|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-380 |
1.17e-119 |
|
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: 351.14 E-value: 1.17e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 2 KITELETVRVR----------DFPNILWVRIHTDEGLVGLGETFFM--AQTVETYIHEVVAPKLVGRDPLEIDRISKDLT 69
Cdd:cd03316 1 KITDVETFVLRvplpepggavTWRNLVLVRVTTDDGITGWGEAYPGgrPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 70 GYLGFRS-TGAEMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTcagntymrdakgqqtanygigGPRRDYD 148
Cdd:cd03316 81 RRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYAS---------------------GGGYDDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 149 dlngfLERADELAEDLLSEGITAMKIWPfdiaaeksGGQYISGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAI 228
Cdd:cd03316 140 -----PEELAEEAKRAVAEGFTAVKLKV--------GGPDSGGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 229 QIARALEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTM 308
Cdd:cd03316 207 RLARALEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAAL 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504345021 309 AEAWHLPVAPHDCTGPVVLAASTHLSLNAPNALVQESVRAYYKTWYaDLTTQLPTVTNGMITIPPGAGHGVD 380
Cdd:cd03316 287 AEAHGVRVAPHGAGGPIGLAASLHLAAALPNFGILEYHLDDLPLRE-DLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-389 |
3.52e-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: 309.45 E-value: 3.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 1 MKITELETVRVR--------------DFPNILWVRIHTDEGLVGLGETFFM---AQTVETYIHEVVAPKLVGRDPLEIDR 63
Cdd:COG4948 1 MKITDIEVYPVRlplkrpftisrgtrTERDVVLVRVETDDGITGWGEAVPGgtgAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 64 ISKDLTgylgfRSTGAEMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCagntymrdakgqqtanyGIGGP 143
Cdd:COG4948 81 LWQRLY-----RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATL-----------------GIDTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 144 rrdyddlngflERADELAEDLLSEGITAMKIWPFdiaaeksggqyisGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQ 223
Cdd:COG4948 139 -----------EEMAEEAREAVARGFRALKLKVG-------------GPDPEEDVERVRAVREAVGPDARLRVDANGAWT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 224 LTPAIQIARALEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAK 303
Cdd:COG4948 195 LEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEAL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 304 KISTMAEAWHLPVAPHD-CTGPVVLAASTHLSLNAPNALVQESVRAYYktWYADLTTQLPTVTNGMITIPPGAGHGVDLA 382
Cdd:COG4948 275 RIAALAEAHGVPVMPHCmLESGIGLAAALHLAAALPNFDIVELDGPLL--LADDLVEDPLRIEDGYLTVPDGPGLGVELD 352
|
....*..
gi 504345021 383 PDLDRKF 389
Cdd:COG4948 353 EDALARY 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-381 |
1.87e-68 |
|
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: 219.89 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 2 KITELETVRVRdfPNILWVRIHTDEGLVGLGETFF--MAQTVETYIHEVVApKLVGRDPLEIDRISKDLTgYLGFRSTGA 79
Cdd:cd03325 1 KITKIETFVVP--PRWLFVKIETDEGVVGWGEPTVegKARTVEAAVQELED-YLIGKDPMNIEHHWQVMY-RGGFYRGGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 80 E-MRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYntcagntymrdakgqqtanYGIGGprrdyDDLNGFLERAD 158
Cdd:cd03325 77 VlMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVY-------------------SWIGG-----DRPSDVAEAAR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 159 ELAEdllsEGITAMKIWPFDIAaeksggQYISGPD-LRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPY 237
Cdd:cd03325 133 ARRE----AGFTAVKMNATEEL------QWIDTSKkVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 238 ATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVA 317
Cdd:cd03325 203 RLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALA 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504345021 318 PHDCTGPVVLAASTHLSLNAPNALVQE-SVRAYY----KTWYADLTTQLPTVTNGMITIPPGAGHGVDL 381
Cdd:cd03325 283 PHCPLGPIALAASLHVDASTPNFLIQEqSLGIHYnegdDLLDYLVDPEVFDMENGYVKLPTGPGLGIEI 351
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
155-384 |
2.04e-67 |
|
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: 212.81 E-value: 2.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 155 ERADELAEDLLSEGITAMKIWPFdiaaeksggqyisGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARAL 234
