|
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: 796.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 1 MKITKITTYRLPPRWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHELGDYLIGQDPSRINDLWQVMYRAGFYRGGPILM 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGGFYRGGPILM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 81 SAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLNGCEELGLIDNSRAV 160
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNGTEELQYIDSPRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 161 DAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSR 240
Cdd:PRK14017 161 DAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 241 FDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHIDFVSYNAVLQEQSMGIHYNKG 320
Cdd:PRK14017 241 WDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49176390 321 AELLDFVKNKEDFSMVGGFFKPLTKPGLGVEIDEAKVIEFSKNAPDWRNPLWRHEDNSVAEW 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: 632.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 2 KITKITTYRLPPRWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHELGDYLIGQDPSRINDLWQVMYRAGFYRGGPILMS 81
Cdd:cd03325 1 KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGGFYRGGPVLMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 82 AIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLNGCEELGLIDNSRAVD 161
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELQWIDTSKKVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 162 AAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRF 241
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 242 DFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHIDFVSYNAVLQEQSMGIHYNKGA 321
Cdd:cd03325 241 DFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGD 320
|
330 340 350
....*....|....*....|....*....|..
gi 49176390 322 ELLDFVKNKEDFSMVGGFFKPLTKPGLGVEID 353
Cdd:cd03325 321 DLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-351 |
3.47e-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: 372.33 E-value: 3.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 2 KITKITTYRLPP------------RWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHE-LGDYLIGQDPSRINDLWQVMY 68
Cdd:cd03316 1 KITDVETFVLRVplpepggavtwrNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDlLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 69 RAGFYRG-GPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAY--SWVGGDRPADVIDGIKTLREIGFDTFKL 145
Cdd:cd03316 81 RRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYasGGGYDDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 146 NGceeLGLIDNSRAVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAA 225
Cdd:cd03316 161 KV---GGPDSGGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 226 QTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHIDFVSYN 305
Cdd:cd03316 238 ATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAALPN 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 49176390 306 AVLQEQSMGIHYnkgaelLDFVKNKEDFSMVGGFFKPLTKPGLGVE 351
Cdd:cd03316 318 FGILEYHLDDLP------LREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-357 |
1.83e-119 |
|
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: 350.28 E-value: 1.83e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 1 MKITKITTYRLPP----------------RWMFLKIETDEGVVGWGEPV-IEGRARTVEAAVHE-LGDYLIGQDPSRIND 62
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftisrgtrterDVVLVRVETDDGITGWGEAVpGGTGAEAVAAALEEaLAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 63 LWQVMYRAGFyrggpILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDT 142
Cdd:COG4948 81 LWQRLYRALP-----GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 143 FKLNgceeLGLIDnsraVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPK 222
Cdd:COG4948 156 LKLK----VGGPD----PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 223 LAAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPL-GPIALAACLHIDF 301
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 49176390 302 VSYNAVLQEQSMGIHYNKgaellDFVknKEDFSMVGGFFKPLTKPGLGVEIDEAKV 357
Cdd:COG4948 308 ALPNFDIVELDGPLLLAD-----DLV--EDPLRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-382 |
8.23e-79 |
|
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: 246.58 E-value: 8.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 2 KITKITTYRLPPRWMF--LKIETDEGVVGWGEPVIEGRARTVEAAVHE-LGDYLIGQDPSRINDLWQVMYRAGFYRGGPI 78
Cdd:cd03322 1 KITAIEVIVTCPGRNFvtLKITTDQGVTGLGDATLNGRELAVKAYLREhLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 79 LMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFdtfklngceelglidnsR 158
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGY-----------------R 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 159 AVDAAVNTVAQ-IREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERM 237
Cdd:cd03322 144 AIRVQLPKLFEaVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 238 FSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCP--LGPIALAACLHIDFVSYNAVLQEQsMGi 315
Cdd:cd03322 224 NSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdLSPVGMAAALHLDLWVPNFGIQEY-MR- 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49176390 316 HYNKGAELLdfvknKEDFSMVGGFFKPLTKPGLGVEIDEAKVIEFSKNAPDWrnPLWRHEDNSVAEW 382
Cdd:cd03322 302 HAEETLEVF-----PHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYL--PVARLEDGTVHNW 361
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
2-353 |
1.98e-72 |
|
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: 229.53 E-value: 1.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 2 KITKITTYRlppRWMFLKIETDEGVVGWGEPVieGRARTVEAAVHELGDYLIGQDPSRINDLWQVMYRAG-FYRGGPILM 80
Cdd:cd03327 1 KIKSVRTRV---GWLFVEIETDDGTVGYANTT--GGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATlAYGRKGIAM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 81 SAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAY-SWVGGDRPADVIDGIKTLREIGFDTFKLNGCEelGLIDNSRA 159
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYaSGLYPTDLDELPDEAKEYLKEGYRGMKMRFGY--GPSDGHAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 160 VDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFS 239
Cdd:cd03327 154 LRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 240 RFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCplgpiALAACLHIDFVSYNAVLQEQSMGIHYNK 319
Cdd:cd03327 234 VYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA-----SQIYNYHFIMSEPNSPFAEYLPNSPDEV 308
|
330 340 350
....*....|....*....|....*....|....
