|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
2-403 |
0e+00 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 874.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 2 PKIIDAKVIVTCPGRNFVTLKIITDEGVHGVGDATLNGRELAVGSYLADHVVPCLIGRDAHRIEDIWQYLYKGAYWRRGP 81
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFVTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGAYWRRGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 82 VTMTAIAAVDMALWDIKGKIAGLPVYQLLGGASREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQCGVPGMASTYG 161
Cdd:PRK15072 81 VTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQCGVPGLKTTYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 162 VSKDK-YFYEPA-DADLPTENVWNTSKYLRVVPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDA 239
Cdd:PRK15072 161 VSKGKgLAYEPAtKGLLPEEELWSTEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 240 TPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDLS 319
Cdd:PRK15072 241 TPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTDLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 320 PVCMAAALHFDLSVPNFGIQEYMRHTPETDAVFPHAYTFSDGMMHPGEAPGLGVDIDEKLAAGYEYKRAFLPVNRLEDGT 399
Cdd:PRK15072 321 PVCMAAALHFDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKYPYEPAYLPVARLEDGT 400
|
....
gi 502818943 400 MFSW 403
Cdd:PRK15072 401 MWNW 404
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
3-403 |
0e+00 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 624.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 3 KIIDAKVIVTCPGRNFVTLKIITDEGVHGVGDATLNGRELAVGSYLADHVVPCLIGRDAHRIEDIWQYLYKGAYWRRGPV 82
Cdd:cd03322 1 KITAIEVIVTCPGRNFVTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 83 TMTAIAAVDMALWDIKGKIAGLPVYQLLGGASREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQCgvpgmastygv 162
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQL----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 163 skdkyfyepadadlptenvwntskylrvvPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPA 242
Cdd:cd03322 150 -----------------------------PKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 243 ENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDLSPVC 322
Cdd:cd03322 201 ENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSPVG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 323 MAAALHFDLSVPNFGIQEYMRHTPETDAVFPHAYTFSDGMMHPGEAPGLGVDIDEKLAAGYEYKRAFLPVNRLEDGTMFS 402
Cdd:cd03322 281 MAAALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPVARLEDGTVHN 360
|
.
gi 502818943 403 W 403
Cdd:cd03322 361 W 361
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
3-374 |
3.70e-128 |
|
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: 373.10 E-value: 3.70e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 3 KIIDAKVIVTCP----------GRNFVTLKIITDEGVHGVGDATLNGRELAVGSYLADHVVPCLIGRDAHRIEDIWQYLY 72
Cdd:cd03316 1 KITDVETFVLRVplpepggavtWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 73 KGAYWR-RGPVTMTAIAAVDMALWDIKGKIAGLPVYQLLGGASREGAMVYGHANGT--TIEDTINAALEYQAQGYKAIRL 149
Cdd:cd03316 81 RRLFWRgRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYddSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 150 QCGVPGMAstygvskdkyfyepadadlptenvwntSKYLRVVPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLE 229
Cdd:cd03316 161 KVGGPDSG---------------------------GEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 230 PYRPFWLEDATPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVR 309
Cdd:cd03316 214 EYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVR 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502818943 310 TGCHGATdlSPVCMAAALHFDLSVPNFGIQEYMRHTPET-DAVFPHAYTFSDGMMHPGEAPGLGVD 374
Cdd:cd03316 294 VAPHGAG--GPIGLAASLHLAAALPNFGILEYHLDDLPLrEDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
12-383 |
7.11e-113 |
|
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: 334.48 E-value: 7.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 12 TCPGRNFVTLKIITDEGVHGVGDATLNGREL-AVGSYLADHVVPCLIGRDAHRIEDIWQYLYkgaywRRGPVTMTAIAAV 90
Cdd:COG4948 25 TRTERDVVLVRVETDDGITGWGEAVPGGTGAeAVAAALEEALAPLLIGRDPLDIEALWQRLY-----RALPGNPAAKAAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 91 DMALWDIKGKIAGLPVYQLLGGASREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQCGVPGMastygvskdkyfye 170
Cdd:COG4948 100 DMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLKVGGPDP-------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 171 paDADLptenvwntskylrvvpELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRL 250
Cdd:COG4948 166 --EEDV----------------ERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 251 IRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDlSPVCMAAALHFD 330
