|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-382 |
0e+00 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 828.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 1 MKITGFECFLIPPRWLFLKIETDEGITGWGEPVIEGKAATVKAAVGELMEYLIGKDPMNIEDHWNVMYRGGFYRGGPILM 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGGFYRGGPILM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 81 SAIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMNGTEELQYIDSHEKI 160
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNGTEELQYIDSPRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 161 DQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSK 240
Cdd:PRK14017 161 DAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 241 WQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPLGPIALAACLQVDATCHNAFIQEQSLGIHYNKG 320
Cdd:PRK14017 241 WDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489278596 321 TDLLDYIVDQKVFFYEDGYVRIPDGPGLGVDINEDHVRKMADIGHNWRNPVWRHKDGSIAEW 382
Cdd:PRK14017 321 ADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNPVWRHADGSVAEW 382
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-353 |
0e+00 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 626.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 2 KITGFECFLIPPRWLFLKIETDEGITGWGEPVIEGKAATVKAAVGELMEYLIGKDPMNIEDHWNVMYRGGFYRGGPILMS 81
Cdd:cd03325 1 KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGGFYRGGPVLMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 82 AIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMNGTEELQYIDSHEKID 161
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELQWIDTSKKVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 162 QVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKW 241
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 242 QFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPLGPIALAACLQVDATCHNAFIQEQSLGIHYNKGT 321
Cdd:cd03325 241 DFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGD 320
|
330 340 350
....*....|....*....|....*....|..
gi 489278596 322 DLLDYIVDQKVFFYEDGYVRIPDGPGLGVDIN 353
Cdd:cd03325 321 DLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-351 |
9.19e-130 |
|
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: 376.57 E-value: 9.19e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 2 KITGFECFLIPP------------RWLFLKIETDEGITGWGEPVIEGKAATVKAAVGELME-YLIGKDPMNIEDHWNVMY 68
Cdd:cd03316 1 KITDVETFVLRVplpepggavtwrNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLApLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 69 RGGFYRG-GPILMSAIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGG--DRPQDVGLAAKQVVDKGFTAVKM 145
Cdd:cd03316 81 RRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGydDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 146 NGTEELqyiDSHEKIDQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIAS 225
Cdd:cd03316 161 KVGGPD---SGGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 226 LVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPLGPIALAACLQVDATCHN 305
Cdd:cd03316 238 ATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAALPN 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489278596 306 AFIQEQSLGIHYNKGTDLLDYIVDqkvffyEDGYVRIPDGPGLGVD 351
Cdd:cd03316 318 FGILEYHLDDLPLREDLFKNPPEI------EDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-359 |
4.02e-129 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 374.93 E-value: 4.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 1 MKITGFECFLIPP----------------RWLFLKIETDEGITGWGEPV-IEGKAATVKAAVGE-LMEYLIGKDPMNIED 62
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftisrgtrterDVVLVRVETDDGITGWGEAVpGGTGAEAVAAALEEaLAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 63 HWNVMYRGGFyrggpILMSAIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTA 142
Cdd:COG4948 81 LWQRLYRALP-----GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 143 VKMNGTeelqyidsHEKIDQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRD 222
Cdd:COG4948 156 LKLKVG--------GPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 223 IASLVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPL-GPIALAACLQVDA 301
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489278596 302 TCHNAFIQEQSLGIHYNKgtdllDYIVDQkvFFYEDGYVRIPDGPGLGVDINEDHVRK 359
Cdd:COG4948 308 ALPNFDIVELDGPLLLAD-----DLVEDP--LRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-382 |