gi 49176390 320 GAELLDFVKNKEDFSmVGGFFKPLTKPGLGVEID 353
Cdd:cd03327 309 GNPLFYYIFLNEPVP-VNGYFDLSDKPGFGLELN 341
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
135-356 |
9.01e-72 |
|
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: 223.60 E-value: 9.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 135 LREIGFDTFKLNGCeelglidnSRAVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLA 214
Cdd:pfam13378 10 VEARGFRAFKLKVG--------GPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 215 EQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALA 294
Cdd:pfam13378 82 DDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPIGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49176390 295 ACLHIDFVSYNAVLQEQSMGIHYnkgaelLDFVKNKEDFSMVGGFFKPLTKPGLGVEIDEAK 356
Cdd:pfam13378 162 ASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-355 |
9.12e-65 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 211.69 E-value: 9.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 1 MKITKITTYRLPPRWMF--LKIETDEGVVGWGEPVIEGRARTVEAAvheLGDY----LIGQDPSRINDLWQVMYRAGFYR 74
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFvtLKITTDDGVTGLGDATLNGRELAVASY---LQDHvcplLIGRDAHRIEDIWQYLYRGAYWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 75 GGPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLN-------- 146
Cdd:PRK15072 78 RGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQcgvpglkt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 147 --GCEELGLIDNSRAVDAAVNTV----------------AQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFI 208
Cdd:PRK15072 158 tyGVSKGKGLAYEPATKGLLPEEelwstekylrfvpklfEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 209 EEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCP- 287
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPt 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176390 288 -LGPIALAACLHIDFVSYNAVLQEqsmgihYNKGAELLDFVkNKEDFSMVGGFFKPLTKPGLGVEIDEA 355
Cdd:PRK15072 318 dLSPVCMAAALHFDLWVPNFGIQE------YMGHSEETLEV-FPHSYTFEDGYLHPGDAPGLGVDFDEK 379
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
15-310 |
2.46e-57 |
|
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: 186.76 E-value: 2.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 15 WMFLKIETDEGVVGWGEpviegrartveaavhelgdyligqdpsrindlwqvmyragfyrggpilmsAIAGIDQALWDIK 94
Cdd:cd00308 26 TVLVKLTTDSGVVGWGE--------------------------------------------------VISGIDMALWDLA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 95 GKVLNAPVWQLMGGLVRDKIKAYSWVggdrpadvidgiktlreigfdtfklngceelglidnsravdaavNTVAQIREAF 174
Cdd:cd00308 56 AKALGVPLAELLGGGSRDRVPAYGSI--------------------------------------------ERVRAVREAF 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 175 GNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAgERMFSRFDFK-RVLEAGGIS 253
Cdd:cd00308 92 GPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA-DESVTTVDDAlEALELGAVD 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176390 254 ILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLG-PIALAACLHIDFVSYNAVLQE 310
Cdd:cd00308 171 ILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAALPNDRAIE 228
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-107 |
2.28e-36 |
|
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: 128.36 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 5 KITTYRLPPRWM-----------------FLKIETDEGVVGWGEPVIEG-RARTVEAAVHE-LGDYLIGQDPSRINDLWQ 65
Cdd:pfam02746 1 AIEVFVVDVGWPlrpiqmafgtvqqqslvIVRIETSEGVVGIGEATSYGgRAETIKAILDDhLAPLLIGRDAANISDLWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 49176390 66 VMYRAGFYrggpiLMSAIAGIDQALWDIKGKVLNAPVWQLMG 107
