|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
7-357 |
1.68e-126 |
|
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: 367.71 E-value: 1.68e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 7 IRHVKLSTARLPLAVPisdakvftgrQKPMTEVVFLFAEITTEQGHSGIGFSYSKRAGGPAQYAHAREVAEGIIGEDPND 86
Cdd:cd03316 2 ITDVETFVLRVPLPEP----------GGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 87 IGRLYTKLLWAGASVGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLGAY-RDSVQTYNtSGGFLHASLAEVKARATVL 165
Cdd:cd03316 72 IERLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKvRDRVRVYA-SGGGYDDSPEELAEEAKRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 166 LDEGIGGIKIKVGLPDTA-----EDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFE 240
Cdd:cd03316 151 VAEGFTAVKLKVGGPDSGgedlrEDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 241 GHADLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFA-----MEIHLH 315
Cdd:cd03316 231 GLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAggpigLAASLH 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 517603070 316 LAAAYPREPWVEHFDWLDP----LFNERLETKNGRMLVPDRPGLGI 357
Cdd:cd03316 311 LAAALPNFGILEYHLDDLPlredLFKNPPEIEDGYVTVPDRPGLGV 356
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
7-363 |
9.34e-104 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 309.83 E-value: 9.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 7 IRHVKLSTARLPLAVPisdakvFTGRQKPMTEVVFLFAEITTEQGHSGIGFSYSKRAGGPAQYAHARE-VAEGIIGEDPN 85
Cdd:COG4948 3 ITDIEVYPVRLPLKRP------FTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGAEAVAAALEEaLAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 86 DIGRLYTKLLwagasvGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLG-AYRDSVQTYNTSGgflHASLAEVKARATV 164
Cdd:COG4948 77 DIEALWQRLY------RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGgKVRDRVPVYATLG---IDTPEEMAEEARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 165 LLDEGIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHAD 244
Cdd:COG4948 148 AVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 245 LARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFAME------IHLHLAA 318
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLEsgiglaAALHLAA 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517603070 319 AYPREPWVEHFD---WLDPLFNERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:COG4948 308 ALPNFDIVELDGpllLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDA 355
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
157-363 |
8.69e-78 |
|
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: 238.62 E-value: 8.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 157 EVKARATVLLDE-GIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLD 235
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 236 AYDFEGHADLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHF-----AM 310
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSgggpiGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517603070 311 EIHLHLAAAYPREPWVEHF----DWLDPLFNERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:pfam13378 161 AASLHLAAAVPNLLIQEYFldplLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
6-363 |
6.25e-71 |
|
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: 225.82 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 6 LIRHVKLSTARLPLAVPISDAkVFTGRQKPMtevvfLFAEITTEQGHSG--IGFSYSKRAGGPAQyAHAREVAEGIIGED 83
Cdd:cd03321 2 LITGLRARAVNVPMQYPVHTS-VGTVATAPL-----VLIDLATDEGVTGhsYLFTYTPAALKSLK-QLLDDMAALLVGEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 84 --PNDIGRLYTKLLwagASVGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVQTYNTSGGFLHASLAEvkaR 161
Cdd:cd03321 75 laPAELERALAKRF---RLLGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATE---R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 162 ATVLLDEGIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEG 241
Cdd:cd03321 149 AVTAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 242 HADLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFAMEIHLHLAAAYP 321
Cdd:cd03321 229 HARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVTP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517603070 322 REPWVEHFDWLDPLFNERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:cd03321 309 TAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKA 350
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
42-360 |
2.92e-67 |
|
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: 216.04 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 42 LFAEITTEQGHSGIgfsYSKRAGGPAQYAHAREVAEGIIGEDPNDIGRLYTKLLWAGASVGRSGVATQALAAIDIALYDL 121
Cdd:cd03327 12 LFVEIETDDGTVGY---ANTTGGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 122 KAKRAGLPLAKFLG-AYRDSVQTYNTsgGFLHASLAEVKARATVLLDEGIGGIKIKV--GLPDTAEDLRR----VAGIRE 194
Cdd:cd03327 89 LGKIRGEPVYKLLGgRTRDKIPAYAS--GLYPTDLDELPDEAKEYLKEGYRGMKMRFgyGPSDGHAGLRKnvelVRAIRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 195 HIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAEHKGLISANGC 274
Cdd:cd03327 167 AVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 275 DIIQPDAPRVGGITQFLRLAALADERGLGLAPHfAMEIH-LHLAAAYPREPWVEHF----DWL-DPLFNERLET----KN 344
Cdd:cd03327 247 DILQPDVNWVGGITELKKIAALAEAYGVPVVPH-ASQIYnYHFIMSEPNSPFAEYLpnspDEVgNPLFYYIFLNepvpVN 325
|
330
....*....|....*.
