|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-378 |
1.32e-121 |
|
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: 356.15 E-value: 1.32e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 2 KITKIET--LEIDLSGQNGLDLWRP-IYVRIHTDEGISGMGEASLAYGtaSEAIAPMIRILAERFLLGQDPNDTETLWEI 78
Cdd:cd03316 1 KITDVETfvLRVPLPEPGGAVTWRNlVLVRVTTDDGITGWGEAYPGGR--PSAVAAAIEDLLAPLLIGRDPLDIERLWEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 79 MRQRSFWAlGGGPVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCYASQLHFGWtdeslmlnDPAEFRETAQI 158
Cdd:cd03316 79 LYRRLFWR-GRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDD--------SPEELAEEAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 159 ARAEGYDCVKLCPVYVDANGERIRkrgvftpaerkLARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNIL 238
Cdd:cd03316 150 AVAEGFTAVKLKVGGPDSGGEDLR-----------EDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 239 FMEEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHN 318
Cdd:cd03316 219 WFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 319 CGSPLAIAMALQFEAAIPNFEIHEHHSFNLKScNRELFEEDLQPVNGKIAVPVTPGFGMT 378
Cdd:cd03316 299 AGGPIGLAASLHLAAALPNFGILEYHLDDLPL-REDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-386 |
6.06e-105 |
|
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: 313.68 E-value: 6.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 1 MKITKIETLEIDL-------SGQNGLDLWRPIYVRIHTDEGISGMGEASlAYGTASEAIAPMIRILAERFLLGQDPNDTE 73
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftISRGTRTERDVVLVRVETDDGITGWGEAV-PGGTGAEAVAAALEEALAPLLIGRDPLDIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 74 TLWEIMRQRSFwalgggpVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCYASqlhfgwtdesLMLNDPAEFR 153
Cdd:COG4948 80 ALWQRLYRALP-------GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYAT----------LGIDTPEEMA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 154 ETAQIARAEGYDCVKLcpvyvdangerirKRGVFTPAErklARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFS 233
Cdd:COG4948 143 EEAREAVARGFRALKL-------------KVGGPDPEE---DVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 234 DLNILFMEEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVG 313
Cdd:COG4948 207 DLGLEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVP 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446627634 314 VQAHN-CGSPLAIAMALQFEAAIPNFEIHEHHSFNLksCNRELFEEDLQPVNGKIAVPVTPGFGMTLRKDAEKR 386
Cdd:COG4948 287 VMPHCmLESGIGLAAALHLAAALPNFDIVELDGPLL--LADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-379 |
5.62e-89 |
|
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: 272.66 E-value: 5.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 2 KITKIETLEIDLsgqngldlwRPIYVRIHTDEGISGMGEASLAyGTAsEAIAPMIRILaERFLLGQDPNDTETLWEIMRQ 81
Cdd:cd03325 1 KITKIETFVVPP---------RWLFVKIETDEGVVGWGEPTVE-GKA-RTVEAAVQEL-EDYLIGKDPMNIEHHWQVMYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 82 RSFWAlgGGPVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCYAsqlHFGwtdeslmLNDPAEFRETAQIARA 161
Cdd:cd03325 69 GGFYR--GGPVLMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYS---WIG-------GDRPSDVAEAARARRE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 162 EGYDCVKL-CPVYVdangerirkRGVFTPAERKLARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFM 240
Cdd:cd03325 137 AGFTAVKMnATEEL---------QWIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 241 EEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNCG 320
Cdd:cd03325 208 EEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPL 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446627634 321 SPLAIAMALQFEAAIPNFEIHEH----HSFNLKSCNRELFE-EDLQPVNGKIAVPVTPGFGMTL 379
Cdd:cd03325 288 GPIALAASLHVDASTPNFLIQEQslgiHYNEGDDLLDYLVDpEVFDMENGYVKLPTGPGLGIEI 351
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-387 |
2.26e-76 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 241.34 E-value: 2.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 1 MKITKIETLEIDLsgqngldlwRPIYVRIHTDEGISGMGEASLayGTASEAIAPMIRILAErFLLGQDPNDTETLWEIMR 80