Cdd:pfam02746 81 LMYRAALG-----NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
20-285 |
2.79e-34 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 130.62 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 20 IETDEGVVGW-----GEPViegrARTVEaavHELGDYLIGQDPSRINDLWQVMYRAGFYRG-GPILMSAIAGIDQALWDI 93
Cdd:PRK15440 63 VEAENGQVGFavstaGEMG----AFIVE---KHLNRFIEGKCVSDIELIWDQMLNATLYYGrKGLVMNTISCVDLALWDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 94 KGKVLNAPVWQLMGGLVRDKIKAYSwvGGDRPaDVIdgiktlREIGFDTFKLNgcEELGLIDNSRAVDAAVNTVAQIREA 173
Cdd:PRK15440 136 LGKVRGLPVYKLLGGAVRDELQFYA--TGARP-DLA------KEMGFIGGKMP--LHHGPADGDAGLRKNAAMVADMREK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 174 FGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKL--AAQTHIPLAAGERMFSRFDFKRVLEAGG 251
Cdd:PRK15440 205 VGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELkrNAPAGMMVTSGEHEATLQGFRTLLEMGC 284
|
250 260 270
....*....|....*....|....*....|....
gi 49176390 252 ISILQPDLSHAGGITECYKIAGMAEAYDVTLAPH 285
Cdd:PRK15440 285 IDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-357 |
3.31e-34 |
|
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: 129.74 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 18 LKIETDEGVVGWGEPV-IEGRA---RTVEAAVHELGDYL----IGQDPSRINDLWQVMYRAGFYRggpilMSAIAGIDQA 89
Cdd:cd03318 33 VRLTTSDGVVGIGEATtPGGPAwggESPETIKAIIDRYLapllIGRDATNIGAAMALLDRAVAGN-----LFAKAAIEMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 90 LWDIKGKVLNAPVWQLMGGLVRDKIK-AYSWVGGDRPADvIDGIKTLREIG-FDTFKLngceELGlidnSRAVDAAVNTV 167
Cdd:cd03318 108 LLDAQGRRLGLPVSELLGGRVRDSLPvAWTLASGDTERD-IAEAEEMLEAGrHRRFKL----KMG----ARPPADDLAHV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 168 AQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVL 247
Cdd:cd03318 179 EAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADAFELA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 248 EAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPL-GPIALAACLH----IDFVSYNAVLqeqsMGIHYNKgAE 322
Cdd:cd03318 259 RRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLeSSIGTAASAHlfatLPSLPFGCEL----FGPLLLA-ED 333
|
330 340 350
....*....|....*....|....*....|....*
gi 49176390 323 LLDFVKNKEDFSMVggffKPlTKPGLGVEIDEAKV 357
Cdd:cd03318 334 LLEEPLAYRDGELH----VP-TGPGLGVRLDEDKV 363
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
18-353 |
1.42e-32 |
|
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: 125.59 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 18 LKIETDEGVVGWGepvIEGRARTVEAAVHE-LGDYLIGQDPSRINDLWQVMYRAgfYRGGPILMsaIAGIDQALWDIKGK 96
Cdd:cd03329 37 LTIETDEGAKGHA---FGGRPVTDPALVDRfLKKVLIGQDPLDRERLWQDLWRL--QRGLTDRG--LGLVDIALWDLAGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 97 VLNAPVWQLMGGLvRDKIKAY--SWVGGDR-----PADVIDGIKTLREIGFDTFKLNGcEELGLIDNSRAVDAAVntvaq 169
Cdd:cd03329 110 YLGLPVHRLLGGY-REKIPAYasTMVGDDLeglesPEAYADFAEECKALGYRAIKLHP-WGPGVVRRDLKACLAV----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 170 iREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGE----RMFSRFDFKR 245
Cdd:cd03329 183 -REAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEhsrgALESRADWVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 246 vleAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPlGPI---ALAACLHIDF--VSYNAVLQEQSMGIHYnkG 320
Cdd:cd03329 262 ---AGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGN-GAAnlhVIAAIRNTRYyeRGLLHPSQKYDVYAGY--L 335
|
330 340 350
....*....|....*....|....*....|...