gi 517603070 345 GRMLVPDRPGLGISLS 360
Cdd:cd03327 326 GYFDLSDKPGFGLELN 341
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
51-361 |
1.56e-58 |
|
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: 193.78 E-value: 1.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 51 GHSGIGFSYSKRAGgpAQYAHArEVAEGIIGEDPNDIGRLYTKLLWAGASVGRSGVATQALAAIDIALYDLKAKRAGLPL 130
Cdd:cd03328 39 GRTGLGYTYADAAA--AALVDG-LLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAMAISAVDIALWDLKARLLGLPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 131 AKFLGAYRDSVQTYNtSGGFLHASLAEVKARATVLLDEGIGGIKIKVGlPDTAEDLRRVAGIREHIGWDVPLMVDANQQW 210
Cdd:cd03328 116 ARLLGRAHDSVPVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIG-RDPRRDPDRVAAARRAIGPDAELFVDANGAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 211 DRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADL-ARA-LDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGIT 288
Cdd:cd03328 194 SRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVrERGpAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 289 QFLRLAALADERGLGLAPHFAMEIHLHLAAAYPRepwVEHFDWLDP-------LFNERLETKNGrMLVPD--RPGLGISL 359
Cdd:cd03328 274 GFLQAAALAAAHHVDLSAHCAPALHAHVACAVPR---LRHLEWFHDhvriermLFDGAPDPSGG-ALRPDlsRPGLGLEL 349
|
..
gi 517603070 360 SE 361
Cdd:cd03328 350 RA 351
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
41-360 |
5.59e-48 |
|
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: 165.96 E-value: 5.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 41 FLFAEITTEQGHSGIG-FSYSKRAGgpAQYAHAREVAEGIIGEDPNDIGRLYTKL----LWAGASVGRSgvatqALAAID 115
Cdd:cd03325 14 WLFVKIETDEGVVGWGePTVEGKAR--TVEAAVQELEDYLIGKDPMNIEHHWQVMyrggFYRGGPVLMS-----AISGID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 116 IALYDLKAKRAGLPLAKFLG-AYRDSVQTYNTSGGflhASLAEVKARATVLLDEGIGGIKikVGLPDTAEDL-------- 186
Cdd:cd03325 87 QALWDIKGKVLGVPVHQLLGgQVRDRVRVYSWIGG---DRPSDVAEAARARREAGFTAVK--MNATEELQWIdtskkvda 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 187 --RRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAE 264
Cdd:cd03325 162 avERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 265 HKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPH-----FAMEIHLHLAAAYP----------REPWVEHf 329
Cdd:cd03325 242 FKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHcplgpIALAASLHVDASTPnfliqeqslgIHYNEGD- 320
|
330 340 350
....*....|....*....|....*....|..