Cdd:PRK14017 1 MKITKLETFRVPP---------RWLFLKIETDEGIVGWGEPVV--EGRARTVEAAVHELAD-YLIGKDPRRIEDHWQVMY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 81 QRSFWAlgGGPVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCYAsqlHFGWtdeslmlNDPAEFRETAQIAR 160
Cdd:PRK14017 69 RGGFYR--GGPILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYS---WIGG-------DRPADVAEAARARV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 161 AEGYDCVKLcpvyvdaNG-ERIRKrgVFTPAERKLARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILF 239
Cdd:PRK14017 137 ERGFTAVKM-------NGtEELQY--IDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 240 MEEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNC 319
Cdd:PRK14017 208 IEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCP 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446627634 320 GSPLAIAMALQFEAAIPNFEIHEH----HsFNLKScnrELFE-----EDLQPVNGKIAVPVTPGFGMTLRKDAEKRM 387
Cdd:PRK14017 288 LGPIALAACLQVDAVSPNAFIQEQslgiH-YNQGA---DLLDyvknkEVFAYEDGFVAIPTGPGLGIEIDEAKVRER 360
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
153-383 |
2.24e-64 |
|
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: 204.72 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 153 RETAQIARAEGYDCVKLcpvyvdangerirKRGVFTPAErklARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYF 232
Cdd:pfam13378 4 AEARRAVEARGFRAFKL-------------KVGGPDPEE---DVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 233 SDLNILFMEEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDV 312
Cdd:pfam13378 68 EELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446627634 313 GVQAHNCGSPLAIAMALQFEAAIPNFEIHEHHSFNLkSCNRELFEEDLQPVNGKIAVPVTPGFGMTLRKDA 383
Cdd:pfam13378 148 PVAPHSGGGPIGLAASLHLAAAVPNLLIQEYFLDPL-LLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
25-379 |
6.28e-57 |
|
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: 189.85 E-value: 6.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 25 IYVRIHTDEGISGMGEaslayGTASEAIAPMIRILAERFLLGQDPNDTETLWEIMRQRSFwALGGGPVIFGAMSALDAAL 104
Cdd:cd03327 12 LFVEIETDDGTVGYAN-----TTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATL-AYGRKGIAMAAISAVDLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 105 WDIKGRAAGLSVHRLLGAKTPAPLRCYASQLHFgwtdeslmlNDPAEFRETAQIARAEGYDCVKLCPVYVDANGERIRKR 184
Cdd:cd03327 86 WDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYP---------TDLDELPDEAKEYLKEGYRGMKMRFGYGPSDGHAGLRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 185 GVftpaerklarSRMEAVREGIGEECDIIIE-WNSLTsTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSRESSIPV 263
Cdd:cd03327 157 NV----------ELVRAIREAVGYDVDLMLDcYMSWN-LNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 264 ATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHncGSPLAiamALQFEAAIPNFEIHEH 343
Cdd:cd03327 226 STGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPH--ASQIY---NYHFIMSEPNSPFAEY 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446627634 344 HSFNLKSCNRELFEE----DLQPVNGKIAVPVTPGFGMTL 379
Cdd:cd03327 301 LPNSPDEVGNPLFYYiflnEPVPVNGYFDLSDKPGFGLEL 340
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-386 |
1.85e-43 |
|
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: 154.90 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 2 KITKIETLEIdlsgQNGLDLwrpIYVRIHTDEGISGMGEASLaygTASE-AIAPMIRILAERFLLGQDPNDTETLWEIMR 80
Cdd:cd03322 1 KITAIEVIVT----CPGRNF---VTLKITTDQGVTGLGDATL---NGRElAVKAYLREHLKPLLIGRDANRIEDIWQYLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 81 QRSFWAlgGGPVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCYAsqlHFGWTDESLMLNDPAEFretaqiaR 160
Cdd:cd03322 71 RGAYWR--RGPVTMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYS---HASGRDIPELLEAVERH-------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 161 AEGYDCVklcpvyvdangeRIRKRGVFtpaerklarsrmEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFM 240
