|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
6-399 |
0e+00 |
|
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: 533.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRPdRHNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNVNAYWRNGPV 85
Cdd:cd03322 2 ITAIEVIVTCP-GRNFVTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 86 MNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIRCQLgfyggtpsglh 165
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQL----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 166 apenPTpgawfdqqeymrntvdMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQV 245
Cdd:cd03322 150 ----PK----------------LFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 246 RQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDMTPIGVAVNTHLNI 325
Cdd:cd03322 210 RQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSPVGMAAALHLDL 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821659268 326 HLHNAAIQEFIPRSAMTDRVFPGAPEVKEGFIYPPVNAGIGVGFNEALAQAHPVMYRPheWTQSRLPDGTLHTP 399
Cdd:cd03322 290 WVPNFGIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRY--LPVARLEDGTVHNW 361
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
6-397 |
9.93e-139 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 401.59 E-value: 9.93e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRPDRhNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNVNAYWRNGPV 85
Cdd:PRK15072 3 IVDAEVIVTCPGR-NFVTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGAYWRRGPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 86 MNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIRCQLGF------YGG 159
Cdd:PRK15072 82 TMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQCGVpglkttYGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 160 TPSGLHAPENPTPGAW-----FDQQEYMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDIL 234
Cdd:PRK15072 162 SKGKGLAYEPATKGLLpeeelWSTEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 235 PPQQSAWLEQVRQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDMTP 314
Cdd:PRK15072 242 PAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTDLSP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 315 IGVAVNTHLNIHLHNAAIQEFIPRSAMTDRVFPGAPEVKEGFIYPPVNAGIGVGFNEALAQAHPvmYRPHEWTQSRLPDG 394
Cdd:PRK15072 322 VCMAAALHFDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKYP--YEPAYLPVARLEDG 399
|
...
gi 1821659268 395 TLH 397
Cdd:PRK15072 400 TMW 402
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
6-367 |
6.90e-116 |
|
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: 341.90 E-value: 6.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRP---------DRHNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNV 76
Cdd:cd03316 2 ITDVETFVLRVplpepggavTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 77 NAYWR-NGPVMNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASG--DTLDALFASVDGLIEQGYRHIRCQ 153
Cdd:cd03316 82 RLFWRgRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGydDSPEELAEEAKRAVAEGFTAVKLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 154 LGFYGGtpsglhapenptpgawfdQQEYMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDI 233
Cdd:cd03316 162 VGGPDS------------------GGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 234 LPPQQSAWLEQVRQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDmt 313
Cdd:cd03316 224 VPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGG-- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1821659268 314 PIGVAVNTHLNIHLHNAAIQEFIPRSAMT-DRVFPGAPEVKEGFIYPPVNAGIGV 367
Cdd:cd03316 302 PIGLAASLHLAAALPNFGILEYHLDDLPLrEDLFKNPPEIEDGYVTVPDRPGLGV 356
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
6-377 |
1.27e-103 |
|
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: 310.60 E-value: 1.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRP-------------DRHNLVTVRVTTDQGVTGHG-CATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLW 71
Cdd:COG4948 3 ITDIEVYPVRLplkrpftisrgtrTERDVVLVRVETDDGITGWGeAVPGGTGAEAVAAALEEALAPLLIGRDPLDIEALW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 72 QMMNvnaywRNGPVMNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIR 151
Cdd:COG4948 83 QRLY-----RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 152 CQLGFYGgtpsglhapenptpgawfdqqeyMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIE 231
Cdd:COG4948 158 LKVGGPD-----------------------PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 232 DILPPQQSAWLEQVRQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGD 311