gi 517603070 330 DWLDPLFN-ERLETKNGRMLVPDRPGLGISLS 360
Cdd:cd03325 321 DLLDYLVDpEVFDMENGYVKLPTGPGLGIEID 352
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
7-356 |
4.27e-47 |
|
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: 164.11 E-value: 4.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 7 IRHVKLSTARLPLAVPISDAKVFTGRQKPMTEVVFLfaEITTEQGHSGIGFSYSKRAGGPAQYAHAREVaegIIGEDPND 86
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALL--TIETDEGAKGHAFGGRPVTDPALVDRFLKKV---LIGQDPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 87 IGRLYTKLL-WAGASVGRsgvatqALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVQTY-NTSGGFLHASLAEVKARATV 164
Cdd:cd03329 77 RERLWQDLWrLQRGLTDR------GLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYaSTMVGDDLEGLESPEAYADF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 165 ---LLDEGIGGIKIKV-GLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFE 240
Cdd:cd03329 151 aeeCKALGYRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 241 GHADLARALDTPIATGEMLASVAEHKG-LISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFAMEIHLHLAAA 319
Cdd:cd03329 231 SYRWLAEKLDIPILGTEHSRGALESRAdWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGAANLHVIAA 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 517603070 320 YPREPWVE--------HFDWLDPLFNERLET--KNGRMLVPDRPGLG 356
Cdd:cd03329 311 IRNTRYYErgllhpsqKYDVYAGYLSVLDDPvdSDGFVHVPKGPGLG 357
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
112-327 |
6.40e-44 |
|
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: 151.71 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 112 AAIDIALYDLKAKRAGLPLA-KFLGAYRDSVQTYNTsggflhaslaevkaratvlldegiggikikvglpdtaedLRRVA 190
Cdd:cd00308 45 SGIDMALWDLAAKALGVPLAeLLGGGSRDRVPAYGS---------------------------------------IERVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 191 GIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAEHKGLIS 270
Cdd:cd00308 86 AVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALEALE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517603070 271 ANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPH------FAMEIHLHLAAAYPREPWVE 327
Cdd:cd00308 166 LGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHgtlessIGTAAALHLAAALPNDRAIE 228
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
42-359 |
5.89e-42 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 151.03 E-value: 5.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 42 LFAEITTEQGHsgIGFSYSKrAGGPAQYAHAREVAEGIIGEDPNDIGRLYTKLLWAGASVGRSGVATQALAAIDIALYDL 121
Cdd:PRK15440 59 LVVEVEAENGQ--VGFAVST-AGEMGAFIVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDLALWDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 122 KAKRAGLPLAKFLG-AYRDSVQTYNTSG--------GFLHASLAEVKARAtvlldEGIGGIKikvglpdtaEDLRRVAGI 192
Cdd:PRK15440 136 LGKVRGLPVYKLLGgAVRDELQFYATGArpdlakemGFIGGKMPLHHGPA-----DGDAGLR---------KNAAMVADM 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 193 REHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTP--IATGEMLASVAEHKGLIS 270
Cdd:PRK15440 202 REKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGmmVTSGEHEATLQGFRTLLE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 271 ANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFAMEIHLHLAAAYPREPWVEHF------DWLDPLFNERLETK- 343
Cdd:PRK15440 282 MGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYSHHFVITRTNSPFSEFLmmspdaDTVVPQFDPILLDEp 361
|
330 340
....*....|....*....|.
gi 517603070 344 ---NGRMLVP--DRPGLGISL 359
Cdd:PRK15440 362 vpvNGRIHKSvlDKPGFGVEL 382
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
19-361 |
6.94e-41 |
|
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: 147.46 E-value: 6.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 19 LAVPISDAKVFTGRQKPMTEVVFLfaEITTEQGHSGIGfsyskRAGGPAQYAHAREVAEGI------------IGEDPND 86
Cdd:cd03318 10 VDLPTRRPHQFAGTTMHTQSLVLV--RLTTSDGVVGIG-----EATTPGGPAWGGESPETIkaiidrylapllIGRDATN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 87 IGRLYTKLlwAGASVGrsgvATQALAAIDIALYDLKAKRAGLPLAKFLG-AYRDSVQ-TYNTSGGFLHASLAEvkarATV 164