8.13e-89 |
|
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: 272.39 E-value: 8.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 2 KITGFECFLIPPRWLF--LKIETDEGITGWGEPVIEGKAATVKAAVGE-LMEYLIGKDPMNIEDHWNVMYRGGFYRGGPI 78
Cdd:cd03322 1 KITAIEVIVTCPGRNFvtLKITTDQGVTGLGDATLNGRELAVKAYLREhLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 79 LMSAIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMngteelqyidshe 158
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRV------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 159 kidQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMF 238
Cdd:cd03322 148 ---QLPKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 239 SKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCP--LGPIALAACLQVDATCHNAFIQEqslgih 316
Cdd:cd03322 225 SIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdLSPVGMAAALHLDLWVPNFGIQE------ 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489278596 317 YNKGTDLLDYIVDQKVFFyEDGYVRIPDGPGLGVDINEDHVRKMADIGHNWrnPVWRHKDGSIAEW 382
Cdd:cd03322 299 YMRHAEETLEVFPHSVRF-EDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYL--PVARLEDGTVHNW 361
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
130-355 |
9.46e-86 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 259.03 E-value: 9.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 130 LAAKQVVDKGFTAVKMNGTeelqyidsHEKIDQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIE 209
Cdd:pfam13378 5 EARRAVEARGFRAFKLKVG--------GPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 210 EPVLPENNEALRDIASLVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPLG 289
Cdd:pfam13378 77 EPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489278596 290 PIALAACLQVDATCHNAFIQEQSLGIHYnkgtdlLDYIVDQKVFFYEDGYVRIPDGPGLGVDINED 355
Cdd:pfam13378 157 PIGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-382 |
4.63e-74 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 235.57 E-value: 4.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 1 MKITGFECFLIPPRWLF--LKIETDEGITGWGEPVIEGKAATVKAAVGE-LMEYLIGKDPMNIEDHWNVMYRGGFYRGGP 77
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFvtLKITTDDGVTGLGDATLNGRELAVASYLQDhVCPLLIGRDAHRIEDIWQYLYRGAYWRRGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 78 ILMSAIAGIDQALWDIKGKFYNAPVHQLLGGKNRESIKVYSWIGG-DRPQDVGLAAKQvVDKGFTAVK-------MNGT- 148
Cdd:PRK15072 81 VTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGrDIDELLDDVARH-LELGYKAIRvqcgvpgLKTTy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 149 --------------------EELQyiDSHEKIDQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFI 208
Cdd:PRK15072 160 gvskgkglayepatkgllpeEELW--STEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 209 EEPVLPENNEALRDIASLVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCP- 287
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPt 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 288 -LGPIALAACLQVDATCHNAFIQEqslgihYNKGTDLLDYIVDQKVFFyEDGYVRIPDGPGLGVDINED----HVRKMAD 362
Cdd:PRK15072 318 dLSPVCMAAALHFDLWVPNFGIQE------YMGHSEETLEVFPHSYTF-EDGYLHPGDAPGLGVDFDEKlaakYPYEPAY 390
|
410 420
....*....|....*....|
gi 489278596 363 IghnwrnPVWRHKDGSIAEW 382
Cdd:PRK15072 391 L------PVARLEDGTMWNW 404
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
15-353 |
2.26e-69 |
|
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: 221.44 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 15 WLFLKIETDEGITGWGEPVieGKAATVKAAVGELMEYLIGKDPMNIEDHWNVMYRGG-FYRGGPILMSAIAGIDQALWDI 93
Cdd:cd03327 11 WLFVEIETDDGTVGYANTT--GGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATlAYGRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 94 KGKFYNAPVHQLLGGKNRESIKVY-SWIGGDRPQDVGLAAKQVVDKGFTAVKMngteELQY--IDSHEKIDQVIERISAV 170
Cdd:cd03327 89 LGKIRGEPVYKLLGGRTRDKIPAYaSGLYPTDLDELPDEAKEYLKEGYRGMKM----RFGYgpSDGHAGLRKNVELVRAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 171 REAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKWQFKNLLTDG 250
Cdd:cd03327 165 REAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 251 YVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCplgpiALAACLQVDATCHNAFIQEQSLGIHYNKGTDLLDYIVDQ 330
Cdd:cd03327 245 AVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA-----SQIYNYHFIMSEPNSPFAEYLPNSPDEVGNPLFYYIFLN 319
|
330 340
....*....|....*....|...