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVG-------------GPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 235 EPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHL 314
Cdd:pfam13378 68 EELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 315 PVAPHDCTGPVVLAASTHLSLNAPNALVQESVrAYYKTWYADLTTQLPTVTNGMITIPPGAGHGVDLAPD 384
Cdd:pfam13378 148 PVAPHSGGGPIGLAASLHLAAAVPNLLIQEYF-LDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-388 |
2.07e-63 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 207.83 E-value: 2.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 1 MKITELETVRVRdfPNILWVRIHTDEGLVGLGETFF--MAQTVETYIHEVvAPKLVGRDPLEIDRISKDLT--GYlgFRS 76
Cdd:PRK14017 1 MKITKLETFRVP--PRWLFLKIETDEGIVGWGEPVVegRARTVEAAVHEL-ADYLIGKDPRRIEDHWQVMYrgGF--YRG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 77 TGAEMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTcagntymrdakgqqtanygIGGPRRdyddlngfler 156
Cdd:PRK14017 76 GPILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSW-------------------IGGDRP----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 157 AD--ELAEDLLSEGITAMKiwpFDIAAEKsggQYISGPD-LRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARA 233
Cdd:PRK14017 126 ADvaEAARARVERGFTAVK---MNGTEEL---QYIDSPRkVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 234 LEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWH 313
Cdd:PRK14017 200 LEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 314 LPVAPHDCTGPVVLAASTHLSLNAPNALVQE-SVRAYYKTwYADLTTQLP-----TVTNGMITIPPGAGHGVDLAPDLDR 387
Cdd:PRK14017 280 VALAPHCPLGPIALAACLQVDAVSPNAFIQEqSLGIHYNQ-GADLLDYVKnkevfAYEDGFVAIPTGPGLGIEIDEAKVR 358
|
.
gi 504345021 388 K 388
Cdd:PRK14017 359 E 359
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
2-381 |
9.12e-59 |
|
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: 194.47 E-value: 9.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 2 KITELETvrvrdFPNILWVRIHTDEGLVGLGETFfMAQTVETYIHEVVAPKLVGRDPLEIDRISKDLtgylgFRST---- 77
Cdd:cd03327 1 KIKSVRT-----RVGWLFVEIETDDGTVGYANTT-GGPVACWIVDQHLARFLIGKDPSDIEKLWDQM-----YRATlayg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 78 --GAEMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCAGNTYmrdakgqqtanygiggprrdyddlngfLE 155
Cdd:cd03327 70 rkGIAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTD---------------------------LD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 156 RADELAEDLLSEGITAMKiWPFdiaaeksggqyISGPD-----LRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQI 230
Cdd:cd03327 123 ELPDEAKEYLKEGYRGMK-MRF-----------GYGPSdghagLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKM 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 231 ARALEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAE 310
Cdd:cd03327 191 ARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAE 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504345021 311 AWHLPVAPHdcTGPVvlaASTHLSLNAPNALVQE----SVRAYYKTWYADLTTQLPTVTNGMITIPPGAGHGVDL 381
Cdd:cd03327 271 AYGVPVVPH--ASQI---YNYHFIMSEPNSPFAEylpnSPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLEL 340
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-394 |
6.16e-41 |
|
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: 148.36 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 2 KITELETVRVRDFPNILWVRIHTDEGLVGLGETFFMAQ--TVETYIHEVVAPKLVGRDPLEIDRISKDLTGYLGFRSTGA 79
Cdd:cd03322 1 KITAIEVIVTCPGRNFVTLKITTDQGVTGLGDATLNGRelAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 80 EMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCAGntymrdakgqqtanygiggprrdyDDLNGFLERAde 159
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASG------------------------RDIPELLEAV-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 160 laEDLLSEGITAMKIwpfdiaaeksggqyisgpdlrKALEPFEKIRKRVGDRIDIMVEFHSmwQLTP--AIQIARALEPY 237
Cdd:cd03322 135 --ERHLAQGYRAIRV---------------------QLPKLFEAVREKFGFEFHLLHDVHH--RLTPnqAARFGKDVEPY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 238 ATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAE------A 311
Cdd:cd03322 190 RLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASlygvrtG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 312 WHlpvAPHDCTgPVVLAASTHLSLNAPNALVQESVRAYYKTwyADLTTQLPTVTNGMITIPPGAGHGVDLAPDLDRKFEV 391
Cdd:cd03322 270 WH---GPTDLS-PVGMAAALHLDLWVPNFGIQEYMRHAEET--LEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPY 343
|
...
