|
Name |
Accession |
Description |
Interval |
E-value |
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
4-365 |
1.18e-165 |
|
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: 467.56 E-value: 1.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIGGLSYGVESPEAISSAINHYLTPLLKGQPA 83
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 84 DNLNALTQRINSAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKDIAEGETLLAEGRHQ 163
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 164 AFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIET 243
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 244 AILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLP-LQW 322
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPsLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490999979 323 GTEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKL 365
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
5-371 |
3.61e-159 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 451.17 E-value: 3.61e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 5 VERIESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIGGLSYGVESPEAISSAINHYLTPLLKGQPAD 84
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 85 NLNALTQRINSAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKDIAEGETLLAEGRHQA 164
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 165 FKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETA 244
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENREALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 245 ILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLP-LQWG 323
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPaLSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490999979 324 TEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKLQFYARK 371
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRRD 368
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
4-368 |
1.85e-114 |
|
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: 337.18 E-value: 1.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIGGlsygveSPEAISSAINHYLTPLLKGQPA 83
Cdd:COG4948 2 KITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGT------GAEAVAAALEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 84 DNLNALTQRINSAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKDIAEGETLLAEGrHQ 163
Cdd:COG4948 76 LDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARG-FR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 164 AFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIET 243
Cdd:COG4948 155 ALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 244 AILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLP-LQW 322
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPnFDI 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490999979 323 GtEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKLQFY 368
Cdd:COG4948 315 V-ELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
8-325 |
2.00e-62 |
|
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: 200.65 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 8 IESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATtigglsygvespeaissainhyltpllkgqpadnln 87
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEAT------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 88 altqrinsaikgntfaKSAIETALLDAQGKALGLPVSALLGGAlQTSLPVLWTLASGDTNKDIAEGETLLAEGrHQAFKL 167
Cdd:cd03315 45 ----------------KAAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRVAHMLGLGEPAEVAEEARRALEAG-FRTFKL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 168 KIGaRELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILA 247
Cdd:cd03315 107 KVG-RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMA 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999979 248 DEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLPL-QWGTE 325
Cdd:cd03315 186 DESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAvTLPGE 264
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
4-359 |
1.10e-56 |
|
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: 188.97 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRPHKlsmtTMGCQTLVIVRITRSDGICGIGEATTIGGlsygvesPEAISSAINHYLTPLLKGQPA 83
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGEAYPGGR-------PSAVAAAIEDLLAPLLIGRDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 84 DNLNALTQRI--NSAIKGN----TFAKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKD--IAEGET 155
Cdd:cd03316 70 LDIERLWEKLyrRLFWRGRggvaMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDSPEelAEEAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 156 LLAEGrHQAFKLKIGA-----RELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQD 230
Cdd:cd03316 150 AVAEG-FTAVKLKVGGpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 231 NAALVRLSHHIETAILADEAVATHYDGYRLAQQGfsgafALKI-----AKAGGPASVLALAHVAQAAGI-----GLYGGt 300
Cdd:cd03316 229 LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAG-----AVDIiqpdvTKVGGITEAKKIAALAEAHGVrvaphGAGGP- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 301 mlegtVGTVASLHAWSTLPLQWGTEMFGPLL-LKDDIVSVPLTFTDGSVVLPQTPGLGVE 359
Cdd:cd03316 303 -----IGLAASLHLAAALPNFGILEYHLDDLpLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
148-364 |
1.47e-56 |
|
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: 183.92 E-value: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 148 KDIAEGETLLAEGRHQAFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVS 227
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 228 AQDNAALVRLSHHIETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGtVG 307
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP-IG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490999979 308 TVASLHAWSTLP-LQWGTEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDK 364
Cdd:pfam13378 160 LAASLHLAAAVPnLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| 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 ... |
7-313 |
3.67e-54 |
|
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: 180.85 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 7 RIESWLVDVPTIRPHKLSMTTMGCQTLVIVRITrSDGICGIGEATtIGGLSYGvESPEAISSAINHyLTPLLKGQPADNL 86
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIE-LDGITGYGEAA-PTPRVTG-ETVESVLAALKS-VRPALIGGDPRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 87 NALtQRINSAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKDIAEGETLLAEGrHQAFK 166
Cdd:cd03319 77 KLL-EALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRG-FPLLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 167 LKIGaRELATDLRHTRAIVEALGDrASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAIL 246
