------GARPDLAKEM---GF------IGGkmpthwgphdgdaGIRKDA 203
Cdd:cd03319 99 ALWDLEAKLLGLPLYQLWGGGAPRPLETDYTisidtpEAMAAAAKKAakrGFpllkikLGG-------------DLEDDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 204 AMVADMREKCGeDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMVTSGEHhgTLQS 283
Cdd:cd03319 166 ERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCF--SAAD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 999851465 284 FRTLSET----GIDI--MQpdvgwCGGLTTLVEIAAIAKSRG 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 ... |
136-389 |
2.20e-13 |
|
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: 70.89 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 136 VDLALWDLFGKVVGLPVYKLLGGAVRDE-----IQFYATGARP----DLAK---EM------GFIGGKMPThwgphdGDA 197
Cdd:cd03326 113 LDMAVWDAVAKIAGLPLYRLLARRYGRGqadprVPVYAAGGYYypgdDLGRlrdEMrryldrGYTVVKIKI------GGA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 198 GIRKDAAMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELkRNAPVGMMVTsGEH 277
Cdd:cd03326 187 PLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAEL-ADHYDGPIAT-GEN 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 278 HGTLQSFRTLSETG-----IDIMQPDVGWCGGLTTLVEIAAIAKSRG---QLVVPHGSSVYSHHAVI----------TFT 339
Cdd:cd03326 265 LFSLQDARNLLRYGgmrpdRDVLQFDPGLSYGLPEYLRMLDVLEAHGwsrRRFFPHGGHLMSLHIAAglglggnesyPDV 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 999851465 340 NTPFSEFlmtsPDCSTMRpqfdpillnepvpvNGRIhkSVLDKPGFGVEL 389
Cdd:cd03326 345 FQPFGGF----ADGCKVE--------------NGYV--RLPDAPGIGFEG 374
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
66-392 |
2.39e-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: 64.65 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 66 LVVEVEAENGQTGF--AVSTAG--------EMGCFIVEKHLNRFIEGKCVSDIKLIHDQMlsatlyysgSGGLVMNTI-- 133
Cdd:cd03318 31 VLVRLTTSDGVVGIgeATTPGGpawggespETIKAIIDRYLAPLLIGRDATNIGAAMALL---------DRAVAGNLFak 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 134 SCVDLALWDLFGKVVGLPVYKLLGGAVRDEIQFYATGARPD------LAKEMGFIGG----KMPTHWGPHdgdagiRKDA 203
Cdd:cd03318 102 AAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDterdiaEAEEMLEAGRhrrfKLKMGARPP------ADDL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 204 AMVADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMM----VTSGEHHG 279
Cdd:cd03318 176 AHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMadesVSGPADAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 280 TLQSFRTLSETGIDIMQpdvgwCGGLTTLVEIAAIAKSRGqlVVPHG-----SSV---YSHHAVITFTNTPF-SEFLMTS 350
Cdd:cd03318 256 ELARRGAADVFSLKIAK-----SGGLRRAQKVAAIAEAAG--IALYGgtmleSSIgtaASAHLFATLPSLPFgCELFGPL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 999851465 351 pdcstmrpQFDPILLNEPVPV-NGRIHksVLDKPGFGVELNRD 392
Cdd:cd03318 329 --------LLAEDLLEEPLAYrDGELH--VPTGPGLGVRLDED 361
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
136-323 |
1.03e-08 |
|
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: 55.81 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 136 VDLALWDLFGKVVGLPVYKLLGGaVRDEIQF-YATGARP-----DLAK---EMGFIGGKMPThwGPHDGdagirKDAAMV 206
Cdd:cd03315 48 VDMALWDLWGKRLGVPVYLLLGG-YRDRVRVaHMLGLGEpaevaEEARralEAGFRTFKLKV--GRDPA-----RDVAVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 207 ADMREKCGEDFWLMLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYESYRELKRNAPVGMMvtSGEHHGTLQ-SFR 285
Cdd:cd03315 120 AALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIM--ADESAFTPHdAFR 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 999851465 286 TLSETGIDIMQPDVGWCGGLTTLVEIAAIAKSRGQLVV 323
Cdd:cd03315 198 ELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVM 235
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
67-157 |
2.13e-07 |
|
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: 49.01 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 67 VVEVEAENGQTG----FAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSATLYysgsgglVMNTISCVDLALWD 142
Cdd:pfam02746 30 IVRIETSEGVVGigeaTSYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALG-------NMSAKAAIDMALWD 102
|
90
....*....|....*
gi 999851465 143 LFGKVVGLPVYKLLG 157
Cdd:pfam02746 103 LKAKVLNLPLADLLG 117
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
67-168 |
5.46e-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: 51.17 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 67 VVEVEAENGQTGFAVSTAGEMGCFIVEKHLNRFIEGKCVSDIKLIHDQMLSATLYYSGSGG--------LVMNTISCVDL 138
Cdd:cd03323 32 IVELTDDNGNTGVGESPGGAEALEALLEAARSLVGGDVFGAYLAVLESVRVAFADRDAGGRglqtfdlrTTVHVVTAFEV 111
|
90 100 110
....*....|....*....|....*....|
gi 999851465 139 ALWDLFGKVVGLPVYKLLGGAVRDEIQFYA 168
Cdd:cd03323 112 ALLDLLGQALGVPVADLLGGGQRDSVPFLA 141
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
127-329 |
3.18e-06 |
|
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: 48.88 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 127 GLVMNtiscvdlALWDLFGKVVGLPVYKLLGGAVRDE----IQF-YATGA-RPDLA-------------KEMGFIGGKMP 187
Cdd:cd03324 112 AAVVN-------AVWDLWAKAEGKPLWKLLVDMTPEElvscIDFrYITDAlTPEEAleilrrgqpgkaaREADLLAEGYP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 188 TH-----W-GPHDG----------DAGIR----KDAAMVAD-------MREKCGEDFWLMLDCWMSQDVNYATKLAHACA 240
Cdd:cd03324 185 AYttsagWlGYSDEklrrlckealAQGFThfklKVGADLEDdirrcrlAREVIGPDNKLMIDANQRWDVPEAIEWVKQLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999851465 241 PYNLKWIEECLPPQQYESYRELKRN-APVGMMVTSGEHHGTLQSFRTLSETG-IDIMQPDVGWCGGLTTLVEIAAIAKSR 318
Cdd:cd03324 265 EFKPWWIEEPTSPDDILGHAAIRKAlAPLPIGVATGEHCQNRVVFKQLLQAGaIDVVQIDSCRLGGVNENLAVLLMAAKF 344
|
250
....*....|.
gi 999851465 319 GQLVVPHGSSV 329
Cdd:cd03324 345 GVPVCPHAGGV 355
|
|
| |