gi 504345021 392 SRR 394
Cdd:cd03322 344 VPR 346
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
20-385 |
1.06e-38 |
|
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: 142.54 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 20 VRIHTDEGLVGlgETFFMAQTVETYIHE-VVAPKLVGRDPLEIDRISKDLTGYLGfrstGAEMRGNSAVDIGLWDLFGKA 98
Cdd:cd03329 37 LTIETDEGAKG--HAFGGRPVTDPALVDrFLKKVLIGQDPLDRERLWQDLWRLQR----GLTDRGLGLVDIALWDLAGKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 99 TNLPIAQLLGGFsRREIRTYntcaGNTYMRDAKGqqtanyGIGGPRrdyddlngflERADElAEDLLSEGITAMKIWPFd 178
Cdd:cd03329 111 LGLPVHRLLGGY-REKIPAY----ASTMVGDDLE------GLESPE----------AYADF-AEECKALGYRAIKLHPW- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 179 iaaeksggqyiSGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPIKMDSLSSLKRYA 258
Cdd:cd03329 168 -----------GPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 259 AASRAPLCASETLATR-WAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVAPHDCTgpvvlAASTHLSLNA 337
Cdd:cd03329 237 EKLDIPILGTEHSRGAlESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNG-----AANLHVIAAI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 504345021 338 PN------ALVQESVR-AYYKTWYADLttQLPTVTNGMITIPPGAGHGVDLAPDL 385
Cdd:cd03329 312 RNtryyerGLLHPSQKyDVYAGYLSVL--DDPVDSDGFVHVPKGPGLGVEIDFDY 364
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-394 |
4.62e-37 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 138.89 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 1 MKITELETVRVRDFPNILWVRIHTDEGLVGLGETFF----MAqtVETYIHEVVAPKLVGRDPLEIDRISKDLtgYLG--F 74
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFVTLKITTDDGVTGLGDATLngreLA--VASYLQDHVCPLLIGRDAHRIEDIWQYL--YRGayW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 75 RSTGAEMRGNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCAGNTY--------MRDAKGQQT----------- 135
Cdd:PRK15072 77 RRGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIdellddvaRHLELGYKAirvqcgvpglk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 136 ANYGIG-GPRRDYddlngfleradELAEDLLsegITAMKIWpfdiaaekSGGQYisgpdLRKALEPFEKIRKRVGDRIDI 214
Cdd:PRK15072 157 TTYGVSkGKGLAY-----------EPATKGL---LPEEELW--------STEKY-----LRFVPKLFEAVRNKFGFDLHL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 215 MVEFHSmwQLTPaIQIAR---ALEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVML 291
Cdd:PRK15072 210 LHDVHH--RLTP-IEAARlgkSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 292 DLSWCGGISEAKKISTMAEAWHLPVAPHDCT--GPVVLAASTHLSLNAPNALVQESVRayyktwYADLTTQL-P---TVT 365
Cdd:PRK15072 287 TVTHAGGITHLRRIADFAALYQVRTGSHGPTdlSPVCMAAALHFDLWVPNFGIQEYMG------HSEETLEVfPhsyTFE 360
|
410 420
....*....|....*....|....*....