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLE-SGIGLAAALHLA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502818943 331 LSVPNFGIQEYMRHTPETDAVFPHAYTFSDGMMHPGEAPGLGVDIDEKLAAGY 383
Cdd:COG4948 307 AALPNFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
3-376 |
1.34e-97 |
|
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: 295.00 E-value: 1.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 3 KIIDAKVIVtCPgRNFVTLKIITDEGVHGVGDATLNGRELAVGSYLADHVvPCLIGRDAHRIEDIWQYLYKGAYWRRGPV 82
Cdd:cd03325 1 KITKIETFV-VP-PRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELE-DYLIGKDPMNIEHHWQVMYRGGFYRGGPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 83 TMTAIAAVDMALWDIKGKIAGLPVYQLLGGASREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQCgvpgmastygv 162
Cdd:cd03325 78 LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNA----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 163 skdkyfyepadaDLPTENVwNTSKYLRVVPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPA 242
Cdd:cd03325 147 ------------TEELQWI-DTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 243 ENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGAtdLSPVC 322
Cdd:cd03325 214 ENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCP--LGPIA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502818943 323 MAAALHFDLSVPNFGIQEYM--RHTPETDAVF-----PHAYTFSDGMMHPGEAPGLGVDID 376
Cdd:cd03325 292 LAASLHVDASTPNFLIQEQSlgIHYNEGDDLLdylvdPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
21-403 |
6.62e-91 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 279.09 E-value: 6.62e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 21 LKIITDEGVHGVGDATLNGRELAVGSY---LADHvvpcLIGRDAHRIEDIWQYLYKGAYWRRGPVTMTAIAAVDMALWDI 97
Cdd:PRK14017 18 LKIETDEGIVGWGEPVVEGRARTVEAAvheLADY----LIGKDPRRIEDHWQVMYRGGFYRGGPILMSAIAGIDQALWDI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 98 KGKIAGLPVYQLLGGASREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQcgvpgmastyGVSKDKYFYEPADADLP 177
Cdd:PRK14017 94 KGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMN----------GTEELQYIDSPRKVDAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 178 TENVWntskylrvvpelfkAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQHTTA 257
Cdd:PRK14017 164 VARVA--------------AVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 258 PLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHgaTDLSPVCMAAALHFDLSVPNFG 337
Cdd:PRK14017 230 PIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPH--CPLGPIALAACLQVDAVSPNAF 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502818943 338 IQEYMR--HTPETDAVF-----PHAYTFSDGMMHPGEAPGLGVDIDEKL--AAGYEYKRAFLPVNRLEDGTMFSW 403
Cdd:PRK14017 308 IQEQSLgiHYNQGADLLdyvknKEVFAYEDGFVAIPTGPGLGIEIDEAKvrERAKTGHDWRNPVWRHADGSVAEW 382
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
19-376 |
1.60e-58 |
|
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: 194.09 E-value: 1.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 19 VTLKIITDEGVHGVGDATLNgrELAVGSYLaDHVVPCLIGRDAHRIEDIWQYLYKGA-YWRRGPVTMTAIAAVDMALWDI 97
Cdd:cd03327 12 LFVEIETDDGTVGYANTTGG--PVACWIVD-QHLARFLIGKDPSDIEKLWDQMYRATlAYGRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 98 KGKIAGLPVYQLLGGASREGAMVYG-HANGTTIEDTINAALEYQAQGYKA--IRLQCGvpgmastygvskdkyfyePADA 174
Cdd:cd03327 89 LGKIRGEPVYKLLGGRTRDKIPAYAsGLYPTDLDELPDEAKEYLKEGYRGmkMRFGYG------------------PSDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 175 DLP-TENVwntskylrvvpELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQ 253
Cdd:cd03327 151 HAGlRKNV-----------ELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 254 HTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATdlspvcmAAALHFDLSV 333
Cdd:cd03327 220 ATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQ-------IYNYHFIMSE 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502818943 334 PNFGIQEYMRHTPETDAVFPHAYTF------SDGMMHPGEAPGLGVDID 376
Cdd:cd03327 293 PNSPFAEYLPNSPDEVGNPLFYYIFlnepvpVNGYFDLSDKPGFGLELN 341
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
193-377 |
1.20e-50 |
|
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: 169.67 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 193 ELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAK 272
Cdd:pfam13378 32 ERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 273 DLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATdlSPVCMAAALHFDLSVPNFGIQEYMR-HTPETDAV 351
Cdd:pfam13378 112 RLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG--GPIGLAASLHLAAAVPNLLIQEYFLdPLLLEDDL 189
|
170 180
....*....|....*....|....*.
