|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-381 |
0e+00 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 703.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 1 MKISDITVYKVKPRWIFVKISTDEGIDGWGEMISGTKTETVVAGAYEIGNRLIGRNPFEIERLFQEMHRS-FFRGGPING 79
Cdd:PRK14017 1 MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGgFYRGGPILM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 80 TIVSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNATEELHYIDSYKKV 159
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNGTEELQYIDSPRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 160 DEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTR 239
Cdd:PRK14017 161 DAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 240 WQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPYGPVALAATLQVDSCTPNVFIQEQSLGIHYNKG 319
Cdd:PRK14017 241 WDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488291624 320 FDLLDFVKNKEVFQYKDGYVDLPSKPGLGLEMDEDRIKEISQEGLVWTNPQWKNYDGTIAEW 381
Cdd:PRK14017 321 ADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNPVWRHADGSVAEW 382
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-352 |
0e+00 |
|
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: 529.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 2 KISDITVYKVKPRWIFVKISTDEGIDGWGEMISGTKTETVVAGAYEIGNRLIGRNPFEIERLFQEMHR-SFFRGGPINGT 80
Cdd:cd03325 1 KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRgGFYRGGPVLMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 81 IVSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNATEELHYIDSYKKVD 160
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELQWIDTSKKVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 161 EVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRW 240
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 241 QFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPYGPVALAATLQVDSCTPNVFIQEQSLGIHYNKGF 320
Cdd:cd03325 241 DFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGD 320
|
330 340 350
....*....|....*....|....*....|..
gi 488291624 321 DLLDFVKNKEVFQYKDGYVDLPSKPGLGLEMD 352
Cdd:cd03325 321 DLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-358 |
8.60e-129 |
|
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: 374.16 E-value: 8.60e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 1 MKISDITVYKVKP----------------RWIFVKISTDEGIDGWGEMI-SGTKTETVVAGAYE-IGNRLIGRNPFEIER 62
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftisrgtrterDVVLVRVETDDGITGWGEAVpGGTGAEAVAAALEEaLAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 63 LFQEMHRSFFrggpINGTIVSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAV 142
Cdd:COG4948 81 LWQRLYRALP----GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 143 KMNATEElhyidsykKVDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEV 222
Cdd:COG4948 157 KLKVGGP--------DPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 223 ADAVAVPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPY-GPVALAATLQVDSC 301
Cdd:COG4948 229 RRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAALHLAAA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488291624 302 TPNVFIQEQSLGIHYNKgfDLLdfvknKEVFQYKDGYVDLPSKPGLGLEMDEDRIKE 358
Cdd:COG4948 309 LPNFDIVELDGPLLLAD--DLV-----EDPLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-350 |
5.63e-127 |
|
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: 369.25 E-value: 5.63e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 2 KISDITVYKVKP------------RWIFVKISTDEGIDGWGEMISGTKTETVVAG-AYEIGNRLIGRNPFEIERLFQEMH 68
Cdd:cd03316 1 KITDVETFVLRVplpepggavtwrNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAiEDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 69 RSFF---RGGPINGTIvSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGG--DRPSEVAEQAQDRFDRGFTAVK 143
Cdd:cd03316 81 RRLFwrgRGGVAMAAI-SAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGydDSPEELAEEAKRAVAEGFTAVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 144 MNATEELHYIdsyKKVDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVA 223
Cdd:cd03316 160 LKVGGPDSGG---EDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 224 DAVAVPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPYGPVALAATLQVDSCTP 303
Cdd:cd03316 237 QATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAALP 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 488291624 304 NVFIQEqslgihYNKGFDLLDFVKNKEVFQYKDGYVDLPSKPGLGLE 350