gi 504345021 366 NGMITIPPGAGHGVDLAPDLDRKFEVSRR 394
Cdd:PRK15072 361 DGYLHPGDAPGLGVDFDEKLAAKYPYEPA 389
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
166-344 |
3.28e-30 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 115.89 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 166 SEGITA--MKIWpfDIAA--------EKSGGQYISGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALE 235
Cdd:cd00308 41 GEVISGidMALW--DLAAkalgvplaELLGGGSRDRVPAYGSIERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 236 PYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLP 315
Cdd:cd00308 119 KYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIR 198
|
170 180 190
....*....|....*....|....*....|
gi 504345021 316 VAPHDCTG-PVVLAASTHLSLNAPNALVQE 344
Cdd:cd00308 199 VMVHGTLEsSIGTAAALHLAAALPNDRAIE 228
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
3-384 |
3.11e-29 |
|
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: 116.65 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 3 ITELETVRVRDFPN-------ILWVRIHTDEGLVGLGE------TFFMAQTVETY---IHEVVAPKLVGRDPLEIDRISK 66
Cdd:cd03318 9 IVDLPTRRPHQFAGttmhtqsLVLVRLTTSDGVVGIGEattpggPAWGGESPETIkaiIDRYLAPLLIGRDATNIGAAMA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 67 DLTGYLgfrstgaemRGN----SAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCAGNTYMRDakgqqtanygigg 142
Cdd:cd03318 89 LLDRAV---------AGNlfakAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERD------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 143 prrdyddlngfLERADELAEDllsegiTAMKIWPFDIAAEksggqyisgpDLRKALEPFEKIRKRVGDRIDIMVEFHSMW 222
Cdd:cd03318 147 -----------IAEAEEMLEA------GRHRRFKLKMGAR----------PPADDLAHVEAIAKALGDRASVRVDVNQAW 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 223 QLTPAIQIARALEPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLatrWAFRDLMET---DAAGVVMLDLSWCGGI 299
Cdd:cd03318 200 DESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESV---SGPADAFELarrGAADVFSLKIAKSGGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 300 SEAKKISTMAEAWHLPvaPHDCT---GPVVLAASTHLSLNAPNALVQEsvrAYYKTWY--ADLTTQLPTVTNGMITIPPG 374
Cdd:cd03318 277 RRAQKVAAIAEAAGIA--LYGGTmleSSIGTAASAHLFATLPSLPFGC---ELFGPLLlaEDLLEEPLAYRDGELHVPTG 351
|
410
....*....|
gi 504345021 375 AGHGVDLAPD 384
Cdd:cd03318 352 PGLGVRLDED 361
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
18-319 |
1.82e-26 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 109.43 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 18 LWVRIHTDEGLVGLGET---FFMAQTVETYIhevvAPKLVGRDPLEIDRISKDL---TGYLGFRstGAEMRGNSAVDIGL 91
Cdd:PRK15440 59 LVVEVEAENGQVGFAVStagEMGAFIVEKHL----NRFIEGKCVSDIELIWDQMlnaTLYYGRK--GLVMNTISCVDLAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 92 WDLFGKATNLPIAQLLGGFSRREIRTYNTcagntymrdakgqqtanygigGPRRDYDDLNGFLEradelaedllseGITA 171
Cdd:PRK15440 133 WDLLGKVRGLPVYKLLGGAVRDELQFYAT---------------------GARPDLAKEMGFIG------------GKMP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 172 MKIWPfdiaAEKSGGqyisgpdLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPIKMD-- 249
Cdd:PRK15440 180 LHHGP----ADGDAG-------LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDdy 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504345021 250 -SLSSLKRyaAASRAPLCAS-ETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVAPH 319
Cdd:PRK15440 249 wGYRELKR--NAPAGMMVTSgEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| 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 ... |
10-316 |
2.97e-22 |
|
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: 96.10 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 10 RVRDFPNILWVRIHTDeGLVGLGET----FFMAQTVETYIHEV--VAPKLVGRDPlEIDRISKDLTGYLGFRSTGAemrg 83