gi 502818943 352 FPHAYTFSDGMMHPGEAPGLGVDIDE 377
Cdd:pfam13378 190 LTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
86-341 |
5.45e-45 |
|
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: 155.18 E-value: 5.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 86 AIAAVDMALWDIKGKIAGLPVYQLLGGASREGAMVYGHangttiedtinaaleyqaqgykairlqcgvpgmastygvskd 165
Cdd:cd00308 43 VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS------------------------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 166 kyfyepadadlptenvwntskylrvvPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQ 245
Cdd:cd00308 81 --------------------------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 246 EAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDlSPVCMAA 325
Cdd:cd00308 135 EGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE-SSIGTAA 213
|
250
....*....|....*.
gi 502818943 326 ALHFDLSVPNFGIQEY 341
Cdd:cd00308 214 ALHLAAALPNDRAIET 229
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
21-376 |
9.31e-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: 139.84 E-value: 9.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 21 LKIITDEGVHGVgdaTLNGRELAVGSYLADHVVPCLIGRDAHRIEDIWQYLYKgayWRRGpVTMTAIAAVDMALWDIKGK 100
Cdd:cd03329 37 LTIETDEGAKGH---AFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQDLWR---LQRG-LTDRGLGLVDIALWDLAGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 101 IAGLPVYQLLGGAsREGAMVYGHANG-------TTIEDTINAALEYQAQGYKAIRLQCGVPGMAstygvskdkyfyepaD 173
Cdd:cd03329 110 YLGLPVHRLLGGY-REKIPAYASTMVgddleglESPEAYADFAEECKALGYRAIKLHPWGPGVV---------------R 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 174 ADLptenvwntskylrvvpELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQ 253
Cdd:cd03329 174 RDL----------------KACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 254 HTTAPLAVGE-IFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGatdlspvCMAAALHFDLS 332
Cdd:cd03329 238 KLDIPILGTEhSRGALESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHG-------NGAANLHVIAA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502818943 333 VPNFGIQEYMRHTPETDAVFPHAYTF-------SDGMMHPGEAPGLGVDID 376
Cdd:cd03329 311 IRNTRYYERGLLHPSQKYDVYAGYLSvlddpvdSDGFVHVPKGPGLGVEID 361
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
18-111 |
1.20e-32 |
|
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: 119.11 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 18 FVTLKIITDEGVHGVGDATLNG-RELAVGSYLADHVVPCLIGRDAHRIEDIWQYLYKGAYWrrgpvTMTAIAAVDMALWD 96
Cdd:pfam02746 28 LVIVRIETSEGVVGIGEATSYGgRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAALG-----NMSAKAAIDMALWD 102
|
90
....*....|....*
gi 502818943 97 IKGKIAGLPVYQLLG 111
Cdd:pfam02746 103 LKAKVLNLPLADLLG 117
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
19-377 |
1.81e-28 |
|
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: 114.72 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 19 VTLKIITDEGVHGVGDATLNGR-----ELAVGSYLA--DHVVPCLIGRDAHRIEDIWQYLYkgaywRRGPVTMTAIAAVD 91
Cdd:cd03318 31 VLVRLTTSDGVVGIGEATTPGGpawggESPETIKAIidRYLAPLLIGRDATNIGAAMALLD-----RAVAGNLFAKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 92 MALWDIKGKIAGLPVYQLLGGASREGAMV-YGHANGTTiEDTINAALEYQAQG-YKAIRLQCGVpgmastygvskdkyfy 169