Cdd:cd03316 317 NFGILE------YHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
126-355 |
4.14e-86 |
|
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: 260.19 E-value: 4.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 126 EVAEQAQDRFDR-GFTAVKMNATEElhyidsykKVDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHP 204
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGP--------DPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 205 MFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPH 284
Cdd:pfam13378 73 LWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488291624 285 APYGPVALAATLQVDSCTPNVFIQEQSLGIHYnkgfdlLDFVKNKEVFQYKDGYVDLPSKPGLGLEMDEDR 355
Cdd:pfam13378 153 SGGGPIGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
15-352 |
1.79e-70 |
|
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: 224.52 E-value: 1.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 15 WIFVKISTDEGIDGWGEMISGTktetVVAGAYEIGNR--LIGRNPFEIERLFQEMHRS--FFRGGPINGTIVSGLEMALW 90
Cdd:cd03327 11 WLFVEIETDDGTVGYANTTGGP----VACWIVDQHLArfLIGKDPSDIEKLWDQMYRAtlAYGRKGIAMAAISAVDLALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 91 DIKGKAFNVPVYELLGGAARDNIKVY-SWIGGDRPSEVAEQAQDRFDRGFTAVKMnateELHY--IDSYKKVDEVVERVA 167
Cdd:cd03327 87 DLLGKIRGEPVYKLLGGRTRDKIPAYaSGLYPTDLDELPDEAKEYLKEGYRGMKM----RFGYgpSDGHAGLRKNVELVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 168 SIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRWQFKNIFK 247
Cdd:cd03327 163 AIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 248 QGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHApygpvALAATLQVDSCTPNVFIQEqslgihYnkgFDLLDFVK 327
Cdd:cd03327 243 GRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA-----SQIYNYHFIMSEPNSPFAE------Y---LPNSPDEV 308
|
330 340 350
....*....|....*....|....*....|...
gi 488291624 328 NKEVFQY--------KDGYVDLPSKPGLGLEMD 352
Cdd:cd03327 309 GNPLFYYiflnepvpVNGYFDLSDKPGFGLELN 341
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-381 |
3.23e-62 |
|
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: 203.83 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 2 KISDITVYKVKPRWIFV--KISTDEGIDGWGEMISGTKTETVVAGAYE-IGNRLIGRNPFEIERLFQEMHR-SFFRGGPI 77
Cdd:cd03322 1 KITAIEVIVTCPGRNFVtlKITTDQGVTGLGDATLNGRELAVKAYLREhLKPLLIGRDANRIEDIWQYLYRgAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 78 NGTIVSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNATeelhyidsyk 157
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQLP---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 158 KVDEVVervasiRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLY 237
Cdd:cd03322 151 KLFEAV------REKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 238 TRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAP--YGPVALAATLQVDSCTPNVFIQEQSlgiH 315
Cdd:cd03322 225 SIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdLSPVGMAAALHLDLWVPNFGIQEYM---R 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 316 YNKgfdlldfvKNKEVF----QYKDGYVDLPSKPGLGLEMDEDRIKEISQEGLVWtnPQWKNYDGTIAEW 381
Cdd:cd03322 302 HAE--------ETLEVFphsvRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYL--PVARLEDGTVHNW 361
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-354 |
3.79e-56 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 188.96 E-value: 3.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 1 MKISDITVYKVKPRWIFV--KISTDEGIDGWGE-MISGTktETVVAgAY---EIGNRLIGRNPFEIERLFQEMHR-SFFR 73
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFVtlKITTDDGVTGLGDaTLNGR--ELAVA-SYlqdHVCPLLIGRDAHRIEDIWQYLYRgAYWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 74 GGPINGTIVSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNA------- 146
Cdd:PRK15072 78 RGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQCgvpglkt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 147 ---------------------TEELHyiDSYKKVDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPM 205
Cdd:PRK15072 158 tygvskgkglayepatkgllpEEELW--STEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 206 FLEEVVLPENEEHYKEVADAVAVPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHA 285
Cdd:PRK15072 236 WLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488291624 286 P--YGPVALAATLQVDSCTPNVFIQEqslgihYNKGFDLLDfvknkEVFQ----YKDGYVDLPSKPGLGLEMDED 354
Cdd:PRK15072 316 PtdLSPVCMAAALHFDLWVPNFGIQE------YMGHSEETL-----EVFPhsytFEDGYLHPGDAPGLGVDFDEK 379