gi 489278596 331 KVfFYEDGYVRIPDGPGLGVDIN 353
Cdd:cd03327 320 EP-VPVNGYFDLSDKPGFGLELN 341
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
15-310 |
1.75e-47 |
|
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: 161.34 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 15 WLFLKIETDEGITGWGEpviegkaatvkaavgelmeyligkdpmniedhwnvmyrggfyrggpilmsAIAGIDQALWDIK 94
Cdd:cd00308 26 TVLVKLTTDSGVVGWGE--------------------------------------------------VISGIDMALWDLA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 95 GKFYNAPVHQLLGGKNRESIKVYSWIggdrpqdvglaakqvvdkgftavkmngteelqyidshekidqviERISAVREAV 174
Cdd:cd00308 56 AKALGVPLAELLGGGSRDRVPAYGSI--------------------------------------------ERVRAVREAF 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 175 GPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATgERMFSKWQFKN-LLTDGYVD 253
Cdd:cd00308 92 GPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA-DESVTTVDDALeALELGAVD 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489278596 254 IIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPLG-PIALAACLQVDATCHNAFIQE 310
Cdd:cd00308 171 ILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAALPNDRAIE 228
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
18-359 |
3.51e-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: 148.70 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 18 LKIETDEGITGW---GEPVIEgkAATVKAAvgeLMEYLIGKDPMNIEDHWNVMYRggFYRGGPILMsaIAGIDQALWDIK 94
Cdd:cd03329 37 LTIETDEGAKGHafgGRPVTD--PALVDRF---LKKVLIGQDPLDRERLWQDLWR--LQRGLTDRG--LGLVDIALWDLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 95 GKFYNAPVHQLLGGkNRESIKVY--SWIGGDR-----PQDVGLAAKQVVDKGFTAVKMNGteelqYIDSHEKIDqvIERI 167
Cdd:cd03329 108 GKYLGLPVHRLLGG-YREKIPAYasTMVGDDLeglesPEAYADFAEECKALGYRAIKLHP-----WGPGVVRRD--LKAC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 168 SAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSK-WQFKNL 246
Cdd:cd03329 180 LAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGAlESRADW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 247 LTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPlgpiaLAACLQVDATCHNAFIQEQSLGIHYNKGTDLLDY 326
Cdd:cd03329 260 VLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGN-----GAANLHVIAAIRNTRYYERGLLHPSQKYDVYAGY 334
|
330 340 350
....*....|....*....|....*....|...
gi 489278596 327 IVDQKVFFYEDGYVRIPDGPGLGVDINEDHVRK 359
Cdd:cd03329 335 LSVLDDPVDSDGFVHVPKGPGLGVEIDFDYIER 367
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-359 |
4.13e-40 |
|
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: 145.54 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 18 LKIETDEGITGWGEPVIEGKAA-------TVKAAVGE-LMEYLIGKDPMNIEDHWNVMYRGGFYRggpilMSAIAGIDQA 89
Cdd:cd03318 33 VRLTTSDGVVGIGEATTPGGPAwggespeTIKAIIDRyLAPLLIGRDATNIGAAMALLDRAVAGN-----LFAKAAIEMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 90 LWDIKGKFYNAPVHQLLGGKNRESIKVySWI--GGDRPQDVGLAAKQVVDKGFTA--VKMnGTEELQyidshekidQVIE 165
Cdd:cd03318 108 LLDAQGRRLGLPVSELLGGRVRDSLPV-AWTlaSGDTERDIAEAEEMLEAGRHRRfkLKM-GARPPA---------DDLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 166 RISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKWQFKN 245
Cdd:cd03318 177 HVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADAFE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 246 LLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCPL-GPIALAACLQVDATchnafIQEQSLGIHYNKGTDLL 324
Cdd:cd03318 257 LARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLeSSIGTAASAHLFAT-----LPSLPFGCELFGPLLLA 331
|
330 340 350
....*....|....*....|....*....|....*
gi 489278596 325 DYIVDQKvFFYEDGYVRIPDGPGLGVDINEDHVRK 359
Cdd:cd03318 332 EDLLEEP-LAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
25-285 |
2.05e-37 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 139.09 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 25 GITGWGEPVIEGKAA--TVKAAV---GE---------LMEYLIGKDPMNIEDHWNVMYRGGFYRG-GPILMSAIAGIDQA 89
Cdd:PRK15440 52 GINVLGTLVVEVEAEngQVGFAVstaGEmgafivekhLNRFIEGKCVSDIELIWDQMLNATLYYGrKGLVMNTISCVDLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 90 LWDIKGKFYNAPVHQLLGGKNRESIKVYSwiGGDRPqDVglaAKQVvdkGFTAVKMngteELQY--IDSHEKIDQVIERI 167