Cdd:cd03318 83 IGAAMALL--DRAVAG----NLFAKAAIEMALLDAQGRRLGLPVSELLGgRVRDSLPvAWTLASGDTERDIAE----AEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 165 LLDEGI-GGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHA 243
Cdd:cd03318 153 MLEAGRhRRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 244 DLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFAME------IHLHLA 317
Cdd:cd03318 233 RLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLEssigtaASAHLF 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 517603070 318 AAYPREPW-VEHFDWL---DPLFNERLETKNGRMLVPDRPGLGISLSE 361
Cdd:cd03318 313 ATLPSLPFgCELFGPLllaEDLLEEPLAYRDGELHVPTGPGLGVRLDE 360
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
100-304 |
7.06e-41 |
|
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: 144.79 E-value: 7.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 100 SVGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVQTYNTSGGflhASLAEVKARATVLLDEGIGGIKIKVGl 179
Cdd:cd03315 34 DDGLVGWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGL---GEPAEVAEEARRALEAGFRTFKLKVG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 180 PDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEML 259
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517603070 260 ASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGL 304
Cdd:cd03315 190 FTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPV 234
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
47-357 |
1.13e-40 |
|
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: 148.26 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 47 TTEQGHSGIGFSYSKRAGGPAQYAHAREVAEGIIGEDPNDI----GRLYTKLL------WAGASvgrSGVATQALAAIDI 116
Cdd:cd03324 40 TDAAGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIvadmGKFWRRLTsdsqlrWIGPE---KGVIHLATAAVVN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 117 ALYDLKAKRAGLPLAKFLG------------------------------------------AYRDSVQTYNTSGGFLHAS 154
Cdd:cd03324 117 AVWDLWAKAEGKPLWKLLVdmtpeelvscidfryitdaltpeealeilrrgqpgkaareadLLAEGYPAYTTSAGWLGYS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 155 LAEVKARATVLLDEGIGGIKIKVGlPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPL 234
Cdd:cd03324 197 DEKLRRLCKEALAQGFTHFKLKVG-ADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 235 DAYDFEGHADLARALDT---PIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFA-- 309
Cdd:cd03324 276 SPDDILGHAAIRKALAPlpiGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGgv 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 517603070 310 ----MEIHL----HLAAAYPREPWV-EHFDWLDPLFNERLETKNGRMLVPDRPGLGI 357
Cdd:cd03324 356 glceLVQHLsmidYICVSGSKEGRViEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSI 412
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
42-363 |
3.81e-39 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 143.50 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 42 LFAEITTEQGHSGIGfsySKRAGGPAQYAHA--REVAEGIIGEDPNDIGRLYTKLLWAGASVGrSGVATQALAAIDIALY 119
Cdd:PRK14017 16 LFLKIETDEGIVGWG---EPVVEGRARTVEAavHELADYLIGKDPRRIEDHWQVMYRGGFYRG-GPILMSAIAGIDQALW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 120 DLKAKRAGLPLAKFLG-AYRDSVQTYNTSGGflhASLAEVKARATVLLDEGIGGIKI----KVGLPDTAED----LRRVA 190
Cdd:PRK14017 92 DIKGKALGVPVHELLGgLVRDRIRVYSWIGG---DRPADVAEAARARVERGFTAVKMngteELQYIDSPRKvdaaVARVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 191 GIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAEHKGLIS 270
Cdd:PRK14017 169 AVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 271 ANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPH-----FAMEIHLHLAAAYPREPWVEH---------FDWLDPLF 336
Cdd:PRK14017 249 AGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHcplgpIALAACLQVDAVSPNAFIQEQslgihynqgADLLDYVK 328
|
330 340
....*....|....*....|....*...
gi 517603070 337 N-ERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:PRK14017 329 NkEVFAYEDGFVAIPTGPGLGIEIDEAK 356
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
110-366 |
1.15e-36 |
|
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: 136.76 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 110 ALAAIDIALYDLKAKRAGLPLAKFL------GAYRDSVQTYnTSGGFLHAS--LAEVKARATVLLDEGIGGIKIKVGLPD 181