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
1-304 |
6.23e-44 |
|
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: 152.10 E-value: 6.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 1 MKISDITVYKVKprWIFVKISTDEGIDGWGEMISGtktetvvagayeignrligrnpfeierlfqemhrsffrggpingt 80
Cdd:cd00308 14 FYLAGGTADTND--TVLVKLTTDSGVVGWGEVISG--------------------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 81 ivsgLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSWIggdrpsevaeqaqdrfdrgftavkmnateelhyidsykkvd 160
Cdd:cd00308 47 ----IDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI----------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 161 evvERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATgERLYTRW 240
Cdd:cd00308 82 ---ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA-DESVTTV 157
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488291624 241 QFKNIF-KQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPYG-PVALAATLQVDSCTPN 304
Cdd:cd00308 158 DDALEAlELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAALPN 223
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-357 |
8.24e-43 |
|
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: 152.86 E-value: 8.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 18 VKISTDEGIDGWGEMIS------GTKTetvVAGAYEIGNR-----LIGRNPFEIERLFQEMHRSFFRggpiNGTIVSGLE 86
Cdd:cd03318 33 VRLTTSDGVVGIGEATTpggpawGGES---PETIKAIIDRylaplLIGRDATNIGAAMALLDRAVAG----NLFAKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 87 MALWDIKGKAFNVPVYELLGGAARDNIKVySWI--GGDRPSEVAEQAQDRFDRGFTA--VKMNAteelhyidsyKKVDEV 162
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGRVRDSLPV-AWTlaSGDTERDIAEAEEMLEAGRHRRfkLKMGA----------RPPADD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 163 VERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRWQF 242
Cdd:cd03318 175 LAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 243 KNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMavaphAPYG------PVALAATLQVDSCTPNVfiqeqSLGIHY 316
Cdd:cd03318 255 FELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGI-----ALYGgtmlesSIGTAASAHLFATLPSL-----PFGCEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488291624 317 NKGFDLLDFVKNkEVFQYKDGYVDLPSKPGLGLEMDEDRIK 357
Cdd:cd03318 325 FGPLLLAEDLLE-EPLAYRDGELHVPTGPGLGVRLDEDKVR 364
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
50-284 |
2.49e-38 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 141.79 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 50 NRLI-GRNPFEIERLFQEMHRS---FFRGGPINGTIvSGLEMALWDIKGKAFNVPVYELLGGAARDNIKVYSwiGGDRPs 125
Cdd:PRK15440 90 NRFIeGKCVSDIELIWDQMLNAtlyYGRKGLVMNTI-SCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFYA--TGARP- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 126 EVAEQAqdrfdrGFTAVKMnateELHY--IDSYKKVDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFH 203
Cdd:PRK15440 166 DLAKEM------GFIGGKM----PLHHgpADGDAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 204 PMFLEEVVLPENEEHYKEVADAVAVPL--ATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAV 281
Cdd:PRK15440 236 LKWIEECLPPDDYWGYRELKRNAPAGMmvTSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLV 315
|
...
gi 488291624 282 APH 284
Cdd:PRK15440 316 VPH 318
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
18-358 |
3.42e-36 |
|
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: 135.22 E-value: 3.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 18 VKISTDEGIDGwgEMISGTKTETVVAGAYEIGNRLIGRNPFEIERLFQEMHRsFFRGGPINGtiVSGLEMALWDIKGKAF 97
Cdd:cd03329 37 LTIETDEGAKG--HAFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQDLWR-LQRGLTDRG--LGLVDIALWDLAGKYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 98 NVPVYELLGGaARDNIKVY--SWIGGDR-----PSEVAEQAQDRFDRGFTAVKMNAteelhYIDSYKKVDevVERVASIR 170
Cdd:cd03329 112 GLPVHRLLGG-YREKIPAYasTMVGDDLeglesPEAYADFAEECKALGYRAIKLHP-----WGPGVVRRD--LKACLAVR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 171 ERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTR-WQFKNIFKQG 249
Cdd:cd03329 184 EAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGAlESRADWVLAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 250 AIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAPYgpvalAATLQVDSCTPNVFIQEQSLgIHYNKGF--------D 321
Cdd:cd03329 264 ATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNG-----AANLHVIAAIRNTRYYERGL-LHPSQKYdvyagylsV 337
|
330 340 350
....*....|....*....|....*....|....*..