gi 49176390 321 AELLDFVKNKedfsmvgGFFKPLTKPGLGVEID 353
Cdd:cd03329 336 SVLDDPVDSD-------GFVHVPKGPGLGVEID 361
|
|
| 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 ... |
19-302 |
9.59e-31 |
|
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: 119.22 E-value: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 19 KIETDeGVVGWGE----PVIEG-RARTVEAAVHELGDYLIGQDPsRINDLWQVMYRAGfyrggPILMSAIAGIDQALWDI 93
Cdd:cd03319 31 EIELD-GITGYGEaaptPRVTGeTVESVLAALKSVRPALIGGDP-RLEKLLEALQELL-----PGNGAARAAVDIALWDL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 94 KGKVLNAPVWQLMGGLVRDKIK-AYSwVGGDRPADVIDGIKTLREIGFDTFKLngceELGLidnsrAVDAAVNTVAQIRE 172
Cdd:cd03319 104 EAKLLGLPLYQLWGGGAPRPLEtDYT-ISIDTPEAMAAAAKKAAKRGFPLLKI----KLGG-----DLEDDIERIRAIRE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 173 AFGNqIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLE---A 249
Cdd:cd03319 174 AAPD-ARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLAGggaY 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 49176390 250 GGISIlqpDLSHAGGITECYKIAGMAEAYDVTLAPHCPLG------PIALAACLHIDFV 302
Cdd:cd03319 253 DGINI---KLMKTGGLTEALRIADLARAAGLKVMVGCMVEsslsiaAAAHLAAAKADFV 308
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
14-282 |
5.63e-26 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 105.12 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 14 RWMFLKIETDEGVVGWGEpviegrartveaavhelgdyligqdpsrindlwqvmyragfyrggpilmSAIAGIDQALWDI 93
Cdd:cd03315 25 DHVLLRLHTDDGLVGWAE-------------------------------------------------ATKAAVDMALWDL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 94 KGKVLNAPVWQLMGGlVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLNGceelglidnSRAVDAAVNTVAQIREA 173
Cdd:cd03315 56 WGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKV---------GRDPARDVAVVAALREA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 174 FGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGIS 253
Cdd:cd03315 126 VGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDAFRELALGAAD 205
|
250 260
....*....|....*....|....*....
gi 49176390 254 ILQPDLSHAGGITECYKIAGMAEAYDVTL 282
Cdd:cd03315 206 AVNIKTAKTGGLTKAQRVLAVAEALGLPV 234
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
18-357 |
1.09e-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: 97.94 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 18 LKIETDEGVVG--WGEPVIEGRARTVEAAVHELGDYLIGQD--PSRINDLWQVMYRAGFYRGgpILMSAIAGIDQALWDI 93
Cdd:cd03321 34 IDLATDEGVTGhsYLFTYTPAALKSLKQLLDDMAALLVGEPlaPAELERALAKRFRLLGYTG--LVRMAAAGIDMAAWDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 94 KGKVLNAPVWQLMGGLVRdKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLngceELGLIDnsRAVDAAVntVAQIREA 173
Cdd:cd03321 112 LAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAVTAAEEGFHAVKT----KIGYPT--ADEDLAV--VRSIRQA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 174 FGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGIS 253
Cdd:cd03321 183 VGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 254 ILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCplgpialaaclhidFVSYNAVLQEQSMGIHYNKGAELLDFVKnKEDF 333
Cdd:cd03321 263 LVMPDLMKIGGVTGWLRASALAEQAGIPMSSHL--------------FQEISAHLLAVTPTAHWLEYVDWAGAIL-EPPL 327
|
330 340
....*....|....*....|....