Cdd:cd03319 20 GSRTEAENVIVEIELD-GITGYGEAaptpRVTGETVESVLAALksVRPALIGGDP-RLEKLLEALQELLPGNGAAR---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 84 nSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTYNTCagntymrdakgqqtanyGIGGPrrdyddlngflERADELAED 163
Cdd:cd03319 94 -AAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTI-----------------SIDTP-----------EAMAAAAKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 164 LLSEGITAMKIwpfdiaaeKSGGqyisgpDLRKALEPFEKIRKRVGDrIDIMVEFHSMWQLTPAIQIARALEPYATFWHE 243
Cdd:cd03319 145 AAKRGFPLLKI--------KLGG------DLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELLRELAELGVELIE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504345021 244 DPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPV 316
Cdd:cd03319 210 QPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKV 282
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
20-316 |
8.19e-22 |
|
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: 93.95 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 20 VRIHTDEGLVGLGEtffmaqtvetyihevvAPKlvgrdpleidriskdltgylgfrstgaemrgnSAVDIGLWDLFGKAT 99
Cdd:cd03315 29 LRLHTDDGLVGWAE----------------ATK--------------------------------AAVDMALWDLWGKRL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 100 NLPIAQLLGGFsRREIRTYNTCagntymrdakgqqtanyGIGGPrrdyddlngflERADELAEDLLSEGITAMKIwpfdi 179
Cdd:cd03315 61 GVPVYLLLGGY-RDRVRVAHML-----------------GLGEP-----------AEVAEEARRALEAGFRTFKL----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 180 aaeKSGGqyisgpDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPIKMDSLSSLKRYAA 259
Cdd:cd03315 107 ---KVGR------DPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALAR 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 504345021 260 ASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPV 316
Cdd:cd03315 178 ATDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPV 234
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
24-389 |
3.67e-20 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 90.62 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 24 TDEGLVGLGETFFMAQTVETYIHEVV---APKLVGRD--PLEIDRISKD---LTGYLGFRSTGAemrgnSAVDIGLWDLF 95
Cdd:cd03321 38 TDEGVTGHSYLFTYTPAALKSLKQLLddmAALLVGEPlaPAELERALAKrfrLLGYTGLVRMAA-----AGIDMAAWDAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 96 GKATNLPIAQLLGGfSRREIRTYNTcagntymrdakgqqtanYGIGGprrdyddlngfLERADELAEDLLSEGITAMKIw 175
Cdd:cd03321 113 AKVHGLPLAKLLGG-NPRPVQAYDS-----------------HGLDG-----------AKLATERAVTAAEEGFHAVKT- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 176 pfdiaaeksggqYISGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPIKMDSLSSLK 255
Cdd:cd03321 163 ------------KIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 256 RYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVAPHdctgpVVLAASTHLSL 335
Cdd:cd03321 231 RIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH-----LFQEISAHLLA 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 504345021 336 NAPNALVQEsvraYYKTWYADLTTQLpTVTNGMITIPPGAGHGVDLAPDLDRKF 389
Cdd:cd03321 306 VTPTAHWLE----YVDWAGAILEPPL-KFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
20-381 |
9.22e-19 |
|
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: 86.70 E-value: 9.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 20 VRIHTDeGLVGLGETFFMAQTVEtYIHEVVAPKLVGRDPLEIDRISkdltgylgfRSTGAEMRGN----------SAVDI 89
Cdd:cd03328 33 VEVRAG-GRTGLGYTYADAAAAA-LVDGLLAPVVEGRDALDPPAAW---------EAMQRAVRNAgrpgvaamaiSAVDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 90 GLWDLFGKATNLPIAQLLGGFSRReirtyntcagntymrdakgqqTANYGIGGpRRDYDDlngfleraDELAEDL---LS 166