Cdd:COG4948 215 QPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLE 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821659268 312 mTPIGVAVNTHLNIHLHNAAIQEFIPRSAMTDRVFPGAPEVKEGFIYPPVNAGIGVGFNEALAQAH 377
Cdd:COG4948 295 -SGIGLAAALHLAAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
6-370 |
1.11e-73 |
|
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: 233.76 E-value: 1.11e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRPdrhNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEyLQPLLTGRDANNIEDLWQMMNVNAYWRNGPV 85
Cdd:cd03325 2 ITKIETFVVPP---RWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRGGFYRGGPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 86 MNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIRCQLgfyggtpsglh 165
Cdd:cd03325 78 LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNA----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 166 apenPTPGAWFDQQEYMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQV 245
Cdd:cd03325 147 ----TEELQWIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 246 RQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPgdMTPIGVAVNTHLNI 325
Cdd:cd03325 223 AARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCP--LGPIALAASLHVDA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1821659268 326 HLHNAAIQE------FIPRSAMTDRVF-PGAPEVKEGFIYPPVNAGIGVGFN 370
Cdd:cd03325 301 STPNFLIQEqslgihYNEGDDLLDYLVdPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
6-395 |
2.04e-64 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 210.52 E-value: 2.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFITRPdrhNLVTVRVTTDQGVTGHGCATFQQRPLAVKTLVEEyLQPLLTGRDANNIEDLWQMMNVNAYWRNGPV 85
Cdd:PRK14017 3 ITKLETFRVPP---RWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRGGFYRGGPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 86 MNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIRcqlgfYGGTPSgLH 165
Cdd:PRK14017 79 LMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVK-----MNGTEE-LQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 166 APENPtpgAWFDQQeymrntVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQV 245
Cdd:PRK14017 153 YIDSP---RKVDAA------VARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 246 RQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPgdMTPIGVAVNTHLNI 325
Cdd:PRK14017 224 AAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCP--LGPIALAACLQVDA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821659268 326 HLHNAAIQE------FIPRSAMTDRVF-PGAPEVKEGFIYPPVNAGIGVGFNEALAQAhpVMYRPHEWTQS--RLPDGT 395
Cdd:PRK14017 302 VSPNAFIQEqslgihYNQGADLLDYVKnKEVFAYEDGFVAIPTGPGLGIEIDEAKVRE--RAKTGHDWRNPvwRHADGS 378
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
6-370 |
3.50e-52 |
|
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: 177.53 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 6 IKNIECFItrpdrhNLVTVRVTTDQGVTGHGCATfqqRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMM-NVNAYWRNGP 84
Cdd:cd03327 2 IKSVRTRV------GWLFVEIETDDGTVGYANTT---GGPVACWIVDQHLARFLIGKDPSDIEKLWDQMyRATLAYGRKG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 85 VMNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAY-SHASGDTLDALFASVDGLIEQGYRHIRCQLGfYGgtPSg 163
Cdd:cd03327 73 IAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYaSGLYPTDLDELPDEAKEYLKEGYRGMKMRFG-YG--PS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 164 lhapenptpgawfDQQEYMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLE 243
Cdd:cd03327 149 -------------DGHAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 244 QVRQHSCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGpgdmtpiGVAVNTHL 323
Cdd:cd03327 216 ELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA-------SQIYNYHF 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1821659268 324 NIHLHNAAIQEFIPRS------AMTDRVFPGAPEVKEGFIYPPVNAGIGVGFN 370
Cdd:cd03327 289 IMSEPNSPFAEYLPNSpdevgnPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
186-372 |
2.90e-38 |
|
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: 136.93 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 186 VDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSCVPLAMGELFNNPSEW 265
Cdd:pfam13378 31 VERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 266 HDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGdmTPIGVAVNTHLNIHLHNAAIQE-FIPRSAMTDR 344
Cdd:pfam13378 111 RRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG--GPIGLAASLHLAAAVPNLLIQEyFLDPLLLEDD 188
|
170 180
....*....|....*....|....*...