gi 49176390 334 SMVGGFFKPLTKPGLGVEIDEAKV 357
Cdd:cd03321 328 KFEDGNAVIPDEPGNGIIWREKAV 351
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
46-355 |
2.40e-20 |
|
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: 90.93 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 46 HELGDYLIGQDPSRINDLWQVMYRAGFYRGGPILMS-AIAGIDQALWDIKGKVLNAPVWQLMGGlVRDKIKAYSwvggdr 124
Cdd:cd03328 58 GLLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAmAISAVDIALWDLKARLLGLPLARLLGR-AHDSVPVYG------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 125 padviDGiktlreiGFDTFKLNG-CEELG--LIDNSRAVDAAVNT--------VAQIREAFGNQIEFGLDFHGRVSAPMA 193
Cdd:cd03328 131 -----SG-------GFTSYDDDRlREQLSgwVAQGIPRVKMKIGRdprrdpdrVAAARRAIGPDAELFVDANGAYSRKQA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 194 KVLIKELEPYRPLFIEEPVLAEQAEyypKLAA-QTHIP----LAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITEC 268
Cdd:cd03328 199 LALARAFADEGVTWFEEPVSSDDLA---GLRLvRERGPagmdIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 269 YKIAGMAEAYDVTLAPHCplgpiALAACLHIDFVSYNAVLQEQSMGiHYNKGAELLDFVknkedFSMVGGFFKP-LTKPG 347
Cdd:cd03328 276 LQAAALAAAHHVDLSAHC-----APALHAHVACAVPRLRHLEWFHD-HVRIERMLFDGA-----PDPSGGALRPdLSRPG 344
|
....*...
gi 49176390 348 LGVEIDEA 355
Cdd:cd03328 345 LGLELRAR 352
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
18-357 |
3.18e-17 |
|
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: 81.90 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 18 LKIETDEGVVGWGEPVIEG----RARTVEAAVHELGDYLIGQDPSR-INDLWQVMYRAGFYRGGPIlmsAIAGIDQALWD 92
Cdd:cd03317 29 VELTDEEGITGYGEVVAFEgpfyTEETNATAWHILKDYLLPLLLGReFSHPEEVSERLAPIKGNNM---AKAGLEMAVWD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 93 IKGKVLNAPVWQLMGGlVRDKIKAYSWVG-GDRPADVIDGIKTLREIGFDTFKLNgceelglIDnsRAVDAAVntVAQIR 171
Cdd:cd03317 106 LYAKAQGQSLAQYLGG-TRDSIPVGVSIGiQDDVEQLLKQIERYLEEGYKRIKLK-------IK--PGWDVEP--LKAVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 172 EAFGnQIEFGLDFHG---RVSAPmakvLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLE 248
Cdd:cd03317 174 ERFP-DIPLMADANSaytLADIP----LLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAEDARKAIE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 249 AGGISILQPDLSHAGGITECYKIA-------------GMAEAyDVTLAPHcplgpIALAACLHIDF---VSYNAvlqeqs 312
Cdd:cd03317 249 LGACKIINIKPGRVGGLTEALKIHdlcqehgipvwcgGMLES-GIGRAHN-----VALASLPNFTYpgdISASS------ 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 49176390 313 mgiHYNKGaellDFVknKEDFSMVGGFFKPLTKPGLGVEIDEAKV 357
Cdd:cd03317 317 ---RYFEE----DII--TPPFELENGIISVPTGPGIGVTVDREAL 352
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-352 |
1.26e-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: 80.85 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 17 FLKIETDE-GVVGWGEPVIEGRARTVE-AAVHELGDYLIGQDPSRINDLWqvmyrAGFYRG----------GP---ILMS 81
Cdd:cd03324 35 YVVLRTDAaGLKGHGLTFTIGRGNEIVcAAIEALAHLVVGRDLESIVADM-----GKFWRRltsdsqlrwiGPekgVIHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 82 AIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKA---YSWVGgD--RPADVID-----------GIKTLREIGFDTFKl 145
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVScidFRYIT-DalTPEEALEilrrgqpgkaaREADLLAEGYPAYT- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 146 NGCEELGLIDN------SRAVDAAVNTVAQ---------------IREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYR 204
Cdd:cd03324 188 TSAGWLGYSDEklrrlcKEALAQGFTHFKLkvgadleddirrcrlAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 205 PLFIEEPVLAEQAEYYPKLA---AQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVT 281
Cdd:cd03324 268 PWWIEEPTSPDDILGHAAIRkalAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVP 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176390 282 LAPHCplGPIALA-ACLH---IDFVSYNAVLQeqsmgihyNKGAELLDFVknKEDF----SMVGGFFKPLTKPGLGVEI 352
Cdd:cd03324 348 VCPHA--GGVGLCeLVQHlsmIDYICVSGSKE--------GRVIEYVDHL--HEHFvypvVIQNGAYMPPTDPGYSIEM 414
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
125-229 |
1.42e-15 |
|
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: 71.54 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 125 PADVIDGIKT-LREIGFDTFKLNGCeelglidnsRAVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPY 203
Cdd:smart00922 1 PEELAEAARRaVAEAGFRAVKVKVG---------GGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDEL 71
|
90 100
....*....|....*....|....*.