Cdd:cd03328 102 ALWDLKARLLGLPLARLLGRAHDS---------------------VPVYGSGG-FTSYDD--------DRLREQLsgwVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 167 EGITAMKIwpfdiaaeKSGGQYISGPDlRKALepfekIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPI 246
Cdd:cd03328 152 QGIPRVKM--------KIGRDPRRDPD-RVAA-----ARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 247 KMDSLSSLK--RYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVAPHdcTGP 324
Cdd:cd03328 218 SSDDLAGLRlvRERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH--CAP 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504345021 325 vvlAASTHLSLNAPNALVQEsvrayyktWYAD-------LTTQLPTVTNGMITIPPG-AGHGVDL 381
Cdd:cd03328 296 ---ALHAHVACAVPRLRHLE--------WFHDhvriermLFDGAPDPSGGALRPDLSrPGLGLEL 349
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
4-384 |
1.19e-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: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 4 TELETVRVRDFpniLWVRIHTDEGLVGLGET------FFMAQTVETYIH---EVVAPKLVGRDPLEIDRISKDLTGYLGF 74
Cdd:cd03317 16 TSFGTLNEREF---LIVELTDEEGITGYGEVvafegpFYTEETNATAWHilkDYLLPLLLGREFSHPEEVSERLAPIKGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 75 RSTGAemrgnsAVDIGLWDLFGKATNLPIAQLLGGfSRREIrtyntcagntYMRDAKGQQtanygiggprrdyDDLNGFL 154
Cdd:cd03317 93 NMAKA------GLEMAVWDLYAKAQGQSLAQYLGG-TRDSI----------PVGVSIGIQ-------------DDVEQLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 155 ERADElaedLLSEGITAMKIwpfDIAAEKSggqyisgpdlrkaLEPFEKIRKRVGDrIDIMVEFHSMWQLTPAIQIARaL 234
Cdd:cd03317 143 KQIER----YLEEGYKRIKL---KIKPGWD-------------VEPLKAVRERFPD-IPLMADANSAYTLADIPLLKR-L 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 235 EPYATFWHEDPIKMDSLSSLKRYAAASRAPLCASETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHL 314
Cdd:cd03317 201 DEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504345021 315 PVAphdCTGPVV--LAASTHLSLNA-PNALVQESVRAYYKTWYADLTTQLPTVTNGMITIPPGAGHGVDLAPD 384
Cdd:cd03317 281 PVW---CGGMLEsgIGRAHNVALASlPNFTYPGDISASSRYFEEDIITPPFELENGIISVPTGPGIGVTVDRE 350
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
2-335 |
5.64e-16 |
|
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: 78.92 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 2 KITELETVRVRdFPNIL-----------------WVRIHTDE-GLVGLGETFFMAQ--TVETYIHEVVAPKLVGRDpleI 61
Cdd:cd03324 2 KITALEVRDVR-FPTSLeldgsdamnpdpdysaaYVVLRTDAaGLKGHGLTFTIGRgnEIVCAAIEALAHLVVGRD---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 62 DRISKDLTGYLGFRSTGAEMR-----------GNSAVDIGLWDLFGKATNLPIAQLLGGFSRREIRTyntCAGNTYMRDA 130
Cdd:cd03324 78 ESIVADMGKFWRRLTSDSQLRwigpekgvihlATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVS---CIDFRYITDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 131 -----------KGQQTANYGIGGPRRD----YDDLNGFLERADE----LAEDLLSEGITAMKIwpfdiaaeKSGGqyisg 191
Cdd:cd03324 155 ltpeealeilrRGQPGKAAREADLLAEgypaYTTSAGWLGYSDEklrrLCKEALAQGFTHFKL--------KVGA----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 192 pDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDPIKMDSLSSLKRYAAASRA---PLCAS 268
Cdd:cd03324 222 -DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPlpiGVATG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504345021 269 ETLATRWAFRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVAPHdcTGPVVLAAST-HLSL 335
Cdd:cd03324 301 EHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPH--AGGVGLCELVqHLSM 366
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
20-108 |
4.45e-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: 70.96 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 20 VRIHTDEGLVGLGETF---FMAQTVETYIHEVVAPKLVGRDPleiDRISkdLTGYLGFRSTGAEMRGNSAVDIGLWDLFG 96
Cdd:pfam02746 31 VRIETSEGVVGIGEATsygGRAETIKAILDDHLAPLLIGRDA---ANIS--DLWQLMYRAALGNMSAKAAIDMALWDLKA 105
|
90
....*....|..