gi 1821659268 345 VFPGAPEVKEGFIYPPVNAGIGVGFNEA 372
Cdd:pfam13378 189 LLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
24-310 |
1.21e-31 |
|
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: 123.28 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 24 VRVTTDQGVTGHgcaTFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMnvnAYW-RNGPVMnnAISGVDMALWDIKS 102
Cdd:cd03329 37 LTIETDEGAKGH---AFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQDL---WRLqRGLTDR--GLGLVDIALWDLAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 103 QLAGMPLYQLFGGkSRDAIPAY-SHASGDTLDAL-----FASV-DGLIEQGYRHIRcqlgfyggtpsgLHAPENPTPgaw 175
Cdd:cd03329 109 KYLGLPVHRLLGG-YREKIPAYaSTMVGDDLEGLespeaYADFaEECKALGYRAIK------------LHPWGPGVV--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 176 fdqqeymRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSCVPLAM 255
Cdd:cd03329 173 -------RRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821659268 256 GEL----FNNPSEWhdlIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPG 310
Cdd:cd03329 246 TEHsrgaLESRADW---VLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNG 301
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
89-335 |
1.42e-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: 117.04 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 89 AISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHAsgdtldalfasvdglieqgyrhircqlgfyggtpsglhape 168
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI----------------------------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 169 nptpgawfdqqeyMRntvdmFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQH 248
Cdd:cd00308 82 -------------ER-----VRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 249 SCVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGDmTPIGVAVNTHLNIHLH 328
Cdd:cd00308 144 TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE-SSIGTAAALHLAAALP 222
|
....*..
gi 1821659268 329 NAAIQEF 335
Cdd:cd00308 223 NDRAIET 229
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
50-347 |
2.13e-28 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 114.83 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 50 LVEEYLQPLLTGRDANNIEDLW-QMMNVNAYW-RNGPVMNnAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYshA 127
Cdd:PRK15440 84 IVEKHLNRFIEGKCVSDIELIWdQMLNATLYYgRKGLVMN-TISCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFY--A 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 128 SGDTLDalfasvdglieqgyrhIRCQLGFYGGTPSGLHAPEnptpgawfDQQEYMRNTVDMFRALREKYGWSLHFLHDVH 207
Cdd:PRK15440 161 TGARPD----------------LAKEMGFIGGKMPLHHGPA--------DGDAGLRKNAAMVADMREKVGDDFWLMLDCW 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 208 ERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHscVPLAM----GELFNNPSEWHDLIVNRRIDFIRCHVSQ 283
Cdd:PRK15440 217 MSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN--APAGMmvtsGEHEATLQGFRTLLEMGCIDIIQPDVGW 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821659268 284 IGGITPALKLAHLCQAFGVRLAWHGPGdmtpigvAVNTHLNIHLHNAAIQEFIPRSAMTDRVFP 347
Cdd:PRK15440 295 CGGLTELVKIAALAKARGQLVVPHGSS-------VYSHHFVITRTNSPFSEFLMMSPDADTVVP 351
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
21-372 |
1.27e-27 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 112.03 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 21 LVTVRVTTDQGVTGHGCAT-------FQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNvnaywrnGPVMNN--AIS 91
Cdd:cd03318 30 LVLVRLTTSDGVVGIGEATtpggpawGGESPETIKAIIDRYLAPLLIGRDATNIGAAMALLD-------RAVAGNlfAKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 92 GVDMALWDIKSQLAGMPLYQLFGGKSRDAIP-AYSHASGDTlDALFASVDGLIEQG-YRHIRCQLGFyggtpsglhapeN 169
Cdd:cd03318 103 AIEMALLDAQGRRLGLPVSELLGGRVRDSLPvAWTLASGDT-ERDIAEAEEMLEAGrHRRFKLKMGA------------R 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 170 PTpgawfdqqeymRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHS 249