Cdd:cd03322 139 AQGYRAI------------RVQLPKLF------------EAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 241 EEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNCG 320
Cdd:cd03322 195 EDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPT 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627634 321 --SPLAIAMALQFEAAIPNFEIHEHHSFNLKScnRELFEEDLQPVNGKIAVPVTPGFGMTLRKDAEKR 386
Cdd:cd03322 275 dlSPVGMAAALHLDLWVPNFGIQEYMRHAEET--LEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAK 340
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-379 |
1.36e-41 |
|
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: 150.24 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 2 KITKIETLEIDLSGQNGLDLWRP-----------IYVRIHTDEGISGmgEASLayGTASEAIAPMIRILAERfLLGQDPN 70
Cdd:cd03329 1 KITDVEVTVFEYPTQPVSFDGGHhhpgpagtrklALLTIETDEGAKG--HAFG--GRPVTDPALVDRFLKKV-LIGQDPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 71 DTETLWEIMRQRsfwaLGGGPVIfgAMSALDAALWDIKGRAAGLSVHRLLGA---KTPAplrcYASQLHFgwtDESLMLN 147
Cdd:cd03329 76 DRERLWQDLWRL----QRGLTDR--GLGLVDIALWDLAGKYLGLPVHRLLGGyreKIPA----YASTMVG---DDLEGLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 148 DPAEFRETAQIARAEGYDCVKLCPvYVDANGERirkrgvftpaERKLARsrmeAVREGIGEECDIIIEWNSLTSTSGALQ 227
Cdd:cd03329 143 SPEAYADFAEECKALGYRAIKLHP-WGPGVVRR----------DLKACL----AVREAVGPDMRLMHDGAHWYSRADALR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 228 LADYFSDLNILFMEEPTHYNSPEAQIKVSRESSIPVATGERLYTR-WGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHL 306
Cdd:cd03329 208 LGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGAlESRADWVLAGATDFLRADVNLVGGITGAMKTAHL 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627634 307 AHAFDVGVQAHNCGSPlaiamALQFEAAIPNFEIHEHH--SFNLKSCNRELFEEDLQ-PVN--GKIAVPVTPGFGMTL 379
Cdd:cd03329 288 AEAFGLDVELHGNGAA-----NLHVIAAIRNTRYYERGllHPSQKYDVYAGYLSVLDdPVDsdGFVHVPKGPGLGVEI 360
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
35-380 |
8.20e-30 |
|
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: 117.90 E-value: 8.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 35 ISGMGEASLAYGTASEAIAPMIRILAERFLLGQDPNDTETLWEIMrQRSFWALGGGPVIFGAMSALDAALWDIKGRAAGL 114
Cdd:cd03328 35 VRAGGRTGLGYTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAM-QRAVRNAGRPGVAAMAISAVDIALWDLKARLLGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 115 SVHRLLG-AKTPAPLrcYASQLHFGWTDESLmlndpaefreTAQIAR--AEGYDCVKLcpvyvdangerirKRGvfTPAE 191
Cdd:cd03328 114 PLARLLGrAHDSVPV--YGSGGFTSYDDDRL----------REQLSGwvAQGIPRVKM-------------KIG--RDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 192 RKLARSRmeAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPE--AQIKVSRESSIPVATGERL 269
Cdd:cd03328 167 RDPDRVA--AARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAglRLVRERGPAGMDIAAGEYA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 270 YTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHnCgsplAIAMALQFEAAIPNFE----IHEHHS 345
Cdd:cd03328 245 YTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH-C----APALHAHVACAVPRLRhlewFHDHVR 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 446627634 346 FnlkscNRELFEEDLQPVNGKIAV-PVTPGFGMTLR 380
Cdd:cd03328 320 I-----ERMLFDGAPDPSGGALRPdLSRPGLGLELR 350
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
39-382 |
5.33e-29 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 116.37 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 39 GEASLAYGTASEAIAPMIRILAERFLLGQDPNDTETLWEIMRQRSFWaLGGGPVIFGAMSALDAALWDIKGRAAGLSVHR 118
Cdd:PRK15440 68 GQVGFAVSTAGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLY-YGRKGLVMNTISCVDLALWDLLGKVRGLPVYK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 119 LLGAKTPAPLRCYASQlhfgwtdeslmlndpaefrETAQIARAEGYDCVKLCPVYVDANGERIRKRGVftpaerklarSR 198
Cdd:PRK15440 147 LLGGAVRDELQFYATG-------------------ARPDLAKEMGFIGGKMPLHHGPADGDAGLRKNA----------AM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 199 MEAVREGIGEECDIIIE-WNSLtSTSGALQLADYFSDLNILFMEEPThynSPE-----AQIKVSRESSIPVATGERLYTR 272