Cdd:cd03319 155 IKLG-GDLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490999979 247 ADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLH 313
Cdd:cd03319 233 ADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAH 299
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
8-365 |
5.94e-41 |
|
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: 147.38 E-value: 5.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 8 IESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIGGLSYgveSPEAISSA---INHYLTPLLKGQPAD 84
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFY---TEETNATAwhiLKDYLLPLLLGREFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 85 NLNALTQRInSAIKGNTFAKSAIETALLDAQGKALGLPVSALLGGaLQTSLPVLWTLASGDTNKDIAEG-ETLLAEGrHQ 163
Cdd:cd03317 78 HPEEVSERL-APIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQLLKQiERYLEEG-YK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 164 AFKLKIGArelATDLRHTRAIVEALGDrASIRVDVNQAWdaTVA-AKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIE 242
Cdd:cd03317 155 RIKLKIKP---GWDVEPLKAVRERFPD-IPLMADANSAY--TLAdIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 243 TAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLhAWSTLPlqw 322
Cdd:cd03317 229 TPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNV-ALASLP--- 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490999979 323 GTEMFGPL-----LLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKL 365
Cdd:cd03317 305 NFTYPGDIsassrYFEEDIITPPFELENGIISVPTGPGIGVTVDREAL 352
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
8-325 |
8.53e-41 |
|
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: 143.62 E-value: 8.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 8 IESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEAttigglsygvespeaissainhyltpllkgqpadnln 87
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 88 altqrinsaikgntfaKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLAsgdtnkdiaegetllaegrhqafkl 167
Cdd:cd00308 44 ----------------ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSIE------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 168 kigarelatdlrHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILA 247
Cdd:cd00308 83 ------------RVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490999979 248 DEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLPLQWGTE 325
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIE 228
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
103-319 |
5.48e-31 |
|
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: 118.52 E-value: 5.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 103 AKSAIETALLDAQGKALG-------LPVSALLGGalqtslpvlwtlasgdtNKDIAEGETLLAEGRHQ-AFKLKIGAREL 174
Cdd:cd03320 48 LAFGIESALANLEALLVGftrprnrIPVNALLPA-----------------GDAAALGEAKAAYGGGYrTVKLKVGATSF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 175 ATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLShhIETAILADEAVATH 254
Cdd:cd03320 111 EEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLA--AGVPIALDESLRRL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490999979 255 YDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLP 319
Cdd:cd03320 189 DDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALP 253
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
7-128 |
1.94e-30 |
|
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: 112.56 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 7 RIESWLVDV-PTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIGGlsygveSPEAISSAINHYLTPLLKGQPADN 85
Cdd:pfam02746 1 AIEVFVVDVgWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGG------RAETIKAILDDHLAPLLIGRDAAN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490999979 86 LNALTQRINSAIKGNTFAKSAIETALLDAQGKALGLPVSALLG 128
Cdd:pfam02746 75 ISDLWQLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
34-361 |
3.75e-28 |
|
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: 112.80 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 34 VIVRITRSDGICGIGEATtigglsygVESPEAISSAINHYLTPLLKGQPADNLNALTQR------------INSAIkgnt 101
Cdd:cd03325 15 LFVKIETDEGVVGWGEPT--------VEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVmyrggfyrggpvLMSAI---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 102 fakSAIETALLDAQGKALGLPVSALLGGALQTSLPVlWTLASGDTNKDIAEgetLLAEGRHQAFK-LKIGARELATDL-- 178
Cdd:cd03325 83 ---SGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRV-YSWIGGDRPSDVAE---AARARREAGFTaVKMNATEELQWIdt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 179 --------RHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEA 250
Cdd:cd03325 156 skkvdaavERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 251 VATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLeGTVGTVASLHAWSTLPLQWGTEMFGPL 330
Cdd:cd03325 236 LFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPL-GPIALAASLHVDASTPNFLIQEQSLGI 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 490999979 331 -------LLKDDIVSVPLTFTDGSVVLPQTPGLGVELD 361
Cdd:cd03325 315 hynegddLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
4-368 |
1.83e-26 |
|
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: 108.34 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRPHKLSMTTMGCQTLVIVRITRSDGICGIGEATTIgglsygveSPEAISS--AINHYLTPLLKGQ 81
Cdd:cd03321 2 LITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYLFTY--------TPAALKSlkQLLDDMAALLVGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 82 ---PADNLNALTQRINSAikGNT----FAKSAIETALLDAQGKALGLPVSALLGGALQtSLPVLWTLASGDTNKDIAEGE 154
Cdd:cd03321 74 plaPAELERALAKRFRLL--GYTglvrMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 155 TLLAEGRHqAFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAAL 234
Cdd:cd03321 151 TAAEEGFH-AVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 235 VRLSHHIETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEgtvgtvASLHA 314
Cdd:cd03321 230 ARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQE------ISAHL 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490999979 315 WSTLPLQWGTEMfgpLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKLQFY 368
Cdd:cd03321 304 LAVTPTAHWLEY---VDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
151-243 |
7.77e-23 |
|
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: 91.57 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 151 AEGETLLAEGRHQAFKLKIGARELAtDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQD 230
Cdd:smart00922 6 EAARRAVAEAGFRAVKVKVGGGPLE-DLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDD 84
|
90
....*....|...