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVY-AAGGYYYPGddLGRLRDEMRRYLDRGYTVVKIKIGGAP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 182 TAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLAS 261
Cdd:cd03326 188 LDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 262 VAEHKGLISANGC----DIIQPDAPRVGGITQFLRLAALADERGLG---LAPHFAMEIHLHLAA--------AYPrepwv 326
Cdd:cd03326 268 LQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGWSrrrFFPHGGHLMSLHIAAglglggneSYP----- 342
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 517603070 327 ehfDWLDPL--FNERLETKNGRMLVPDRPGLGISLSEQARAW 366
Cdd:cd03326 343 ---DVFQPFggFADGCKVENGYVRLPDAPGIGFEGKAELAAE 381
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
23-365 |
2.45e-36 |
|
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: 135.26 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 23 ISDAKVFTGRqkPMTEVVFLfaEITTEQGHSGIG-FSYSKRAGGPAQYAHaREVAEGIIGEDPNDIGRLYtKLLWAGASV 101
Cdd:cd03322 2 ITAIEVIVTC--PGRNFVTL--KITTDQGVTGLGdATLNGRELAVKAYLR-EHLKPLLIGRDANRIEDIW-QYLYRGAYW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 102 GRSGVATQALAAIDIALYDLKAKRAGLPLAKFLG-AYRDSVQTYNTSGGflhASLAEVKARATVLLDEGIGGIKIKvgLP 180
Cdd:cd03322 76 RRGPVTMNAIAAVDMALWDIKGKAAGMPLYQLLGgKSRDGIMVYSHASG---RDIPELLEAVERHLAQGYRAIRVQ--LP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 181 DTAEDLRRVAGIREHIGWDVPLMVDANQqwdratALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLA 260
Cdd:cd03322 151 KLFEAVREKFGFEFHLLHDVHHRLTPNQ------AARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 261 SVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPHFA-------MEIHLHLAAAYPR---EPWVEHFD 330
Cdd:cd03322 225 SIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdlspvgMAAALHLDLWVPNfgiQEYMRHAE 304
|
330 340 350
....*....|....*....|....*....|....*
gi 517603070 331 WLDPLFNERLETKNGRMLVPDRPGLGISLSEQARA 365
Cdd:cd03322 305 ETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAA 339
|
|
| 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 ... |
9-333 |
2.67e-36 |
|
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: 134.24 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 9 HVKLSTARLPLAVPIsdaKVFTGRQkpmTEVVFLFAEITTEqGHSGIGfsyskrAGGPAQY----------AHAREVAEG 78
Cdd:cd03319 1 KISLRPERLPLKRPF---TIARGSR---TEAENVIVEIELD-GITGYG------EAAPTPRvtgetvesvlAALKSVRPA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 79 IIGEDPNdIGRLYTKLlwAGASVGRSGvatqALAAIDIALYDLKAKRAGLPLAKF-LGAYRDSVQTYNTSGgflHASLAE 157
Cdd:cd03319 68 LIGGDPR-LEKLLEAL--QELLPGNGA----ARAAVDIALWDLEAKLLGLPLYQLwGGGAPRPLETDYTIS---IDTPEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 158 VKARATVLLDEGIGGIKIKVGLPDtAEDLRRVAGIREHIGwDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAY 237
Cdd:cd03319 138 MAAAAKKAAKRGFPLLKIKLGGDL-EDDIERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 238 DFEGHADLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGLG------LAPHFAME 311
Cdd:cd03319 216 DDDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKvmvgcmVESSLSIA 295
|
330 340
....*....|....*....|..
gi 517603070 312 IHLHLAAAyprepwveHFDWLD 333
Cdd:cd03319 296 AAAHLAAA--------KADFVD 309
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
110-363 |
3.69e-34 |
|
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: 129.28 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 110 ALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVqtyntSGGflhASLAEVKARATVL------LDEGIGGIKIKVglpDTA 183
Cdd:cd03317 95 AKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSI-----PVG---VSIGIQDDVEQLLkqieryLEEGYKRIKLKI---KPG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 184 EDLRRVAGIREHIGwDVPLMVDANQQWDRATALRMgRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVA 263
Cdd:cd03317 164 WDVEPLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 264 EHKGLISANGCDIIQPDAPRVGGITQFLRLAALADER------------GLGLAphfameIHLHLAA----AYPRE-PWV 326
Cdd:cd03317 242 DARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHgipvwcggmlesGIGRA------HNVALASlpnfTYPGDiSAS 315
|
250 260 270
....*....|....*....|....*....|....*..