Cdd:PRK15440 198 VADMREKVGDDFWLMLDcWMSL-DVNYATKLAHACAPYGLKWIEECL---PPDdywgyRELKRNAPAGMMVTSGEHEATL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 273 WGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNCG------------SPLA--IAMALQFEAAIPNF 338
Cdd:PRK15440 274 QGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSvyshhfvitrtnSPFSefLMMSPDADTVVPQF 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446627634 339 eihehhsfnlkscNRELFEEDLqPVNGKIAVPV--TPGFGMTLRKD 382
Cdd:PRK15440 354 -------------DPILLDEPV-PVNGRIHKSVldKPGFGVELNRD 385
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-345 |
2.10e-28 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 115.01 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 1 MKITKIETLeIDLSGQNGLDLwrpiyvRIHTDEGISGMGEASL--------AYgtASEAIAPMirilaerfLLGQDPNDT 72
Cdd:PRK15072 1 MKIVDAEVI-VTCPGRNFVTL------KITTDDGVTGLGDATLngrelavaSY--LQDHVCPL--------LIGRDAHRI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 73 ETLWEIMRQRSFWAlgGGPVIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLRCY--ASqlhfGWTDESLmLNDPA 150
Cdd:PRK15072 64 EDIWQYLYRGAYWR--RGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYghAN----GRDIDEL-LDDVA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 151 EFREtaqiaraEGYDCVK-------LCPVYVDANGerirKRGVFTPAERKLARSR---------------MEAVREGIGE 208
Cdd:PRK15072 137 RHLE-------LGYKAIRvqcgvpgLKTTYGVSKG----KGLAYEPATKGLLPEEelwstekylrfvpklFEAVRNKFGF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 209 ECDII---------IEwnsltstsgALQLADYFSDLNILFMEEPTHYNSPEAQIKVSRESSIPVATGERLYTRWGFLPYL 279
Cdd:PRK15072 206 DLHLLhdvhhrltpIE---------AARLGKSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLI 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 280 QQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNCG--SPLAIAMALQFEAAIPNFEIHEH--HS 345
Cdd:PRK15072 277 EEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTdlSPVCMAAALHFDLWVPNFGIQEYmgHS 346
|
|
| 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 ... |
27-334 |
1.32e-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: 108.04 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 27 VRIHTDeGISGMGEAS-LAYGTAsEAIAPMIRILAE--RFLLGQDPNDTETLWEIMRqrsfwALGGGPvifGAMSALDAA 103
Cdd:cd03319 30 VEIELD-GITGYGEAApTPRVTG-ETVESVLAALKSvrPALIGGDPRLEKLLEALQE-----LLPGNG---AARAAVDIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 104 LWDIKGRAAGLSVHRLLGAKTPAPLRcyasqlhfgwTDESLMLNDPAEFRETAQIARAEGYDCVKlcpVYVDANGERIRK 183
Cdd:cd03319 100 LWDLEAKLLGLPLYQLWGGGAPRPLE----------TDYTISIDTPEAMAAAAKKAAKRGFPLLK---IKLGGDLEDDIE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 184 rgvftpaerklarsRMEAVREGIGeECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSRESSIPV 263
Cdd:cd03319 167 --------------RIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446627634 264 ATGERLYTRWGFLPYLQQGAIDMIqpDIGLV--GGITEGMKIAHLAHAFDVGVQahnCG----SPLAIAMALQFEAA 334
Cdd:cd03319 232 MADESCFSAADAARLAGGGAYDGI--NIKLMktGGLTEALRIADLARAAGLKVM---VGcmveSSLSIAAAAHLAAA 303
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
98-337 |
2.01e-23 |
|
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: 97.40 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 98 SALDAALWDIKGRAAGLSVHRLLGAKTpaplrcyasqlhfgwtdeslmlndpaefretaqiaraegYDCVklcPVYvdAN 177
Cdd:cd00308 45 SGIDMALWDLAAKALGVPLAELLGGGS---------------------------------------RDRV---PAY--GS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 178 GERIRkrgvftpaerklarsrmeAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSR 257
Cdd:cd00308 81 IERVR------------------AVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 258 ESSIPVATgERLYTRWGFLPY-LQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAH-NCGSPLAIAMALQFEAAI 335
Cdd:cd00308 143 RTGIPIAA-DESVTTVDDALEaLELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHgTLESSIGTAAALHLAAAL 221
|
..