gi 490999979 231 NAALVRLSHHIET 243
Cdd:smart00922 85 LEGLAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
32-370 |
1.84e-22 |
|
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: 97.39 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 32 TLVIVRITRSDGICGIGEattigglSYGveSPEAISsAINHYLTPLLKGQPADN-LNALTQRINSAIKGN-------TF- 102
Cdd:cd03323 29 TRNIVELTDDNGNTGVGE-------SPG--GAEALE-ALLEAARSLVGGDVFGAyLAVLESVRVAFADRDaggrglqTFd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 103 ------AKSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTL-ASGDTNKD--------IAEGETLLAEG------- 160
Cdd:cd03323 99 lrttvhVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPFLAYLfYKGDRHKTdlpypwfrDRWGEALTPEGvvrlara 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 161 ---RH--QAFKLKIGARELATDLRHTRAIVEALgDRASIRVDVNQAWDATVAAKGCRELAAMgIDLIEQPVSAQDNAALV 235
Cdd:cd03323 179 aidRYgfKSFKLKGGVLPGEEEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDPCGGREGMAEF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 236 RLShhieTAI-LADEAVATHYD--GYRLAQQgfsgafALKIAKA-----GGPASVLALAHVAQAAGIGLYGGTMLEGTVG 307
Cdd:cd03323 257 RRA----TGLpLATNMIVTDFRqlGHAIQLN------AVDIPLAdhhfwGGMRGSVRVAQVCETWGLGWGMHSNNHLGIS 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999979 308 TVASLHAWSTLP-LQWGTEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDEDKLQFYAR 370
Cdd:cd03323 327 LAMMTHVAAAAPgLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHE 390
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
32-363 |
1.05e-21 |
|
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: 94.81 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 32 TLVIVRITRSDGICGIGEATTIGglsygveSPEAISSAINHYLTPLLKGQPADNLNALTQR------------INSAIkg 99
Cdd:cd03322 15 NFVTLKITTDQGVTGLGDATLNG-------RELAVKAYLREHLKPLLIGRDANRIEDIWQYlyrgaywrrgpvTMNAI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 100 ntfakSAIETALLDAQGKALGLPVSALLGGALQTSLPVlWTLASGDtnkDIAegETLLAEGRHQAfklkIGAREL-ATDL 178
Cdd:cd03322 86 -----AAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMV-YSHASGR---DIP--ELLEAVERHLA----QGYRAIrVQLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 179 RHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEAVATHYDGY 258
Cdd:cd03322 151 KLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 259 RLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGI--GLYGGTMLEgTVGTVASLHAWSTLPlQWGTEMFGPLLLK-DD 335
Cdd:cd03322 231 NLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrtGWHGPTDLS-PVGMAAALHLDLWVP-NFGIQEYMRHAEEtLE 308
|
330 340
....*....|....*....|....*...
