|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-360 |
1.87e-99 |
|
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: 298.66 E-value: 1.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 1 MKITRITVCQLDMPLTEPYFLSGGRlkFEKLDSTFVRIDTDEGVSGWGEGCPWGHtylpaHGPGIRAGI-ETLAPALLGL 79
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGT--RTERDVVLVRVETDDGITGWGEAVPGGT-----GAEAVAAALeEALAPLLIGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 80 DPRSPDHVNRVMDVQLPGHPYVKSAIDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAAQKGY 159
Cdd:COG4948 74 DPLDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 160 TVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPC--ETLDQCAHVASRVC 235
Cdd:COG4948 154 RALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGleWIEQPLpaEDLEGLAELRRATP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 236 NPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDFGVSVGWQMHIEDVGGSALADTAAIHLAASTPAAn 315
Cdd:COG4948 234 VPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNF- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568320502 316 RLASWLCHYHLDVDPVPGqGARNAGGAAVPPSLPGLGVAPEEGAL 360
Cdd:COG4948 313 DIVELDGPLLLADDLVED-PLRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-353 |
1.96e-52 |
|
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: 177.80 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 2 KITRITVCQLDMPLTEPYFLSGGRlkfeklDSTFVRIDTDEGVSGWGEgcpwghTYLPAHGPGIRAGIET-LAPALLGLD 80
Cdd:cd03316 1 KITDVETFVLRVPLPEPGGAVTWR------NLVLVRVTTDDGITGWGE------AYPGGRPSAVAAAIEDlLAPLLIGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 81 PRSPDHVNRVM----DVQLPGHPYVK--SAIDIACWDILGKATGMPLWQLMGGA--ETAPVLVNSSISTGSPEQMLALIA 152
Cdd:cd03316 69 PLDIERLWEKLyrrlFWRGRGGVAMAaiSAVDIALWDIKGKAAGVPVYKLLGGKvrDRVRVYASGGGYDDSPEELAEEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 153 RAAQKGYTVHSAKVGGTDTG-----LDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPC--ET 223
Cdd:cd03316 149 RAVAEGFTAVKLKVGGPDSGgedlrEDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDlfWFEEPVppDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 224 LDQCAHVASRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQI----RDFGVSVGWqmHiedVGGSAL 299
Cdd:cd03316 229 LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIaalaEAHGVRVAP--H---GAGGPI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568320502 300 ADTAAIHLAASTPAAnrlasWLCHYHLDVDPVPGQGARNA----GGAAVPPSLPGLGV 353
Cdd:cd03316 304 GLAASLHLAAALPNF-----GILEYHLDDLPLREDLFKNPpeieDGYVTVPDRPGLGV 356
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-360 |
1.03e-48 |
|
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: 168.26 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 2 KITRITVCQLDMPLTEPYFLSGGRLKFEKLdsTFVRIDTDEGVSGWGEGCPWGHtylPAHGP----GIRAGIET-LAPAL 76
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSL--VLVRLTTSDGVVGIGEATTPGG---PAWGGespeTIKAIIDRyLAPLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 77 LGLDPRSPDHVNRVMDVQLPGHPYVKSAIDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIAR-AA 155
Cdd:cd03318 76 IGRDATNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEmLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 156 QKGYTVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKAR--DWVEQPC--ETLDQCAHVA 231
Cdd:cd03318 156 AGRHRRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAgvELIEQPVprENLDGLARLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 232 SRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDFGVSVGwqmhIEDVGGSALADT----AAIHL 307
Cdd:cd03318 236 SRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAG----IALYGGTMLESSigtaASAHL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568320502 308 AASTPaanrLASWLCHY---HLDVDPVPGQGARNAGGAAVPPSLPGLGVAPEEGAL 360
Cdd:cd03318 312 FATLP----SLPFGCELfgpLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| 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 ... |
5-310 |
1.58e-48 |
|
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: 166.21 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 5 RITVCQLDMPLTEPYFLSGGRLkfEKLDSTFVRIDTDeGVSGWGEGCPWGHTYlpahG---PGIRAGIETLAPALLGLDP 81