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGRVRDSLPVaWTLASGDT-ERDIAEAEEMLEAGrHRRFKLKMGA---------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 170 EPADADLptenvwntskyLRVVpelfkAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFR 249
Cdd:cd03318 169 RPPADDL-----------AHVE-----AIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 250 LIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVrtGCHGATDL-SPVCMAAALH 328
Cdd:cd03318 233 RLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTMLeSSIGTAASAH 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502818943 329 FDLSVPN--FGIQEYMRHTPETDAV-FPHAYTfsDGMMHPGEAPGLGVDIDE 377
Cdd:cd03318 311 LFATLPSlpFGCELFGPLLLAEDLLeEPLAYR--DGELHVPTGPGLGVRLDE 360
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
32-387 |
1.98e-27 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 112.13 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 32 VGDATLNGRELavGSYLAD-HVVPCLIGRDAHRIEDIWQYLYKGA-YWRRGPVTMTAIAAVDMALWDIKGKIAGLPVYQL 109
Cdd:PRK15440 70 VGFAVSTAGEM--GAFIVEkHLNRFIEGKCVSDIELIWDQMLNATlYYGRKGLVMNTISCVDLALWDLLGKVRGLPVYKL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 110 LGGASREgamvyghangttiedtinaALEYQAQGYKairlqcgvPGMASTYGV--SKDKYFYEPADADlptenvwntsKY 187
Cdd:PRK15440 148 LGGAVRD-------------------ELQFYATGAR--------PDLAKEMGFigGKMPLHHGPADGD----------AG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 188 LRVVPELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQHTTAPLAV--GEIF 265
Cdd:PRK15440 191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVtsGEHE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 266 NSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDLSpvcmaaaLHFDLSVPNFGIQEYMRHT 345
Cdd:PRK15440 271 ATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYS-------HHFVITRTNSPFSEFLMMS 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 502818943 346 PETDAVFPHAYTF-------SDGMMH--PGEAPGLGVDIDEKLAAGYEYKR 387
Cdd:PRK15440 344 PDADTVVPQFDPIlldepvpVNGRIHksVLDKPGFGVELNRDCNLKRPYSH 394
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
42-372 |
3.25e-23 |
|
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: 99.41 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 42 LAVGSYLADHVVPCLIGRDAHRIEDIWQylykgAYWR------RGPVTMTAIAAVDMALWDIKGKIAGLPVYQLLGgASR 115
Cdd:cd03328 50 AAAAALVDGLLAPVVEGRDALDPPAAWE-----AMQRavrnagRPGVAAMAISAVDIALWDLKARLLGLPLARLLG-RAH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 116 EGAMVYGHANGTTIEDtinAALEYQAQGYKAIrlqcGVPGMastygvsKDKYFYEPADAdlptenvwntskylrvvPELF 195
Cdd:cd03328 124 DSVPVYGSGGFTSYDD---DRLREQLSGWVAQ----GIPRV-------KMKIGRDPRRD-----------------PDRV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 196 KAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQHTTAPLAV--GEIFNSIWDAKD 273
Cdd:cd03328 173 AAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAGMDIaaGEYAYTLAYFRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 274 LIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVrtgchgatDLSPVCmAAALHFDL--SVPNFGIQEYMR-HTPETDA 350
Cdd:cd03328 253 LLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHV--------DLSAHC-APALHAHVacAVPRLRHLEWFHdHVRIERM 323
|
330 340
....*....|....*....|...