gi 490999979 336 IVSVPLTFTDGSVVLPQTPGLGVELDED 363
Cdd:cd03322 309 VFPHSVRFEDGYLHPGEEPGLGVEIDEK 336
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
4-363 |
7.68e-19 |
|
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: 86.68 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRP-----HKLSMTTmGCQTLVIVRITRSDGICGIgeatTIGGlsygveSPEAISSAINHYLTPLL 78
Cdd:cd03329 1 KITDVEVTVFEYPTQPVsfdggHHHPGPA-GTRKLALLTIETDEGAKGH----AFGG------RPVTDPALVDRFLKKVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 79 KGQPADNLNALTQRINSAIKGNTF-AKSAIETALLDAQGKALGLPVSALLGGaLQTSLPVLWTLASGDTNKDIA------ 151
Cdd:cd03329 70 IGQDPLDRERLWQDLWRLQRGLTDrGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLEGLEspeaya 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 152 -EGETLLAEGrHQAFKLKI-GARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQ 229
Cdd:cd03329 149 dFAEECKALG-YRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 230 DNAALVRLSHHIETAILADEAVATHYDGYR-LAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIG--LYGgtmlegtv 306
Cdd:cd03329 228 SISSYRWLAEKLDIPILGTEHSRGALESRAdWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDveLHG-------- 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490999979 307 GTVASLHAWSTL------------PLQWGTEMFGPLLLKDDIVSvpltfTDGSVVLPQTPGLGVELDED 363
Cdd:cd03329 300 NGAANLHVIAAIrntryyergllhPSQKYDVYAGYLSVLDDPVD-----SDGFVHVPKGPGLGVEIDFD 363
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
34-361 |
1.06e-18 |
|
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: 85.85 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 34 VIVRITRSDGICGIGEATtigglsygveSPEAISSAINHYLTPLLKGQPADNLNALTQ---RINSAI--KGNTF-AKSAI 107
Cdd:cd03327 12 LFVEIETDDGTVGYANTT----------GGPVACWIVDQHLARFLIGKDPSDIEKLWDqmyRATLAYgrKGIAMaAISAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 108 ETALLDAQGKALGLPVSALLGGALQTSLPVLWT-LASGDTNKDIAEGETLLAEGrHQAFKLKI------GARELATDLRH 180
Cdd:cd03327 82 DLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYLKEG-YRGMKMRFgygpsdGHAGLRKNVEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 181 TRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEAVATHYDGYRL 260
Cdd:cd03327 161 VRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 261 AQQGfsgafALKIAK-----AGGPASVLALAHVAQAagiglYGGTMLEGTvGTVASLHA------------WSTLPLQWG 323
Cdd:cd03327 241 LEGR-----AVDILQpdvnwVGGITELKKIAALAEA-----YGVPVVPHA-SQIYNYHFimsepnspfaeyLPNSPDEVG 309
|
330 340 350
....*....|....*....|....*....|....*...
gi 490999979 324 TEMFGPLLLkDDIVSVpltftDGSVVLPQTPGLGVELD 361
Cdd:cd03327 310 NPLFYYIFL-NEPVPV-----NGYFDLSDKPGFGLELN 341
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
36-365 |
2.27e-18 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 85.33 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 36 VRITRSDGICGIGEATtIGGLSYGVEspeaissAINHYLTPLLKGQPADNLNALTQRIN------------SAIKGntfa 103
Cdd:PRK14017 18 LKIETDEGIVGWGEPV-VEGRARTVE-------AAVHELADYLIGKDPRRIEDHWQVMYrggfyrggpilmSAIAG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 104 ksaIETALLDAQGKALGLPVSALLGGALQTSLPVL-WtlASGDTNKDIAEGETLLAEGRHQAFKLKiGAREL-------A 175
Cdd:PRK14017 86 ---IDQALWDIKGKALGVPVHELLGGLVRDRIRVYsW--IGGDRPADVAEAARARVERGFTAVKMN-GTEELqyidsprK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 176 TD--LRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEAVAT 253
Cdd:PRK14017 160 VDaaVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 254 HYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLeGTVGTVASLHAWSTLP---LQ--------- 321
Cdd:PRK14017 240 RWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPL-GPIALAACLQVDAVSPnafIQeqslgihyn 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 490999979 322 WGTEMFGPLLLKDDivsvpLTFTDGSVVLPQTPGLGVELDEDKL 365
Cdd:PRK14017 319 QGADLLDYVKNKEV-----FAYEDGFVAIPTGPGLGIEIDEAKV 357
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
4-298 |
2.98e-18 |
|
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: 84.77 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 4 TVERIESWLVDVPTIRPHKLSMTTMGCQTLVIVRItRSDGICGIGeattiggLSYGvesPEAISSAINHYLTPLLKGQPA 83