gi 517603070 327 EHFdWLDPLFNERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:cd03317 316 SRY-FEEDIITPPFELENGIISVPTGPGIGVTVDREA 351
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
23-365 |
2.40e-32 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 125.41 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 23 ISDAKVFT---GRQkpmtevvFLFAEITTEQGHSGIG-FSYSKRAGGPAQYAhaRE-VAEGIIGEDPNDIGRLYtKLLWA 97
Cdd:PRK15072 3 IVDAEVIVtcpGRN-------FVTLKITTDDGVTGLGdATLNGRELAVASYL--QDhVCPLLIGRDAHRIEDIW-QYLYR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 98 GASVGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLG-AYRDSVQTYNTSGGFLHASLAEVKARAtvlLDEGIGGIKIK 176
Cdd:PRK15072 73 GAYWRRGPVTMSAIAAVDMALWDIKAKAAGMPLYQLLGgASREGVMVYGHANGRDIDELLDDVARH---LELGYKAIRVQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 177 VGLP------------------------------DTAEDLRRV----AGIREHIGWDVPLMVDANQQWDRATALRMGRRL 222
Cdd:PRK15072 150 CGVPglkttygvskgkglayepatkgllpeeelwSTEKYLRFVpklfEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 223 EEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGL 302
Cdd:PRK15072 230 EPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQV 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517603070 303 GLAPHFA-------MEIHLHLAAAYPR---EPWVEHFDWLDPLFNERLETKNGRMLVPDRPGLGISLSEQARA 365
Cdd:PRK15072 310 RTGSHGPtdlspvcMAAALHFDLWVPNfgiQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAA 382
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
155-251 |
2.50e-27 |
|
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: 103.52 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 155 LAEVKARATVLLDE-GIGGIKIKVGLPDtAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEP 233
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 517603070 234 LDAYDFEGHADLARALDT 251
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
110-303 |
7.99e-24 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 100.30 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 110 ALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVQTYNTSGgflHASLAEVKARATVLLDEGIGGIKIKVGlPDTAEDLRRV 189
Cdd:TIGR01928 91 AKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSG---LANDEQMLKQIESLKATGYKRIKLKIT-PQIMHQLVKL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 190 AGIREHigwDVPLMVDANQQWDRATALRMgRRLEEFNLVWIEEPLDAYDFEGHADLARALDTPIATGEMLASVAEHKGLI 269
Cdd:TIGR01928 167 RRLRFP---QIPLVIDANESYDLQDFPRL-KELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDARNLI 242
|
170 180 190
....*....|....*....|....*....|....
gi 517603070 270 SANGCDIIQPDAPRVGGITQFLRLAALADERGLG 303
Cdd:TIGR01928 243 ELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAK 276
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
45-363 |
2.32e-23 |
|
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: 100.09 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 45 EITTEQGHSGIGFSYskraGGPAQYAHAREVAEGIIG-----EDPNDIGRLYTKLLWAGASVGRSG-----VATQALAAI 114
Cdd:cd03323 34 ELTDDNGNTGVGESP----GGAEALEALLEAARSLVGgdvfgAYLAVLESVRVAFADRDAGGRGLQtfdlrTTVHVVTAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 115 DIALYDLKAKRAGLPLAKFLGAY-RDSVQT----------YNTSGGFLHASLAE--------VKARATVLLDE-GIGGIK 174
Cdd:cd03323 110 EVALLDLLGQALGVPVADLLGGGqRDSVPFlaylfykgdrHKTDLPYPWFRDRWgealtpegVVRLARAAIDRyGFKSFK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 175 IKVGLPDTAEDLRRVAGIREHIGwDVPLMVDANQQWDRATALRMGRRLEEFnLVWIEEPldAYDFEGHADLARALDTPIA 254
Cdd:cd03323 190 LKGGVLPGEEEIEAVKALAEAFP-GARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDP--CGGREGMAEFRRATGLPLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 255 TgEMLASVAEHKG-LISANGCDIIQPDAPRVGGITQFLRLAALADERGLGLAPH--------FAMeiHLHLAAAYPREPW 325
Cdd:cd03323 266 T-NMIVTDFRQLGhAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHsnnhlgisLAM--MTHVAAAAPGLIT 342
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517603070 326 V--EHFDWLDP--LFNERLETKNGRMLVPDRPGLGISLSEQA 363
Cdd:cd03323 343 AcdTHWIWQDGqvITGEPLRIKDGKVAVPDKPGLGVELDRDK 384
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
156-324 |
4.18e-23 |
|
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: 96.95 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 156 AEVKARATVLLDEGIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLD 235
Cdd:cd03320 84 AAALGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 236 AYDFEGHadLARALDTPIATGEMLASVAEHKGLISANGCD--IIQPdaPRVGGITQFLRLAALADERGLGLAPHFAME-- 311
Cdd:cd03320 164 PDDLAEL--RRLAAGVPIALDESLRRLDDPLALAAAGALGalVLKP--ALLGGPRALLELAEEARARGIPAVVSSALEss 239
|
170
....*....|....*..