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSR--TEAENVIVEIELD-GITGYGEAAPTPRVT----GetvESVLAALKSVRPALIGGDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 82 RSPDHVNRVMDVqLPGHPYVKSAIDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAAQKGYTV 161
Cdd:cd03319 74 RLEKLLEALQEL-LPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 162 HSAKVGGtDTGLDIDRIEAISEGLPkghKVTF--DVNRAWQPGVAVEVLNSVKAR--DWVEQPCET--LDQCAHVASRVC 235
Cdd:cd03319 153 LKIKLGG-DLEDDIERIRAIREAAP---DARLrvDANQGWTPEEAVELLRELAELgvELIEQPVPAgdDDGLAYLRDKSP 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568320502 236 NPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDF----GVSVGWQMHIEdvggSALADTAAIHLAAS 310
Cdd:cd03319 229 LPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLaraaGLKVMVGCMVE----SSLSIAAAAHLAAA 303
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-312 |
8.00e-37 |
|
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: 132.84 E-value: 8.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 6 ITVCQLDMPLTEPYFLSGGRlkFEKLDSTFVRIDTDEGVSGWGEgcpwghtylpahgpgiragietlapallgldprspd 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGT--ADTNDTVLVKLTTDSGVVGWGE------------------------------------ 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 86 hvnrvmdvqlpghpyVKSAIDIACWDILGKATGMPLWQLMGGAETAPVLVNSSIStgspeqmlaliaraaqkgytvhsak 165
Cdd:cd00308 43 ---------------VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSIE------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 166 vggtdtgldidRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPCETLDQ--CAHVASRVCNPIMLD 241
Cdd:cd00308 83 -----------RVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGlaWIEEPCAPDDLegYAALRRRTGIPIAAD 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568320502 242 ECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDFGVSVGWQMHIEDVGGSALADTAAIHLAASTP 312
Cdd:cd00308 152 ESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALP 222
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-360 |
9.54e-37 |
|
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: 136.21 E-value: 9.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 6 ITVCQLDMPLTEPYFLSGGRLkfEKLDSTFVRIDTDEGVSGWGEGC----PWghtYLPAHGPGIRAGI-ETLAPALLGLD 80
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTL--NEREFLIVELTDEEGITGYGEVVafegPF---YTEETNATAWHILkDYLLPLLLGRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 81 PRSPDHVNRVMDvQLPGHPYVKSAIDIACWDILGKATGMPLWQLMGG-AETAPVLVNSSISTgSPEQMLALIARAAQKGY 159
Cdd:cd03317 76 FSHPEEVSERLA-PIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGtRDSIPVGVSIGIQD-DVEQLLKQIERYLEEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 160 TVHSAKVggtDTGLDIDRIEAISEGLPkGHKVTFDVNRAWQpgvaVEVLNSVKARD-----WVEQPCETLD--QCAHVAS 232
Cdd:cd03317 154 KRIKLKI---KPGWDVEPLKAVRERFP-DIPLMADANSAYT----LADIPLLKRLDeygllMIEQPLAADDliDHAELQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 233 RVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDF----GVSVgWqmhiedVGG---SALADTAAI 305
Cdd:cd03317 226 LLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLcqehGIPV-W------CGGmleSGIGRAHNV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568320502 306 HLAA--------STPAANRlaswlcHYHLDV--DPVpgqgaRNAGGAAVPPSLPGLGVAPEEGAL 360
Cdd:cd03317 299 ALASlpnftypgDISASSR------YFEEDIitPPF-----ELENGIISVPTGPGIGVTVDREAL 352
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
12-316 |
2.10e-36 |
|
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: 132.85 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 12 DMPLTEPYFLSGGRLKfeKLDSTFVRIDTDEGVSGWGEgcpwghtylpahgpgiragietlAPallgldprspdhvnrvm 91
Cdd:cd03315 7 RLPLKRPLKWASGTLT--TADHVLLRLHTDDGLVGWAE-----------------------AT----------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 92 dvqlpghpyvKSAIDIACWDILGKATGMPLWQLMGGAeTAPVLVNSSISTGSPEQMLALIARAAQKGYTVHSAKVGGtDT 171
Cdd:cd03315 45 ----------KAAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGR-DP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 172 GLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKAR--DWVEQPCET--LDQCAHVASRVCNPIMLDECLHTF 247