Cdd:cd03318 170 PP-----------ADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 250 CVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLawHGpGDM--TPIGVAVNTHLnihl 327
Cdd:cd03318 239 RVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIAL--YG-GTMleSSIGTAASAHL---- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1821659268 328 hNAAIQ------EFIPRSAMTDRVFPGAPEVKEGFIYPPVNAGIGVGFNEA 372
Cdd:cd03318 312 -FATLPslpfgcELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDED 361
|
|
| 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 ... |
20-323 |
3.97e-26 |
|
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: 106.89 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 20 NLVTVRVTTDqGVTGHGCATfqqrPLAVKT--------LVEEYLQPLLTGRDANnIEDLWQMMNvNAYWRNGPvmnnAIS 91
Cdd:cd03319 26 ENVIVEIELD-GITGYGEAA----PTPRVTgetvesvlAALKSVRPALIGGDPR-LEKLLEALQ-ELLPGNGA----ARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 92 GVDMALWDIKSQLAGMPLYQLFGGKSRDAIP-AYShASGDTLDALFASVDGLIEQGYRHIRCQLGfyggtpSGLHAPenp 170
Cdd:cd03319 95 AVDIALWDLEAKLLGLPLYQLWGGGAPRPLEtDYT-ISIDTPEAMAAAAKKAAKRGFPLLKIKLG------GDLEDD--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 171 tpgawfdqqeymrntVDMFRALREKYGwSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSC 250
Cdd:cd03319 165 ---------------IERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821659268 251 VPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWhgpGDM--TPIGVAVNTHL 323
Cdd:cd03319 229 LPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMV---GCMveSSLSIAAAAHL 300
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
21-114 |
8.36e-25 |
|
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: 97.93 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 21 LVTVRVTTDQGVTGHG-CATFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMNVNAYWrNGpvmnNAISGVDMALWD 99
Cdd:pfam02746 28 LVIVRIETSEGVVGIGeATSYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALG-NM----SAKAAIDMALWD 102
|
90
....*....|....*
gi 1821659268 100 IKSQLAGMPLYQLFG 114
Cdd:pfam02746 103 LKAKVLNLPLADLLG 117
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
21-372 |
1.18e-21 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 95.24 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 21 LVTVRVTTDQGVTGHGcATFQQRPLAVKT---LVEEyLQPLLTGRDANNIEdLWQMMNvnAYWR---NGPVMNNAISGVD 94
Cdd:cd03321 31 LVLIDLATDEGVTGHS-YLFTYTPAALKSlkqLLDD-MAALLVGEPLAPAE-LERALA--KRFRllgYTGLVRMAAAGID 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 95 MALWDIKSQLAGMPLYQLFGGKSRdAIPAYSHASGDTLDALFASVDGLIEQGYRHIRCQLGFyggtpsglhapenPTpga 174
Cdd:cd03321 106 MAAWDALAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGY-------------PT--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 175 wfdqqeyMRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSCVPLA 254
Cdd:cd03321 169 -------ADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 255 MGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWHgpgdmtpIGVAVNTHLnihLHNAAIQE 334
Cdd:cd03321 242 MGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH-------LFQEISAHL---LAVTPTAH 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 1821659268 335 FIPRSAMTDRVFPGAPEVKEGFIYPPVNAGIGVGFNEA 372
Cdd:cd03321 312 WLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREK 349
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
21-372 |
1.32e-20 |
|
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: 92.09 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 21 LVTVRVTTDqGVTGHGcatFQQRPLAVKTLVEEYLQPLLTGRDANNIEDLWQMMnVNAYWRNGP--VMNNAISGVDMALW 98
Cdd:cd03328 30 LVLVEVRAG-GRTGLG---YTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAM-QRAVRNAGRpgVAAMAISAVDIALW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 99 DIKSQLAGMPLYQLFGgKSRDAIPAYshASGD----TLDALFASVDGLIEQGYRHIRCQLGfyggtpsglhapENPtpga 174
Cdd:cd03328 105 DLKARLLGLPLARLLG-RAHDSVPVY--GSGGftsyDDDRLREQLSGWVAQGIPRVKMKIG------------RDP---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 175 wfdqqeymRNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHSCVPL- 253