gi 504345021 97 KATNLPIAQLLG 108
Cdd:pfam02746 106 KVLNLPLADLLG 117
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
20-387 |
2.83e-14 |
|
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: 73.51 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 20 VRIHTDEGLVGLGETFFMAQTVEtyIHEVVAPKLVGRDP-LEIDRISKDLTGYlgFRSTGAEMRGN------------SA 86
Cdd:cd03323 33 VELTDDNGNTGVGESPGGAEALE--ALLEAARSLVGGDVfGAYLAVLESVRVA--FADRDAGGRGLqtfdlrttvhvvTA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 87 VDIGLWDLFGKATNLPIAQLLGGFSRREIRTyntcAGNTYMRDAKGQQTANYgiggprRDYDDLNGfleradelaEDLLS 166
Cdd:cd03323 109 FEVALLDLLGQALGVPVADLLGGGQRDSVPF----LAYLFYKGDRHKTDLPY------PWFRDRWG---------EALTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 167 EGITAMKiwpfDIAAEKSGGQYI--SGPDLRKA--LEPFEKIRKRV-GDRIDImvEFHSMWQLTPAIQIARALE---PYA 238
Cdd:cd03323 170 EGVVRLA----RAAIDRYGFKSFklKGGVLPGEeeIEAVKALAEAFpGARLRL--DPNGAWSLETAIRLAKELEgvlAYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 239 tfwhEDPIKmdSLSSLKRYAAASRAPLcASETLATRWA-FRDLMETDAAGVVMLDLSWCGGISEAKKISTMAEAWHLPVA 317
Cdd:cd03323 244 ----EDPCG--GREGMAEFRRATGLPL-ATNMIVTDFRqLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504345021 318 PHDCTG-PVVLAASTHLSLNAPNALVqeSVRAYYKTWYAD-LTTQLPTVTNGMITIPPGAGHGVDLapDLDR 387
Cdd:cd03323 317 MHSNNHlGISLAMMTHVAAAAPGLIT--ACDTHWIWQDGQvITGEPLRIKDGKVAVPDKPGLGVEL--DRDK 384
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
155-262 |
3.74e-13 |
|
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: 65.00 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 155 ERADELAEDLLSEGITAMKIWPfdiaaeksggqyisGPDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARAL 234
Cdd:smart00922 3 ELAEAARRAVAEAGFRAVKVKV--------------GGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEAL 68
|
90 100
....*....|....*....|....*...
gi 504345021 235 EPYATFWHEDPIKMDSLSSLKRYAAASR 262
Cdd:smart00922 69 DELGLEWIEEPVPPDDLEGLAELRRATP 96
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
45-245 |
1.94e-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: 52.78 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 45 IHEVVAPKLVGRDPleiDRISKDLTGYLG-FRSTGAEMRGN------------SAVDIGLWDLFGKATNLPIAQLLggfS 111
Cdd:cd03326 61 LRERFIPRLLAAAP---DSLLDDAGGNLDpARAWAAMMRNEkpgghgeravavGALDMAVWDAVAKIAGLPLYRLL---A 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504345021 112 RReirtyntcagntYMRDAKGQQTANYGIGGPRRDYDDLNGFlerADELaEDLLSEGITAMKIwpfdiaaeksggqYISG 191
Cdd:cd03326 135 RR------------YGRGQADPRVPVYAAGGYYYPGDDLGRL---RDEM-RRYLDRGYTVVKI-------------KIGG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504345021 192 PDLRKALEPFEKIRKRVGDRIDIMVEFHSMWQLTPAIQIARALEPYATFWHEDP 245
Cdd:cd03326 186 APLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP 239
|
|
| |