gi 502818943 351 VFPHAYTFSDGMMHPGEA-PGLG 372
Cdd:cd03328 324 LFDGAPDPSGGALRPDLSrPGLG 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 ... |
24-329 |
2.09e-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: 96.49 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 24 ITDEGVHGVGDATLNGRELA--VGSYLA--DHVVPCLIGRDAhRIEDIWQYLYKGAywrrgPVTMTAIAAVDMALWDIKG 99
Cdd:cd03319 32 IELDGITGYGEAAPTPRVTGetVESVLAalKSVRPALIGGDP-RLEKLLEALQELL-----PGNGAARAAVDIALWDLEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 100 KIAGLPVYQLLGGASREGAMvyghaNGTTI-----EDTINAALEYQAQGYKAIRLQCGvpgmastygvskdkyfyEPADA 174
Cdd:cd03319 106 KLLGLPLYQLWGGGAPRPLE-----TDYTIsidtpEAMAAAAKKAAKRGFPLLKIKLG-----------------GDLED 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 175 DLptenvwntskylrvvpELFKAAREALGwDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQH 254
Cdd:cd03319 164 DI----------------ERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDK 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502818943 255 TTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRT--GCHGATDLSpvcMAAALHF 329
Cdd:cd03319 227 SPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVmvGCMVESSLS---IAAAAHL 300
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
79-378 |
7.99e-22 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 95.63 E-value: 7.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 79 RGPVTMtAIAAVDMALWDIKGKIAGLPVYQLLGGASREGAmVYGHANGTTIEDTINAALEYQAQGYKAIRLQCGVPGmas 158
Cdd:cd03321 94 TGLVRM-AAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQ-AYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGYPT--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 159 tygvskdkyfyepADADLptenvwntskylrvvpELFKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLED 238
Cdd:cd03321 169 -------------ADEDL----------------AVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 239 ATPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDL 318
Cdd:cd03321 220 PTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEI 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 319 SpvcmaaaLHFDLSVPNFGIQEYMRHtpeTDAVFPHAYTFSDGMMHPGEAPGLGVDIDEK 378
Cdd:cd03321 300 S-------AHLLAVTPTAHWLEYVDW---AGAILEPPLKFEDGNAVIPDEPGNGIIWREK 349
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
88-329 |
9.96e-21 |
|
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: 90.86 E-value: 9.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 88 AAVDMALWDIKGKIAGLPVYQLLGGAsREGAMVYGHANGTTIEDTINAALEYQAQGYKAIRLQCGVPgmastygvskdky 167
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRD------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 168 fyepADADLptenvwntskylRVVPELfkaaREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEA 247
Cdd:cd03315 112 ----PARDV------------AVVAAL----REAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 248 FRLIRQHTTAPLAVGEifnSIWDAKDL---IQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDlSPVCMA 324
Cdd:cd03315 172 RAALARATDTPIMADE---SAFTPHDAfreLALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIE-SGLGTL 247
|
....*
gi 502818943 325 AALHF 329
Cdd:cd03315 248 ANAHL 252
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
135-256 |
1.03e-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: 75.01 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 135 AALEYQAQGYKAIRLQCGVPGMAstygvskdkyfyepadadlptenvwntskylrvVPELFKAAREALGWDVHLLHDIHH 214
Cdd:smart00922 8 ARRAVAEAGFRAVKVKVGGGPLE---------------------------------DLARVAAVREAVGPDADLMVDANG 54
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502818943 215 RLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQHTT 256
Cdd:smart00922 55 AWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAELRRATP 96
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
16-388 |
3.09e-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: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 16 RNFVTlkIITDEGVHGVGD-----ATLNGRELAVGSYLADHVvpclIGRDAHRIEDIWQYLYKGAYWRRGPVTMT----- 85
Cdd:cd03323 30 RNIVE--LTDDNGNTGVGEspggaEALEALLEAARSLVGGDV----FGAYLAVLESVRVAFADRDAGGRGLQTFDlrttv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 86 -AIAAVDMALWDIKGKIAGLPVYQLLGGASRE----------------GAMVY-----GHANGTTIEDTI-NAALEYQAQ 142
Cdd:cd03323 104 hVVTAFEVALLDLLGQALGVPVADLLGGGQRDsvpflaylfykgdrhkTDLPYpwfrdRWGEALTPEGVVrLARAAIDRY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 143 GYKAIRLQCGVpgmastygvskdkyfyepadadLPTENVWNTSKYLRvvpELFKAAREAL----GWdvhllhdihhrlTP 218
Cdd:cd03323 184 GFKSFKLKGGV----------------------LPGEEEIEAVKALA---EAFPGARLRLdpngAW------------SL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 219 IEAGRLGRDLE---PYrpfwLEDatPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITH 295
Cdd:cd03323 227 ETAIRLAKELEgvlAY----LED--PCGGREGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 296 LRRIAALADLYQVRTGCHGATDLSpVCMAAALHFDLSVPN--FGIQEYMRHTpETDAVFPHAYTFSDGMMHPGEAPGLGV 373
Cdd:cd03323 301 SVRVAQVCETWGLGWGMHSNNHLG-ISLAMMTHVAAAAPGliTACDTHWIWQ-DGQVITGEPLRIKDGKVAVPDKPGLGV 378
|
410
....*....|....*..