gi 517603070 312 ----IHLHLAAAYPREP 324
Cdd:cd03320 240 iglgALAHLAAALPPLP 256
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
36-135 |
2.67e-10 |
|
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: 57.48 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 36 MTEVVFLFAEITTEQGHSGIG--FSYSKRAGGPAQYAHArEVAEGIIGEDP---NDIGRL-YTKLLWAGAsvgrsgvatq 109
Cdd:pfam02746 23 VQQQSLVIVRIETSEGVVGIGeaTSYGGRAETIKAILDD-HLAPLLIGRDAaniSDLWQLmYRAALGNMS---------- 91
|
90 100
....*....|....*....|....*.
gi 517603070 110 ALAAIDIALYDLKAKRAGLPLAKFLG 135
Cdd:pfam02746 92 AKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
95-301 |
3.47e-10 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 61.80 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 95 LWAGASVGRSGVATQALAAIDIALYDLKAKRAGLPLAKFLGAYRDSVQTYNTSG-----GFL--HASLAEVKARATVLLD 167
Cdd:PLN02980 1024 IWSELGIPPSSIFPSVRCGLEMAILNAIAVRHGSSLLNILDPYQKDENGSEQSHsvqicALLdsNGSPLEVAYVARKLVE 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 168 EGIGGIKIKVGL-PDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYD----FEGH 242
Cdd:PLN02980 1104 EGFSAIKLKVGRrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDEDdlikFCEE 1183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517603070 243 ADLARALDTPIATGE-----MLASVAeHKGLISAngcdIIQPDAprVGGITQFLRLAALADERG 301
Cdd:PLN02980 1184 TGLPVALDETIDKFEecplrMLTKYT-HPGIVAV----VIKPSV--VGGFENAALIARWAQQHG 1240
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
174-324 |
3.52e-09 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 174 KIKVGLP--DTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRL-EEFNLVWIEEPLDAydFEGHADLARALD 250
Cdd:PRK02901 107 KVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT--VEELAELRRRVG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 251 TPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALAD---------ERGLGLAphfameIHLHLAAAYP 321
Cdd:PRK02901 185 VPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDIAEQIGlpvvvssalDTSVGIA------AGLALAAALP 258
|
...
gi 517603070 322 REP 324
Cdd:PRK02901 259 ELD 261
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
93-304 |
3.86e-06 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 48.20 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 93 KLLWAGAsvgrsgvatqALAAIDIALYDLKAKRAGLPLAKFLGAyrDSVQTYNTSGGFLHASLAEVKARATVLLDEGIGG 172
Cdd:PRK15129 80 KLLPAGA----------ARNAVDCALWDLAARQQQQSLAQLIGI--TLPETVTTAQTVVIGTPEQMANSASALWQAGAKL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 173 IKIKvgLPDTAEDLRRVAgIREHIGwDVPLMVDANQQWDRATALRMGRRLEEFNLVWIEEPLDAYDFEGHADLARALdtP 252
Cdd:PRK15129 148 LKVK--LDNHLISERMVA-IRSAVP-DATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPL--P 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517603070 253 IATGEMLASVAEHKGLIsanGC-DIIQPDAPRVGGITQFLRLAALADERGLGL 304
Cdd:PRK15129 222 ICADESCHTRSSLKALK---GRyEMVNIKLDKTGGLTEALALATEARAQGFAL 271
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
165-264 |
5.47e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 41.54 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 165 LLDEGIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATA---LRMGRRLEEFNLVWIEEPLDAYDFEG 241
Cdd:PRK02714 129 LWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDE 208
|
90 100
....*....|....*....|...
gi 517603070 242 HADLARALDTPIATGEMLASVAE 264
Cdd:PRK02714 209 MLQLSQDYQTPIALDESVANLAQ 231
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
167-302 |
1.76e-03 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 39.79 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517603070 167 DEGIGGIKIKVGLPDTAEDLRRVAGIREHIGWDVPLMVDANQQWDRATALRMGRRLEEFNLV---WIEEPLDAYDFEghA 243
Cdd:TIGR01927 122 AEGFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNLRGriaFLEEPLPDADEM--S 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 517603070 244 DLARALDTPIATGEMLASVAEHKGLISANGCDIIQPDAPRVGGITQFLRLAALADERGL 302
Cdd:TIGR01927 200 AFSEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGL 258
|
|
| |