Cdd:cd03328 166 --------RRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAGMd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 254 -AMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRLAWH-GPGDMTPIGVAVNT--HLN-IHLH 328
Cdd:cd03328 238 iAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHcAPALHAHVACAVPRlrHLEwFHDH 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1821659268 329 NAAIQEFiprsamtdrvFPGAPEVKEGFIYP-PVNAGIGVGFNEA 372
Cdd:cd03328 318 VRIERML----------FDGAPDPSGGALRPdLSRPGLGLELRAR 352
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
18-367 |
1.18e-18 |
|
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: 86.52 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 18 RHNLVtVRVTTDQGVTGHG-CATFQQrPL-------AVKTLVEEYLQPLLTGRDANNIEDLwqmmnvnaYWRNGPVMNN- 88
Cdd:cd03317 24 REFLI-VELTDEEGITGYGeVVAFEG-PFyteetnaTAWHILKDYLLPLLLGREFSHPEEV--------SERLAPIKGNn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 89 -AISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPAYSHASGDTLDALFASVDGLIEQGYRHIRCQLgfyggtpsglhap 167
Cdd:cd03317 94 mAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQLLKQIERYLEEGYKRIKLKI------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 168 enpTPGaWfdqqeymrnTVDMFRALREKYGwSLHFLHDVHERLFPQQAVQLaKQLEPY------QPYFIEDILppqQSAW 241
Cdd:cd03317 161 ---KPG-W---------DVEPLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYgllmieQPLAADDLI---DHAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 242 L-EQVRqhscVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVrLAWHgpGDM--TPIGVA 318
Cdd:cd03317 223 LqKLLK----TPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI-PVWC--GGMleSGIGRA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821659268 319 VNTHLnihlhnAAIQEF-IP-------RSAMTDRVFPgAPEVKEGFIYPPVNAGIGV 367
Cdd:cd03317 296 HNVAL------ASLPNFtYPgdisassRYFEEDIITP-PFELENGIISVPTGPGIGV 345
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
91-323 |
4.91e-17 |
|
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: 80.46 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 91 SGVDMALWDIKSQLAGMPLYQLfGGKSRDAIP-AYSHASGDTLDALfASVDGLIEQGYRHIRCQLGFYGGtpsglhapen 169
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLL-LGGYRDRVRvAHMLGLGEPAEVA-EEARRALEAGFRTFKLKVGRDPA---------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 170 ptpgawfdqqeymrNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQSAWLEQVRQHS 249
Cdd:cd03315 114 --------------RDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARAT 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821659268 250 CVPLAMGELFNNPSEWHDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVRlAWHGPGDMTPIGVAVNTHL 323
Cdd:cd03315 180 DTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLP-VMVGSMIESGLGTLANAHL 252
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
144-249 |
1.31e-11 |
|
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: 60.37 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 144 EQGYRHIRCQLGFYGGtpsglhapenptpgawfdqqeymrNTVDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLE 223
Cdd:smart00922 14 EAGFRAVKVKVGGGPL------------------------EDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALD 69
|
90 100
....*....|....*....|....*.
gi 1821659268 224 PYQPYFIEDILPPQQSAWLEQVRQHS 249
Cdd:smart00922 70 ELGLEWIEEPVPPDDLEGLAELRRAT 95
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
89-380 |
7.79e-11 |
|
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: 63.18 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 89 AISGVDMALWDIKSQLAGMPLYQLFG-----GKSRDAIPAYS----HASGDTLDALFASVDGLIEQGYRHIRCQLGfygg 159
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAaggyYYPGDDLGRLRDEMRRYLDRGYTVVKIKIG---- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 160 tpsglhapenptpGAWFDQqeymrntvDMFR--ALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQ 237