Cdd:PRK15440 132 LWDLLGKVRGLPVYKLLGGAVRDELQFYA--TGARP-DL---AKEM---GFIGGKM----PLHHgpADGDAGLRKNAAMV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 168 SAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLV--SIPIATGERMFSKWQFKN 245
Cdd:PRK15440 199 ADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNApaGMMVTSGEHEATLQGFRT 278
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489278596 246 LLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPH 285
Cdd:PRK15440 279 LLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
16-359 |
2.70e-30 |
|
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: 119.12 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 16 LFLKIETDEGITG--WGEPVIEGKAATVKAAVGELMEYLIGKD--PMNIEDHWNVMYRGGFYRGgpILMSAIAGIDQALW 91
Cdd:cd03321 32 VLIDLATDEGVTGhsYLFTYTPAALKSLKQLLDDMAALLVGEPlaPAELERALAKRFRLLGYTG--LVRMAAAGIDMAAW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 92 DIKGKFYNAPVHQLLGGKNReSIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMngteELQYIDSHEKIdqviERISAVR 171
Cdd:cd03321 110 DALAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAVTAAEEGFHAVKT----KIGYPTADEDL----AVVRSIR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 172 EAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKWQFKNLLTDGY 251
Cdd:cd03321 181 QAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 252 VDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHcpLGPIALAACLQVDATCHnafiqeqslGIHYnkgTDLLDYIVdQK 331
Cdd:cd03321 261 CDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH--LFQEISAHLLAVTPTAH---------WLEY---VDWAGAIL-EP 325
|
330 340
....*....|....*....|....*...
gi 489278596 332 VFFYEDGYVRIPDGPGLGVDINEDHVRK 359
Cdd:cd03321 326 PLKFEDGNAVIPDEPGNGIIWREKAVRK 353
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
14-107 |
1.44e-28 |
|
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: 107.94 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 14 RWLFLKIETDEGITGWGEPVIEGKAA-TVKAAVGE-LMEYLIGKDPMNIEDHWNVMYRGGFYrggpiLMSAIAGIDQALW 91
Cdd:pfam02746 27 SLVIVRIETSEGVVGIGEATSYGGRAeTIKAILDDhLAPLLIGRDAANISDLWQLMYRAALG-----NMSAKAAIDMALW 101
|
90
....*....|....*.
gi 489278596 92 DIKGKFYNAPVHQLLG 107
Cdd:pfam02746 102 DLKAKVLNLPLADLLG 117
|
|
| 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 ... |
19-280 |
4.35e-28 |
|
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: 111.90 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 19 KIETDeGITGWGE----PVIEGK-AATVKAAVGELMEYLIGKDPMNIEDH---WNVMYRGGfyrggpilmSAIAGIDQAL 90
Cdd:cd03319 31 EIELD-GITGYGEaaptPRVTGEtVESVLAALKSVRPALIGGDPRLEKLLealQELLPGNG---------AARAAVDIAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 91 WDIKGKFYNAPVHQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMNgteelqyIDSHEKIDqvIERISAV 170
Cdd:cd03319 101 WDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK-------LGGDLEDD--IERIRAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 171 REAVgPYIGIGID------FHGrvhkpmAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKWQFK 244
Cdd:cd03319 172 REAA-PDARLRVDanqgwtPEE------AVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAA 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 489278596 245 NLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDV 280
Cdd:cd03319 245 RLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGL 280
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
36-296 |
4.58e-25 |
|
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: 104.42 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 36 GKAATVKAAVGELMEYLIGKDPMNIEDHWNVMYRGGFYRGGPILMS-AIAGIDQALWDIKGKFYNAPVHQLLGgKNRESI 114
Cdd:cd03328 48 ADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAmAISAVDIALWDLKARLLGLPLARLLG-RAHDSV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 115 KVYSWIGGDRPQDVGLAAKQV--VDKGFTAVKMNgteelqyIDSHEKIDqvIERISAVREAVGPYIGIGIDFHGRVHKPM 192
Cdd:cd03328 127 PVYGSGGFTSYDDDRLREQLSgwVAQGIPRVKMK-------IGRDPRRD--PDRVAAARRAIGPDAELFVDANGAYSRKQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 193 AKILAKELEPFRPMFIEEPVLPENNEALRDI--ASLVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKK 270
Cdd:cd03328 198 ALALARAFADEGVTWFEEPVSSDDLAGLRLVreRGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQ 277
|
250 260
....*....|....*....|....*.