gi 488291624 322 LLDFVKNkevfqykDGYVDLPSKPGLGLEMDEDRIKE 358
Cdd:cd03329 338 LDDPVDS-------DGFVHVPKGPGLGVEIDFDYIER 367
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
18-361 |
1.63e-26 |
|
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: 109.33 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 18 VKISTDEGIDGWGEMISGTKTetvVAGAYEIGNRLIGRNPF-EIERLFQEMHRSFF-RGGPINGT----------IVSGL 85
Cdd:cd03323 33 VELTDDNGNTGVGESPGGAEA---LEALLEAARSLVGGDVFgAYLAVLESVRVAFAdRDAGGRGLqtfdlrttvhVVTAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 86 EMALWDIKGKAFNVPVYELLGGAARDNIKV----------------YSWIgGDRPSEV---------AEQAQDRFdrGFT 140
Cdd:cd03323 110 EVALLDLLGQALGVPVADLLGGGQRDSVPFlaylfykgdrhktdlpYPWF-RDRWGEAltpegvvrlARAAIDRY--GFK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 141 AVKMNAteelhyidsykKV---DEVVERVASIRERFGDAmDIGVDFHG--------RVHKPMAKVLAkalepfhpmFLEE 209
Cdd:cd03323 187 SFKLKG-----------GVlpgEEEIEAVKALAEAFPGA-RLRLDPNGawsletaiRLAKELEGVLA---------YLED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 210 VVLpeNEEHYKEVADAVAVPLATgERLYTRW-QFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPHAP-- 286
Cdd:cd03323 246 PCG--GREGMAEFRRATGLPLAT-NMIVTDFrQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNnh 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488291624 287 YGpVALAATLQVDSCTPNvfiQEQSLGIHYNKGFDllDFVKnKEVFQYKDGYVDLPSKPGLGLEMDEDRIKEISQ 361
Cdd:cd03323 323 LG-ISLAMMTHVAAAAPG---LITACDTHWIWQDG--QVIT-GEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHE 390
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
16-357 |
2.71e-26 |
|
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: 107.95 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 16 IFVKISTDEGIDGWGEMISGTKTETVVAGAY--EIGNRLIGRN--PFEIERLFQEMHRSFFRGGpINGTIVSGLEMALWD 91
Cdd:cd03321 32 VLIDLATDEGVTGHSYLFTYTPAALKSLKQLldDMAALLVGEPlaPAELERALAKRFRLLGYTG-LVRMAAAGIDMAAWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 92 IKGKAFNVPVYELLGGAARDnIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNAteelhyidSYKKVDEVVERVASIRE 171
Cdd:cd03321 111 ALAKVHGLPLAKLLGGNPRP-VQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKI--------GYPTADEDLAVVRSIRQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 172 RFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRWQFKNIFKQGAI 251
Cdd:cd03321 182 AVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGAC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 252 DIIQPDVALCGGILETRKIAAMAEAHDMAVAPHapygpVALAATLQVDSCTPNVfiqeqslgiHYNKGFDLLDFVKnKEV 331
Cdd:cd03321 262 DLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH-----LFQEISAHLLAVTPTA---------HWLEYVDWAGAIL-EPP 326
|
330 340
....*....|....*....|....*.