Cdd:cd03328 1 AVERVEARAYTVPTDAPEADGTLAWDATTLVLVEV-RAGGRTGLG-------YTYA---DAAAAALVDGLLAPVVEGRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 84 DNLNALTQRINSAIKGN------TFAKSAIETALLDAQGKALGLPVSALLGGAlQTSLPVLWTlaSGDTNKDIAEGETLL 157
Cdd:cd03328 70 LDPPAAWEAMQRAVRNAgrpgvaAMAISAVDIALWDLKARLLGLPLARLLGRA-HDSVPVYGS--GGFTSYDDDRLREQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 158 AEGRHQAF---KLKIGaRELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNA-- 232
Cdd:cd03328 147 SGWVAQGIprvKMKIG-RDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAgl 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999979 233 ALVRLSHHIETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYG 298
Cdd:cd03328 226 RLVRERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSA 291
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
34-350 |
3.84e-17 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 81.33 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 34 VIVRITRSDGICGIGEATTIggLSYGvESPEAISSAINHYLTPLLKGQPADnlnALTQRINSAIkgntfAKSAIETALLD 113
Cdd:PRK15129 29 VVVVELEEEGIKGTGECTPY--PRYG-ESDASVMAQIMSVVPQLEKGLTRE---ALQKLLPAGA-----ARNAVDCALWD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 114 AQGKALGLPVSALLGgalqTSLPVLWTLA---SGDTNKDIAEGETLLAEGRHQAFKLKIGARELATDLRHTRAIVEalgd 190
Cdd:PRK15129 98 LAARQQQQSLAQLIG----ITLPETVTTAqtvVIGTPEQMANSASALWQAGAKLLKVKLDNHLISERMVAIRSAVP---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 191 RASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIetAILADEAVATHYDGYRLaqQGFSGAFA 270
Cdd:PRK15129 170 DATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIHPL--PICADESCHTRSSLKAL--KGRYEMVN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 271 LKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTVGTVASLhawSTLPLQWGTEMFGPLLLKDDiVSVPLTFTDGSVVL 350
Cdd:PRK15129 246 IKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAAL---PLVPQVRFADLDGPTWLAVD-VEPALQFTTGELHL 321
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
163-319 |
1.95e-16 |
|
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: 79.08 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 163 QAFKLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDATVA---AKGCRELAAMGIDLIEQPVsaQDNAALVRLSH 239
Cdd:TIGR01927 126 RTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAqqfLKALDPNLRGRIAFLEEPL--PDADEMSAFSE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 240 HIETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIGLYGGTMLEGTV--GTVASLHAWST 317
Cdd:TIGR01927 204 ATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIalGQLARLAAKLS 283
|
..
gi 490999979 318 LP 319
Cdd:TIGR01927 284 PD 285
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
106-313 |
1.60e-15 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 76.59 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 106 AIETALLDAQGKAL-----GLPVSALLGgalqTSLPVLWTLasgdtnkdiaegETLLAEGrHQAFKLKIGARELATDLRH 180
Cdd:PRK02714 90 GFESALENESGSRSnvtlnPLSYSALLP----AGEAALQQW------------QTLWQQG-YRTFKWKIGVDPLEQELKI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 181 TRAIVEALGDRASIRVDVNQAWDATVAA---KGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEAVATHYDG 257
Cdd:PRK02714 153 FEQLLERLPAGAKLRLDANGGLSLEEAKrwlQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANLAQL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490999979 258 YRLAQQGFSGAFALKIAKAGGPasvLALAHVAQAAGIGLYGGTMLEGTVGTVASLH 313
Cdd:PRK02714 233 QQCYQQGWRGIFVIKPAIAGSP---SRLRQFCQQHPLDAVFSSVFETAIGRKAALA 285
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
165-369 |
1.36e-14 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 165 FKLKIGARE--LATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCREL-AAMGIDLIEQPVSAQDNAALVRLShhI 241
Cdd:PRK02901 106 AKVKVAEPGqtLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCATVEELAELRRR--V 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 242 ETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLAlahVAQAAGIGLYGGTMLEGTVGTVASLHAWSTLP-L 320
Cdd:PRK02901 184 GVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALD---IAEQIGLPVVVSSALDTSVGIAAGLALAAALPeL 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490999979 321 QW----GTemfGPLLLKDdiVSVPLTFTDGSVVLPQtpglgVELDEDKLQFYA 369