gi 489278596 271 ILSMAEAFDVAAAPHCPLGPIALAAC 296
Cdd:cd03328 278 AAALAAAHHVDLSAHCAPALHAHVAC 303
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
14-280 |
4.32e-23 |
|
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: 97.03 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 14 RWLFLKIETDEGITGWGEpviegkaatvkaavgelmeylIGKdpmniedhwnvmyrggfyrggpilmsaiAGIDQALWDI 93
Cdd:cd03315 25 DHVLLRLHTDDGLVGWAE---------------------ATK----------------------------AAVDMALWDL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 94 KGKFYNAPVhQLLGGKNRESIKVYSWIGGDRPQDVGLAAKQVVDKGFTAVKMNgteelqyIDSHEKIDqvIERISAVREA 173
Cdd:cd03315 56 WGKRLGVPV-YLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLK-------VGRDPARD--VAVVAALREA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 174 VGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLVSIPIATGERMFSKWQFKNLLTDGYVD 253
Cdd:cd03315 126 VGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDAFRELALGAAD 205
|
250 260
....*....|....*....|....*..
gi 489278596 254 IIQPDLSHAGGITECKKILSMAEAFDV 280
Cdd:cd03315 206 AVNIKTAKTGGLTKAQRVLAVAEALGL 232
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-285 |
8.08e-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: 93.18 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 17 FLKIETDE-GITGWGEPVIEGKAA-TVKAAVGELMEYLIGKDPMNIEDHWnvmyrGGFYRG----------GP---ILMS 81
Cdd:cd03324 35 YVVLRTDAaGLKGHGLTFTIGRGNeIVCAAIEALAHLVVGRDLESIVADM-----GKFWRRltsdsqlrwiGPekgVIHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 82 AIAGIDQALWDIKGKFYNAPVHQLL-----------------------------------GGKNRESI------KVYS-- 118
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqpGKAAREADllaegyPAYTts 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 119 --WIGGDRPQDVGLAaKQVVDKGFTAVKMNGTEELQyidshekidQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKIL 196
Cdd:cd03324 190 agWLGYSDEKLRRLC-KEALAQGFTHFKLKVGADLE---------DDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 197 AKELEPFRPMFIEEPVLPENNEALRDIA---SLVSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILS 273
Cdd:cd03324 260 VKQLAEFKPWWIEEPTSPDDILGHAAIRkalAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLL 339
|
330
....*....|..
gi 489278596 274 MAEAFDVAAAPH 285
Cdd:cd03324 340 MAAKFGVPVCPH 351
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
20-363 |
3.08e-20 |
|
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: 91.23 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 20 IETDEGITGWGEpvIEGKAATVkAAVGELMEYLIGKDPMNIEDHWNVMYRGGFYRGGP-----------ILMSAIAGIDQ 88
Cdd:cd03323 35 LTDDNGNTGVGE--SPGGAEAL-EALLEAARSLVGGDVFGAYLAVLESVRVAFADRDAggrglqtfdlrTTVHVVTAFEV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 89 ALWDIKGKFYNAPVHQLLGGKNRESIKV--YSWIGGDRPQD--------------------VGLAAKQVVDKGFTAVKMN 146
Cdd:cd03323 112 ALLDLLGQALGVPVADLLGGGQRDSVPFlaYLFYKGDRHKTdlpypwfrdrwgealtpegvVRLARAAIDRYGFKSFKLK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 147 GTEELQyidshekiDQVIERISAVREAVgPYIGIGIDFHGRVHKPMAKILAKELEPFRPmFIEEPVLpeNNEALRDIASL 226
Cdd:cd03323 192 GGVLPG--------EEEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGVLA-YLEDPCG--GREGMAEFRRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 227 VSIPIATGERMFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVAAAPHCP--LGpIALAACLQVDATCH 304
Cdd:cd03323 260 TGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNnhLG-ISLAMMTHVAAAAP 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489278596 305 NafiQEQSLGIHYNKGTDllDYIVDQKvFFYEDGYVRIPDGPGLGVDINEDHVRKMADI 363
Cdd:cd03323 339 G---LITACDTHWIWQDG--QVITGEP-LRIKDGKVAVPDKPGLGVELDRDKLAKAHEL 391
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