gi 446627634 336 PN 337
Cdd:cd00308 222 PN 223
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
2-376 |
1.16e-21 |
|
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: 95.87 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 2 KITKIETLEI------DLSGQNGLDL---WRPIYVRIHTDE-GISGMGeASLAYGTASEAIAPMIRILAERfLLGQDpnd 71
Cdd:cd03324 2 KITALEVRDVrfptslELDGSDAMNPdpdYSAAYVVLRTDAaGLKGHG-LTFTIGRGNEIVCAAIEALAHL-VVGRD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 72 TETLWEIMRQrsFWALGG--------GP---VIFGAMSALDAALWDIKGRAAGLSVHRLLGAKTPAPLrcyASQLHFGW- 139
Cdd:cd03324 77 LESIVADMGK--FWRRLTsdsqlrwiGPekgVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEEL---VSCIDFRYi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 140 TD-----ESL-MLNDPAEFRET-AQIARAEGYDC---------------VKLCPVYVDANGERIR-KRGvftpAERKLAR 196
Cdd:cd03324 152 TDaltpeEALeILRRGQPGKAArEADLLAEGYPAyttsagwlgysdeklRRLCKEALAQGFTHFKlKVG----ADLEDDI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 197 SRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPThynSPE-----AQI-KVSRESSIPVATGERLY 270
Cdd:cd03324 228 RRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPT---SPDdilghAAIrKALAPLPIGVATGEHCQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 271 TRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNCGSPLA-----------IAMALQFEAAIPNF- 338
Cdd:cd03324 305 NRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCelvqhlsmidyICVSGSKEGRVIEYv 384
|
410 420 430
....*....|....*....|....*....|....*....
gi 446627634 339 -EIHEHhsfnlkscnrelFEEDLQPVNGKIAVPVTPGFG 376
Cdd:cd03324 385 dHLHEH------------FVYPVVIQNGAYMPPTDPGYS 411
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
98-321 |
8.80e-20 |
|
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: 88.17 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 98 SALDAALWDIKGRAAGLSVHRLLGAktpaplrcYASQLHFGWTdesLMLNDPAEFRETAQIARAEGYDCVKLcpvyvdan 177
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGG--------YRDRVRVAHM---LGLGEPAEVAEEARRALEAGFRTFKL-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 178 gerirKRGVftPAERKLARSRmeAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSR 257
Cdd:cd03315 107 -----KVGR--DPARDVAVVA--ALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALAR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446627634 258 ESSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVqahNCGS 321
Cdd:cd03315 178 ATDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPV---MVGS 238
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
27-386 |
1.69e-19 |
|
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: 88.91 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 27 VRIHTDEGISGMGEAS----LAYGTAS-EAIAPMIRILAERFLLGQDPNDTETLWEIMRQRSFWALGggpvifgAMSALD 101
Cdd:cd03318 33 VRLTTSDGVVGIGEATtpggPAWGGESpETIKAIIDRYLAPLLIGRDATNIGAAMALLDRAVAGNLF-------AKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 102 AALWDIKGRAAGLSVHRLLGAKtpapLRcyaSQLHFGWTdeslmLNDP---AEFRETAQIARAEGYDCVKLcpvyvdang 178
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGR----VR---DSLPVAWT-----LASGdteRDIAEAEEMLEAGRHRRFKL--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 179 erirKRGVFTPAErklARSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSRE 258
Cdd:cd03318 165 ----KMGARPPAD---DLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 259 SSIPVATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQ-AHNCGSPLAIAMALQFEAAIPN 337
Cdd:cd03318 238 NRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYgGTMLESSIGTAASAHLFATLPS 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446627634 338 FEiHEHHSFNLKSCNRELFEEDLQPVNGKIAVPVTPGFGMTLRKDAEKR 386