gi 488291624 332 FQYKDGYVDLPSKPGLGLEMDEDRIK 357
Cdd:cd03321 327 LKFEDGNAVIPDEPGNGIIWREKAVR 352
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
83-281 |
4.39e-26 |
|
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: 105.50 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 83 SGLEMALWDIKGKAFNVPVYELLGGAaRDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMNAteelhyidsykKVDEV 162
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKV-----------GRDPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 163 --VERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVAVPLATGERLYTRW 240
Cdd:cd03315 114 rdVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPH 193
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488291624 241 QFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAV 281
Cdd:cd03315 194 DAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPV 234
|
|
| 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 ... |
18-281 |
6.78e-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: 106.12 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 18 VKISTDeGIDGWGE-----MISGTKTETVVAGAYEIGNRLIGRNpFEIERLFQEMHRSFfrggPINGTIVSGLEMALWDI 92
Cdd:cd03319 30 VEIELD-GITGYGEaaptpRVTGETVESVLAALKSVRPALIGGD-PRLEKLLEALQELL----PGNGAARAAVDIALWDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 93 KGKAFNVPVYELLGGAARDNIKVYSWIGGDRPSEVAEQAQDRFDRGFTAVKMnateelhyidsykKVD----EVVERVAS 168
Cdd:cd03319 104 EAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKI-------------KLGgdleDDIERIRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 169 IRERFGDAMdIGVDfhgrvhkpmA------KVLAKALEPFHPM---FLEEVVLPENEEHYKEVADAVAVPLATGERLYTR 239
Cdd:cd03319 171 IREAAPDAR-LRVD---------AnqgwtpEEAVELLRELAELgveLIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488291624 240 WQFKNIFKQGAIDIIqpDVAL--CGGILETRKIAAMAEAHDMAV 281
Cdd:cd03319 241 ADAARLAGGGAYDGI--NIKLmkTGGLTEALRIADLARAAGLKV 282
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
82-360 |
4.61e-23 |
|
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: 99.39 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 82 VSGLEMALWDIKGKAFNVPVYELLG-----GAARDNIKVYSWIGGDRPSEVAEQAQDRF----DRGFTAVKMnateelhy 152
Cdd:cd03326 110 VGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAAGGYYYPGDDLGRLRDEMrrylDRGYTVVKI-------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 153 idsykKV-----DEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVA 227
Cdd:cd03326 182 -----KIggaplDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 228 VPLATGERLYTRWQFKNIFKQGAI----DIIQPDVALCGGILETRKIAAMAEAHDM---AVAPHAPYG-PVALAATLQVD 299
Cdd:cd03326 257 GPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGWsrrRFFPHGGHLmSLHIAAGLGLG 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488291624 300 SC--TPNVFiqeQSLGihynkGFDllDFVKnkevfqYKDGYVDLPSKPGLGLEMDEDRIKEIS 360
Cdd:cd03326 337 GNesYPDVF---QPFG-----GFA--DGCK------VENGYVRLPDAPGIGFEGKAELAAEMR 383
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
52-295 |
2.37e-22 |
|
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: 96.71 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 52 LIGRNPFEIERLFQEMHRSFFRGGP--INGTIVSGLEMALWDIKGKAFNVPVYELLGgAARDNIKVYSwIGG---DRPSE 126
Cdd:cd03328 64 VEGRDALDPPAAWEAMQRAVRNAGRpgVAAMAISAVDIALWDLKARLLGLPLARLLG-RAHDSVPVYG-SGGftsYDDDR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 127 VAEQAQDRFDRGFTAVKMNateelhyIDSYKKVDevVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPFHPMF 206
Cdd:cd03328 142 LREQLSGWVAQGIPRVKMK-------IGRDPRRD--PDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 207 LEEVVLPENEEHYKEVADA--VAVPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAVAPH 284
Cdd:cd03328 213 FEEPVSSDDLAGLRLVRERgpAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH 292
|
250
....*....|....
gi 488291624 285 -APY--GPVALAAT 295
Cdd:cd03328 293 cAPAlhAHVACAVP 306
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
12-106 |
6.02e-17 |
|
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: 75.97 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 12 KPRWIFVKISTDEGIDGWGEMISGTKTETVVAGAYE--IGNRLIGRNPFEIERLFQEMhrsfFRGGPINGTIVSGLEMAL 89
Cdd:pfam02746 25 QQSLVIVRIETSEGVVGIGEATSYGGRAETIKAILDdhLAPLLIGRDAANISDLWQLM----YRAALGNMSAKAAIDMAL 100
|
90
....*....|....*..