Cdd:PRK02901 261 DHacglAT---GGLFEED--VADPLLPVDGFLPVRR-----VTPDPARLAALA 303
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
34-363 |
5.28e-11 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 63.39 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 34 VIVRITRSDGICGIGEATTIGglsygveSPEAISSAINHYLTPLLKGQPADNLNALTQRIN------------SAIkgnt 101
Cdd:PRK15072 18 VTLKITTDDGVTGLGDATLNG-------RELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYrgaywrrgpvtmSAI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 102 fakSAIETALLDAQGKALGLPVSALLGGALQTSLPVlWTLASGdtnKDIAegETLLAEGRHQAF---------------- 165
Cdd:PRK15072 87 ---AAVDMALWDIKAKAAGMPLYQLLGGASREGVMV-YGHANG---RDID--ELLDDVARHLELgykairvqcgvpglkt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 166 -----KLKIGARELATD--------------LRHT----RAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLI 222
Cdd:PRK15072 158 tygvsKGKGLAYEPATKgllpeeelwstekyLRFVpklfEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 223 EQPVSAQDNAALVRLSHHIETAILADEAVATHYDGYRLAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGI--GLYGGT 300
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVrtGSHGPT 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490999979 301 MLEgTVGTVASLHAWSTLP---LQwgtEMFGPLLLKDDIVSVPLTFTDGSVVLPQTPGLGVELDED 363
Cdd:PRK15072 318 DLS-PVCMAAALHFDLWVPnfgIQ---EYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEK 379
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
103-363 |
3.50e-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: 57.79 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 103 AKSAIETALLDAQGKALGLPVSALLGG--ALQTSLPVLWTLASG-------DTNKDIAEGETLLAEGrHQAFKLKIGARE 173
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLARryGRGQADPRVPVYAAGgyyypgdDLGRLRDEMRRYLDRG-YTVVKIKIGGAP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 174 LATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAILADEAVAT 253
Cdd:cd03326 188 LDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 254 HYDGYRLAQQGFSGA----FALKIAKAGGPASVLALAHVAQAAGIGL-----YGGTMLegtvgtvaSLHAWSTLPLQWGT 324
Cdd:cd03326 268 LQDARNLLRYGGMRPdrdvLQFDPGLSYGLPEYLRMLDVLEAHGWSRrrffpHGGHLM--------SLHIAAGLGLGGNE 339
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490999979 325 ---EMFGPLLLKDDIVSVpltfTDGSVVLPQTPGLGVELDED 363
Cdd:cd03326 340 sypDVFQPFGGFADGCKV----ENGYVRLPDAPGIGFEGKAE 377
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
157-230 |
7.99e-07 |
|
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: 50.42 E-value: 7.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490999979 157 LAEGrHQAFKLKIGArELATDLRHTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQD 230
Cdd:cd03324 208 LAQG-FTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDD 279
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
32-363 |
1.91e-06 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 49.34 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 32 TLViVRITRSDGicGIGEATTIGG--LSYGVEspeaissaiNHyLTPLLKGQ-PADNLNALTQRINSAI----KG---NT 101
Cdd:PRK15440 58 TLV-VEVEAENG--QVGFAVSTAGemGAFIVE---------KH-LNRFIEGKcVSDIELIWDQMLNATLyygrKGlvmNT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 102 FakSAIETALLDAQGKALGLPVSALLGGALQTSLPVLWTLASGDTNKDIA--EGETLLAEGRHQafklkiGARELATDLR 179
Cdd:PRK15440 125 I--SCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFYATGARPDLAKEMGfiGGKMPLHHGPAD------GDAGLRKNAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 180 HTRAIVEALGDRASIRVDVNQAWDATVAAKGCRELAAMGIDLIEQPVSAQDNAALVRLSHHIETAIL--ADEAVATHYdG 257
Cdd:PRK15440 197 MVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMvtSGEHEATLQ-G 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490999979 258 YR-LAQQGFSGAFALKIAKAGGPASVLALAHVAQAAGIglyggtMLEGTVGTVASLHAWSTLPLQWGTE----------- 325
Cdd:PRK15440 276 FRtLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQ------LVVPHGSSVYSHHFVITRTNSPFSEflmmspdadtv 349
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490999979 326 --MFGPLLLkDDIVSVpltftDGSVVLPQ--TPGLGVELDED 363
Cdd:PRK15440 350 vpQFDPILL-DEPVPV-----NGRIHKSVldKPGFGVELNRD 385
|
|
| |