Cdd:cd03318 318 LP-FGCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
31-386 |
9.91e-18 |
|
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: 83.69 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 31 TDEGISGMGEASLAYGTASEAIAPMIRILAErfLLGQDPNDTETLWEIMRQRsFWALGGGPVIFGAMSALDAALWDIKGR 110
Cdd:cd03321 38 TDEGVTGHSYLFTYTPAALKSLKQLLDDMAA--LLVGEPLAPAELERALAKR-FRLLGYTGLVRMAAAGIDMAAWDALAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 111 AAGLSVHRLLGAKtPAPLRCYASQlhfgwtdeslmlndpaefretaqiaraeGYDCVKLCPvyvdANGERIRKRGvFTPA 190
Cdd:cd03321 115 VHGLPLAKLLGGN-PRPVQAYDSH----------------------------GLDGAKLAT----ERAVTAAEEG-FHAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 191 ERKLARSRME-------AVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPEAQIKVSRESSIPV 263
Cdd:cd03321 161 KTKIGYPTADedlavvrSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 264 ATGERLYTRWGFLPYLQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHncgspLAIAMALQFEAAIPNfeiheH 343
Cdd:cd03321 241 QMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH-----LFQEISAHLLAVTPT-----A 310
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446627634 344 HSFNLKSCNRELFEEDLQPVNGKIAVPVTPGFGMTLRKDAEKR 386
Cdd:cd03321 311 HWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
27-121 |
2.74e-15 |
|
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: 71.73 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 27 VRIHTDEGISGMGEASlAYGTASEAIAPMIRILAERFLLGQDPNDTETLWEIMRQRSFWALGggpvifgAMSALDAALWD 106
Cdd:pfam02746 31 VRIETSEGVVGIGEAT-SYGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALGNMS-------AKAAIDMALWD 102
|
90
....*....|....*
gi 446627634 107 IKGRAAGLSVHRLLG 121
Cdd:pfam02746 103 LKAKVLNLPLADLLG 117
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
27-383 |
1.88e-12 |
|
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: 68.12 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 27 VRIHTDEGISGMGEAslaYGTAS--EAIAPMIRILAERFLLGQDPNDTETLWEIMRQRSfwALGGGPVIFG------AMS 98
Cdd:cd03323 33 VELTDDNGNTGVGES---PGGAEalEALLEAARSLVGGDVFGAYLAVLESVRVAFADRD--AGGRGLQTFDlrttvhVVT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 99 ALDAALWDIKGRAAGLSVHRLLGAK--TPAPLRCYasqLHFGWTDESLMLNDPA------EFRETAQIAR-AE------G 163
Cdd:cd03323 108 AFEVALLDLLGQALGVPVADLLGGGqrDSVPFLAY---LFYKGDRHKTDLPYPWfrdrwgEALTPEGVVRlARaaidryG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 164 YDCVKLcpvyvdangerirKRGVFTPAERKLArsrMEAVREGIgEECDIIIEWNSLTSTSGALQLADYFSDLNiLFMEEP 243
Cdd:cd03323 185 FKSFKL-------------KGGVLPGEEEIEA---VKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGVL-AYLEDP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 244 ThyNSPEAQIKVSRESSIPVATgERLYTRWGFLPY-LQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQAHNcGSP 322
Cdd:cd03323 247 C--GGREGMAEFRRATGLPLAT-NMIVTDFRQLGHaIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHS-NNH 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446627634 323 LAI--AMALQFEAAIPN----FEIHEHHSfnlksCNRELFEEDLQPVNGKIAVPVTPGFGMTLRKDA 383
Cdd:cd03323 323 LGIslAMMTHVAAAAPGlitaCDTHWIWQ-----DGQVITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
149-261 |
1.44e-09 |
|
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: 54.59 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 149 PAEFRETAQIARAE-GYDCVKlcpvyvdangerirkrgVFTPAERKLARSRMEAVREGIGEECDIIIEWNSLTSTSGALQ 227
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVK-----------------VKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIR 63
|
90 100 110
....*....|....*....|....*....|....