gi 49176390 204 RPLFIEEPVLAEQAEYYPKLAAQTHI 229
Cdd:smart00922 72 GLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
20-359 |
2.45e-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: 73.90 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 20 IETDEGVVGWGEPV--IEGRARTVEAAVHELGDYLIGQDPSRINDLWQVMYRAGFYRGGPILMS------AIAGIDQALW 91
Cdd:cd03323 35 LTDDNGNTGVGESPggAEALEALLEAARSLVGGDVFGAYLAVLESVRVAFADRDAGGRGLQTFDlrttvhVVTAFEVALL 114
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 92 DIKGKVLNAPVWQLMGGLVRDKIK--AYSWVGGDRPAD---------------VIDGIKTLREI-----GFDTFKLNGce 149
Cdd:cd03323 115 DLLGQALGVPVADLLGGGQRDSVPflAYLFYKGDRHKTdlpypwfrdrwgealTPEGVVRLARAaidryGFKSFKLKG-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 150 elGLIDNSRAVDAavntVAQIREAF-GNQIEfgLDFHGRVSAPMAKVLIKELE---PYrplfIEEPVLAEQ--AEyypkL 223
Cdd:cd03323 193 --GVLPGEEEIEA----VKALAEAFpGARLR--LDPNGAWSLETAIRLAKELEgvlAY----LEDPCGGREgmAE----F 256
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 224 AAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCP--LGpIALAACLHIdf 301
Cdd:cd03323 257 RRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNnhLG-ISLAMMTHV-- 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 302 vsyNAVLQEQSMGI--HYNKGAEllDFVKnKEDFSMVGGFFKPLTKPGLGVEIDEAKVIE 359
Cdd:cd03323 334 ---AAAAPGLITACdtHWIWQDG--QVIT-GEPLRIKDGKVAVPDKPGLGVELDRDKLAK 387
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| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
38-277 |
1.23e-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: 59.33 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 38 ARTVEAAVHELGDYLIGQ-DPSRIndlWQVMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRD---- 112
Cdd:cd03326 67 PRLLAAAPDSLLDDAGGNlDPARA---WAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRgqad 143
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 113 -KIKAYSWVGGDRPADVIDGIKtlREI------GFDTFKLN-GCEELGliDNSRAVDAAVntvaqirEAFGNQIEFGLDF 184
Cdd:cd03326 144 pRVPVYAAGGYYYPGDDLGRLR--DEMrryldrGYTVVKIKiGGAPLD--EDLRRIEAAL-------DVLGDGARLAVDA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 185 HGRVSAPMAKVLIKELEPYRPLFIEEP-------VLAEQAEYYPKlaaqthiPLAAGERMFSRFDFKRVLEAGGI----S 253
Cdd:cd03326 213 NGRFDLETAIAYAKALAPYGLRWYEEPgdpldyaLQAELADHYDG-------PIATGENLFSLQDARNLLRYGGMrpdrD 285
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250 260
....*....|....*....|....
gi 49176390 254 ILQPDLSHAGGITECYKIAGMAEA 277
Cdd:cd03326 286 VLQFDPGLSYGLPEYLRMLDVLEA 309
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|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
84-280 |
5.54e-07 |
|
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: 50.34 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 84 AGIDQALWDikgkvLNAPVWQLMGGLVRDKIKAYSWVGgdrPADVIDGIKTLREIGFDTFKLngceELGLIDNsravDAA 163
Cdd:cd03320 50 FGIESALAN-----LEALLVGFTRPRNRIPVNALLPAG---DAAALGEAKAAYGGGYRTVKL----KVGATSF----EED 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176390 164 VNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQaeyYPKLAAQTH-IPLAAGERMFSRFD 242
Cdd:cd03320 114 LARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDD---LAELRRLAAgVPIALDESLRRLDD 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 49176390 243 FKRVLEAG--GISILQPDLshAGGITECYKIAGMAEAYDV 280
Cdd:cd03320 191 PLALAAAGalGALVLKPAL--LGGPRALLELAEEARARGI 228
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