130-229 |
1.70e-18 |
|
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: 79.63 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 130 LAAKQVVDKGFTAVKMNGTEELqyidshekiDQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIE 209
Cdd:smart00922 7 AARRAVAEAGFRAVKVKVGGGP---------LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIE 77
|
90 100
....*....|....*....|
gi 489278596 210 EPVLPENNEALRDIASLVSI 229
Cdd:smart00922 78 EPVPPDDLEGLAELRRATPI 97
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
82-349 |
4.66e-17 |
|
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: 81.67 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 82 AIAGIDQALWDIKGKFYNAPVHQLLG-----GKNRESIKVYSWIGGDRPQD--VGLAA--KQVVDKGFTAVKMngteelq 152
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAAGGYYYPGDdlGRLRDemRRYLDRGYTVVKI------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 153 yidsheKI-----DQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRDIASLV 227
Cdd:cd03326 182 ------KIggaplDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 228 SIPIATGERMFSKWQFKNLLTDGYV----DIIQPDLSHAGGITECKKILSMAEA--FDVAAA-PHC-PLGPIALAACLQV 299
Cdd:cd03326 256 DGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAhgWSRRRFfPHGgHLMSLHIAAGLGL 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489278596 300 DATchnafiqEQSLGIHYNKGtdllDYIVDQKVffyEDGYVRIPDGPGLG 349
Cdd:cd03326 336 GGN-------ESYPDVFQPFG----GFADGCKV---ENGYVRLPDAPGIG 371
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
16-359 |
3.35e-13 |
|
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: 69.96 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 16 LFLKIETDEGITGWGEPVIEG----KAATVKAAVGELMEYLI----GKDpmnIEDHWNVMYRGGFYRGGPIlmsAIAGID 87
Cdd:cd03317 27 LIVELTDEEGITGYGEVVAFEgpfyTEETNATAWHILKDYLLplllGRE---FSHPEEVSERLAPIKGNNM---AKAGLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 88 QALWDIKGKFYNAPVHQLLGGkNRESIKVYSWIGGDRPQDVGLAA-KQVVDKGFTAVKMngteelqyidsheKID--QVI 164
Cdd:cd03317 101 MAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQLLKQiERYLEEGYKRIKL-------------KIKpgWDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 165 ERISAVREAVgPYIGIGIDFHGrvhkpmAKILA-----KELEPFRPMFIEEPvLPENNeaLRD---IASLVSIPIATGER 236
Cdd:cd03317 167 EPLKAVRERF-PDIPLMADANS------AYTLAdipllKRLDEYGLLMIEQP-LAADD--LIDhaeLQKLLKTPICLDES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 237 MFSKWQFKNLLTDGYVDIIQPDLSHAGGITECKKILSMAEAFDVaaapHCPLGP-----IALAACLQVDATCHNAFIQEQ 311
Cdd:cd03317 237 IQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI----PVWCGGmlesgIGRAHNVALASLPNFTYPGDI 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489278596 312 SLGIHYNKgTDlldyIVDQKVFFyEDGYVRIPDGPGLGVDINEDHVRK 359
Cdd:cd03317 313 SASSRYFE-ED----IITPPFEL-ENGIISVPTGPGIGVTVDREALKK 354
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
84-306 |
3.92e-05 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 44.94 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 84 AGIDQALWDikgkfYNAPVHQllGGKNRESIKVYSWIGGDRPQDVGLAAKQVvDKGFTAVKMngteelqyidsheKI--- 160
Cdd:cd03320 50 FGIESALAN-----LEALLVG--FTRPRNRIPVNALLPAGDAAALGEAKAAY-GGGYRTVKL-------------KVgat 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 161 --DQVIERISAVREAVGPYIGIGIDFHGRVHKPMAKILAKELEPFRPMFIEEPVLPENNEALRdiASLVSIPIATGERMF 238
Cdd:cd03320 109 sfEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELR--RLAAGVPIALDESLR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489278596 239 SKWQFKNLLTDGYVD--IIQPDLshAGGITECKKILSMAE----------AFDvaaaphcplGPIALAACLQVDATCHNA 306
Cdd:cd03320 187 RLDDPLALAAAGALGalVLKPAL--LGGPRALLELAEEARargipavvssALE---------SSIGLGALAHLAAALPPL 255
|
|
| |