gi 446627634 228 LADYFSDLNILFMEEPTHYNSPEAQIKVSRESSI 261
Cdd:smart00922 64 ALEALDELGLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
23-386 |
1.23e-08 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 56.09 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 23 RPIY-VRIHTDEGISGMGEASLA----YGtaSEAIAPMIRILAERF---LLGQDPNDTETLWEImrqrsFWALGGGPVif 94
Cdd:cd03317 24 REFLiVELTDEEGITGYGEVVAFegpfYT--EETNATAWHILKDYLlplLLGREFSHPEEVSER-----LAPIKGNNM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 95 gAMSALDAALWDIKGRAAGLSVHRLLGaktpaplrcyasqlhfGWTDE-----SLMLNDPAEfrETA-QIARA--EGYDC 166
Cdd:cd03317 95 -AKAGLEMAVWDLYAKAQGQSLAQYLG----------------GTRDSipvgvSIGIQDDVE--QLLkQIERYleEGYKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 167 VKLcpvyvdangeRIRKRGVFTPaerklarsrMEAVREGIGeecDI--IIEWNSltstsgALQLADY-----FSDLNILF 239
Cdd:cd03317 156 IKL----------KIKPGWDVEP---------LKAVRERFP---DIplMADANS------AYTLADIpllkrLDEYGLLM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 240 MEEPTHYNSPEAQIKVSRESSIPVATGERLYT----RWGFlpylQQGAIDMIQPDIGLVGGITEGMKIAHLAHAFDVGVQ 315
Cdd:cd03317 208 IEQPLAADDLIDHAELQKLLKTPICLDESIQSaedaRKAI----ELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVW 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 316 ahnCGSPL------AIAMALqfeAAIPNF----EIhehhsfnlkSCNRELFEEDL--QPV---NGKIAVPVTPGFGMTLR 380
Cdd:cd03317 284 ---CGGMLesgigrAHNVAL---ASLPNFtypgDI---------SASSRYFEEDIitPPFeleNGIISVPTGPGIGVTVD 348
|
....*.
gi 446627634 381 KDAEKR 386
Cdd:cd03317 349 REALKK 354
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
96-387 |
2.09e-07 |
|
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: 52.40 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 96 AMSALDAALWDIKGRAAGLSVHRLL----GAKTPAP-LRCYASQLHFGWTDESLMLNDpaEFRETAqiarAEGYDCVKLc 170
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLarryGRGQADPrVPVYAAGGYYYPGDDLGRLRD--EMRRYL----DRGYTVVKI- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 171 pvyvdangerirKRGVFTPAERklaRSRMEAVREGIGEECDIIIEWNSLTSTSGALQLADYFSDLNILFMEEPTHYNSPE 250
Cdd:cd03326 182 ------------KIGGAPLDED---LRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627634 251 AQIKVSRESSIPVATGERLYTRWGFLPYLQQGAI----DMIQPDIGLVGGITEGMKIAHL--AHAFDVGvQAHNCGSPLa 324
Cdd:cd03326 247 LQAELADHYDGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVleAHGWSRR-RFFPHGGHL- 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446627634 325 iaMALQFEAAIpnfeihehhsfNLKSCnrELFEEDLQPV----------NGKIAVPVTPGFGMTLRKDAEKRM 387
Cdd:cd03326 325 --MSLHIAAGL-----------GLGGN--ESYPDVFQPFggfadgckveNGYVRLPDAPGIGFEGKAELAAEM 382
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