Cdd:cd03326 185 -------------GAPLDE--------DLRRieAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 238 QSAWLEQVRQHSCVPLAMGE-LFNNPsEWHDLI----VNRRIDFIRCHVSQIGGITPALK-LAHLCQA-FGVRLAW-HGp 309
Cdd:cd03326 244 DYALQAELADHYDGPIATGEnLFSLQ-DARNLLryggMRPDRDVLQFDPGLSYGLPEYLRmLDVLEAHgWSRRRFFpHG- 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821659268 310 gdmtpiGVAVNTHLNIHLH----NAAIQEFIPRSAmtdrvFPGAPEVKEGFIYPPVNAGIGVgfnEALAQAHPVM 380
Cdd:cd03326 322 ------GHLMSLHIAAGLGlggnESYPDVFQPFGG-----FADGCKVENGYVRLPDAPGIGF---EGKAELAAEM 382
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
10-377 |
1.98e-08 |
|
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: 55.79 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 10 ECFITRpdrhNLVTVrvTTDQGVTGHG---------CATFQ-QRPLAVKTLVEEYLQPLLTGR----DANNIEDLWQMMN 75
Cdd:cd03323 25 EPFFTR----NIVEL--TDDNGNTGVGespggaealEALLEaARSLVGGDVFGAYLAVLESVRvafaDRDAGGRGLQTFD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 76 VNaywrngpVMNNAISGVDMALWDIKSQLAGMPLYQLFGGKSRDAIPA-----YSHASGDTLDALFASVDG-----LIEQ 145
Cdd:cd03323 99 LR-------TTVHVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPFlaylfYKGDRHKTDLPYPWFRDRwgealTPEG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 146 GYRHIRCQLGFYGGT----PSGLHAPEnptpgawfdqQEymrntVDMFRALREKY-----------GWSLhflhdvherl 210
Cdd:cd03323 172 VVRLARAAIDRYGFKsfklKGGVLPGE----------EE-----IEAVKALAEAFpgarlrldpngAWSL---------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 211 fpQQAVQLAKQLEPYQPYfIEDILPPQQSawLEQVRQHSCVPLAMgelfnnpsewhDLIVnrrIDF------IRCHVSQI 284
Cdd:cd03323 227 --ETAIRLAKELEGVLAY-LEDPCGGREG--MAEFRRATGLPLAT-----------NMIV---TDFrqlghaIQLNAVDI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 285 --------GGITPALKLAHLCQAFGVRLAWHGpgdmtpigvavNTHLNIHL----HNAA--------IQEFIPRSAmTDR 344
Cdd:cd03323 288 pladhhfwGGMRGSVRVAQVCETWGLGWGMHS-----------NNHLGISLammtHVAAaapglitaCDTHWIWQD-GQV 355
|
410 420 430
....*....|....*....|....*....|....
gi 1821659268 345 VFPGAPEVKEGFIYPPVNAGIGVGFN-EALAQAH 377
Cdd:cd03323 356 ITGEPLRIKDGKVAVPDKPGLGVELDrDKLAKAH 389
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
24-359 |
3.29e-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: 55.04 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 24 VRVTTD-QGVTGHGcATFQ-QRPLAVKTLVEEYLQPLLTGRDANNIEDlwqmmNVNAYWRN----------GP---VMNN 88
Cdd:cd03324 36 VVLRTDaAGLKGHG-LTFTiGRGNEIVCAAIEALAHLVVGRDLESIVA-----DMGKFWRRltsdsqlrwiGPekgVIHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 89 AISGVDMALWDIKSQLAGMPLYQLF-----------------------------------GGKSRDAI------PAYSHA 127
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqpGKAAREADllaegyPAYTTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 128 SG------DTLDALFASVdglIEQGYRHIRCQLGFyggtpsglhapenptpgawfDQQEYMRNTvdmfRALREKYGWSLH 201
Cdd:cd03324 190 AGwlgysdEKLRRLCKEA---LAQGFTHFKLKVGA--------------------DLEDDIRRC----RLAREVIGPDNK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 202 FLHDVHERLFPQQAVQLAKQLEPYQPYFIE------DILppQQSAWLEQVRQHScVPLAMGELFNNPSEWHDLIVNRRID 275
Cdd:cd03324 243 LMIDANQRWDVPEAIEWVKQLAEFKPWWIEeptspdDIL--GHAAIRKALAPLP-IGVATGEHCQNRVVFKQLLQAGAID 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 276 FIRCHVSQIGGITPALKLAHLCQAFGVRLAWHGPGdmtpIGVAvntHLNIHLhnaAIQEFIPRSA-MTDRVFPGAPEVKE 354
Cdd:cd03324 320 VVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGG----VGLC---ELVQHL---SMIDYICVSGsKEGRVIEYVDHLHE 389
|
....*
gi 1821659268 355 GFIYP 359
Cdd:cd03324 390 HFVYP 394
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
186-303 |
6.65e-06 |
|
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: 47.25 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821659268 186 VDMFRALREKYGWSLHFLHDVHERLFPQQAVQLAKQLEPYQPYFIEDILPPQQsaWLEQVRQHSCVPLAMGELFNNPSEW 265
Cdd:cd03320 114 LARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDD--LAELRRLAAGVPIALDESLRRLDDP 191
|
90 100 110
....*....|....*....|....*....|....*...
gi 1821659268 266 HDLIVNRRIDFIRCHVSQIGGITPALKLAHLCQAFGVR 303
Cdd:cd03320 192 LALAAAGALGALVLKPALLGGPRALLELAEEARARGIP 229
|
|
| |