gi 502818943 374 DID-EKLAAGYE-YKRA 388
Cdd:cd03323 379 ELDrDKLAKAHElYQRL 395
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
16-377 |
5.74e-10 |
|
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: 60.33 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 16 RNFVTLKIITDEGVHGVGDAT-----LNGRELAVGSY--LADHVVPCLIGRDAHRIEDIWQYL--YKGAywrrgpvTMtA 86
Cdd:cd03317 24 REFLIVELTDEEGITGYGEVVafegpFYTEETNATAWhiLKDYLLPLLLGREFSHPEEVSERLapIKGN-------NM-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 87 IAAVDMALWDIKGKIAGLPVYQLLGGASR--EGAMVYGHAngTTIEDTINAALEYQAQGYKAIRLQCGvPGmastygvsk 164
Cdd:cd03317 96 KAGLEMAVWDLYAKAQGQSLAQYLGGTRDsiPVGVSIGIQ--DDVEQLLKQIERYLEEGYKRIKLKIK-PG--------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 165 dkyfyepadadlptenvWNTskylrvvpELFKAAREALGwDVHLLHDIHHRLTPIEAGRLgRDLEPYRPFWLEDATPAEN 244
Cdd:cd03317 164 -----------------WDV--------EPLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 245 QEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGITHLRRIAALADLYQVRTGCHGATDlSPVCMA 324
Cdd:cd03317 217 LIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLE-SGIGRA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502818943 325 AALHFDlSVPNFGIQEYM---RHTPETDAVFPhAYTFSDGMMHPGEAPGLGVDIDE 377
Cdd:cd03317 296 HNVALA-SLPNFTYPGDIsasSRYFEEDIITP-PFELENGIISVPTGPGIGVTVDR 349
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
85-381 |
1.00e-09 |
|
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: 59.72 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 85 TAIAAVDMALWDIKGKIAGLPVYQLL------GGASRE------GAMVYGHANGTTIEDTINaalEYQAQGYKAIRLQCG 152
Cdd:cd03326 108 VAVGALDMAVWDAVAKIAGLPLYRLLarrygrGQADPRvpvyaaGGYYYPGDDLGRLRDEMR---RYLDRGYTVVKIKIG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 153 vpgmastyGVskdkyfyePADADLptenvwntskyLRVvpelfKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYR 232
Cdd:cd03326 185 --------GA--------PLDEDL-----------RRI-----EAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 233 PFWLEDATPAENQEAFRLIRQHTTAPLAVGEIFNSIWDAKDLIQNQLI----DYIRATVVHAGGIT-HLRRIAALADLYQ 307
Cdd:cd03326 233 LRWYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPeYLRMLDVLEAHGW 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 308 VRTGC--HGATDLSpVCMAAALHF-------DLSVPNFGiqeymrhtpetdavFPHAYTFSDGMMHPGEAPGLGVDIDEK 378
Cdd:cd03326 313 SRRRFfpHGGHLMS-LHIAAGLGLggnesypDVFQPFGG--------------FADGCKVENGYVRLPDAPGIGFEGKAE 377
|
...
gi 502818943 379 LAA 381
Cdd:cd03326 378 LAA 380
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
48-293 |
2.60e-08 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 55.43 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 48 LADHVVpcliGRDAHRIEDIWqylykGAYWRR----------GP---VTMTAIAAVDMALWDIKGKIAGLPVYQLLGGAS 114
Cdd:cd03324 68 LAHLVV----GRDLESIVADM-----GKFWRRltsdsqlrwiGPekgVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 115 REgaMVYGHANGTTIEDTINA--ALEY--QAQGYKAIR----LQCGVPGMAST---YGVSKDKYfyepadADLPTENV-- 181
Cdd:cd03324 139 PE--ELVSCIDFRYITDALTPeeALEIlrRGQPGKAAReadlLAEGYPAYTTSagwLGYSDEKL------RRLCKEALaq 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502818943 182 -WNTSKyLRVVPEL------FKAAREALGWDVHLLHDIHHRLTPIEAGRLGRDLEPYRPFWLEDATPAENQEAFRLIRQH 254
Cdd:cd03324 211 gFTHFK-LKVGADLeddirrCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKA 289
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502818943 255 TTA---PLAVGEIFNSIWDAKDLIQNQLIDYIRATVVHAGGI 293
Cdd:cd03324 290 LAPlpiGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGV 331
|
|
| |