gi 488291624 90 WDIKGKAFNVPVYELLG 106
Cdd:pfam02746 101 WDLKAKVLNLPLADLLG 117
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-351 |
7.42e-17 |
|
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: 81.62 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 17 FVKISTDE-GIDGWGEMIS-GTKTETVVAGAYEIGNRLIGRNpfeIERLFQEMhRSFFRG----------GPINGTI--- 81
Cdd:cd03324 35 YVVLRTDAaGLKGHGLTFTiGRGNEIVCAAIEALAHLVVGRD---LESIVADM-GKFWRRltsdsqlrwiGPEKGVIhla 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 82 VSGLEMALWDIKGKAFNVPVYELL-----------------------------------GGAAR------DNIKVYS--- 117
Cdd:cd03324 111 TAAVVNAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqpGKAAReadllaEGYPAYTtsa 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 118 -WIG-GDrpSEVAEQAQDRFDRGFTAVKMnateelhyidsykKVDEVVE----RVASIRERFGDAMDIGVDFHGRVHKPM 191
Cdd:cd03324 191 gWLGySD--EKLRRLCKEALAQGFTHFKL-------------KVGADLEddirRCRLAREVIGPDNKLMIDANQRWDVPE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 192 AKVLAKALEPFHPMFLEEVVLPENEEHYKEVADAVA---VPLATGERLYTRWQFKNIFKQGAIDIIQPDVALCGGILETR 268
Cdd:cd03324 256 AIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAplpIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 269 KIAAMAEAHDMAVAPHApyGPVALaatlqvdsCTpnvFIQEQSLgIHY-----NKGFDLLDFVKN-KEVFQY----KDGY 338
Cdd:cd03324 336 AVLLMAAKFGVPVCPHA--GGVGL--------CE---LVQHLSM-IDYicvsgSKEGRVIEYVDHlHEHFVYpvviQNGA 401
|
410
....*....|...
gi 488291624 339 VDLPSKPGLGLEM 351
Cdd:cd03324 402 YMPPTDPGYSIEM 414
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
124-228 |
1.68e-16 |
|
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: 74.24 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 124 PSEVAEQAQDRF-DRGFTAVKMNATEELhyidsykkvDEVVERVASIRERFGDAMDIGVDFHGRVHKPMAKVLAKALEPF 202
Cdd:smart00922 1 PEELAEAARRAVaEAGFRAVKVKVGGGP---------LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDEL 71
|
90 100
....*....|....*....|....*.
gi 488291624 203 HPMFLEEVVLPENEEHYKEVADAVAV 228
Cdd:smart00922 72 GLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
16-358 |
2.38e-16 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 79.59 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 16 IFVKISTDEGIDGWGEMISGTK---TETVVAGAYEI-----GNRLIGR---NPFEIERLFQemhrsFFRGGPIngtIVSG 84
Cdd:cd03317 27 LIVELTDEEGITGYGEVVAFEGpfyTEETNATAWHIlkdylLPLLLGRefsHPEEVSERLA-----PIKGNNM---AKAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 85 LEMALWDIKGKAFNVPVYELLGGaARDNIKVYSWIGGDRPSEV-AEQAQDRFDRGFTAVKMNateelhyIDSYKKVdEVV 163
Cdd:cd03317 99 LEMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQlLKQIERYLEEGYKRIKLK-------IKPGWDV-EPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 164 ERVasiRERFGDAMdIGVDFHGRVHKPMAKVLaKALEPFHPMFLEEvVLPENE--EHyKEVADAVAVPLATGERLYTRWQ 241
Cdd:cd03317 170 KAV---RERFPDIP-LMADANSAYTLADIPLL-KRLDEYGLLMIEQ-PLAADDliDH-AELQKLLKTPICLDESIQSAED 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488291624 242 FKNIFKQGAIDIIQPDVALCGGILETRKIAAMAEAHDMAV------------APHapygpVALAA----TLQVD-SCTPN 304
Cdd:cd03317 243 ARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVwcggmlesgigrAHN-----VALASlpnfTYPGDiSASSR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488291624 305 VFIQeqslgihynkgfdllDFVKNKevFQYKDGYVDLPSKPGLGLEMDEDRIKE 358
Cdd:cd03317 318 YFEE---------------DIITPP--FELENGIISVPTGPGIGVTVDREALKK 354
|
|
| |