Cdd:cd03315 113 ARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLglDYVEQPLPAddLEGRAALARATDTPIMADESAFTP 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568320502 248 GDHLNAWQRGACEGVKVKPNRVGGLTKARQI----RDFGVSVgwqmhieDVGG---SALADTAAIHLAASTPAANR 316
Cdd:cd03315 193 HDAFRELALGAADAVNIKTAKTGGLTKAQRVlavaEALGLPV-------MVGSmieSGLGTLANAHLAAALRAVTL 261
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
146-359 |
1.33e-34 |
|
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: 126.53 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 146 QMLALIARA-AQKGYTVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPC- 221
Cdd:pfam13378 1 ELAAEARRAvEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGllWIEEPVp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 222 -ETLDQCAHVASRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRD----FGVSVgwQMHiedVGG 296
Cdd:pfam13378 81 pDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAAlaeaFGVPV--APH---SGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568320502 297 SALADTAAIHLAASTPAANRLASWLCHYHLDVDPVPGqGARNAGGAAVPPSLPGLGVAPEEGA 359
Cdd:pfam13378 156 GPIGLAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTE-PLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
35-353 |
1.52e-25 |
|
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: 105.49 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 35 FVRIDTDEGVSGWGEGCPWGHTYlpahgpGIRAGIETLAPALLGLDPRSPDHVNRVMDVqlpgHPYVK---------SAI 105
Cdd:cd03325 16 FVKIETDEGVVGWGEPTVEGKAR------TVEAAVQELEDYLIGKDPMNIEHHWQVMYR----GGFYRggpvlmsaiSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 106 DIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAAQKGYTvhSAKVGGT------DTGLDID--- 176
Cdd:cd03325 86 DQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFT--AVKMNATeelqwiDTSKKVDaav 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 177 -RIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPC--ETLDQCAHVASRVCNPIMLDECLHTFGDHL 251
Cdd:cd03325 164 eRVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRllFIEEPVlpENVEALAEIAARTTIPIATGERLFSRWDFK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 252 NAWQRGACEGVKVKPNRVGGLTKARQIRDFG--VSVGWQMHIEdVGGSALAdtAAIHLAASTPaaNRLASWLC---HYHL 326
Cdd:cd03325 244 ELLEDGAVDIIQPDISHAGGITELKKIAAMAeaYDVALAPHCP-LGPIALA--ASLHVDASTP--NFLIQEQSlgiHYNE 318
|
330 340 350
....*....|....*....|....*....|.
gi 568320502 327 DVDP----VPGQGARNAGGAAVPPSLPGLGV 353
Cdd:cd03325 319 GDDLldylVDPEVFDMENGYVKLPTGPGLGI 349
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-361 |
2.39e-22 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 96.78 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 1 MKITRITVCQLDMPLTEPYFLSGGRLKfeklDSTFVRID--TDEGVsgwgEGCPWGHTYLPAHGPGIRAGIETLAPALLG 78
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVA----TAPLVLIDlaTDEGV----TGHSYLFTYTPAALKSLKQLLDDMAALLVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 79 lDPRSPDHVNRVMDVQ--LPGHP----YVKSAIDIACWDILGKATGMPLWQLMGGAeTAPVLVNSSISTGSPEQMLALIA 152
Cdd:cd03321 73 -EPLAPAELERALAKRfrLLGYTglvrMAAAGIDMAAWDALAKVHGLPLAKLLGGN-PRPVQAYDSHGLDGAKLATERAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 153 RAAQKGYTVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKAR--DWVEQPCETLDQ--CA 228
Cdd:cd03321 151 TAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEglTWIEEPTLQHDYegHA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 229 HVASRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTkarqirdfgvsvGWqmhiedVGGSALADTAAI--- 305
Cdd:cd03321 231 RIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVT------------GW------LRASALAEQAGIpms 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568320502 306 ---------HLAASTPAANrlasWLCHYHLdVDPVPGQGARNAGGAAVPPSLPGLGVAPEEGALG 361
Cdd:cd03321 293 shlfqeisaHLLAVTPTAH----WLEYVDW-AGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVR 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
6-312 |
4.62e-21 |
|
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: 91.17 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 6 ITVCQLDMPLTEPYFLSGGRL-KFEKLdstFVRIDTDEGVSGWGEGCPwghtyLPahgpgIRAGIETlapALLGLDPrsp 84
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLtRRRGL---LLRLEDLTGPVGWGEIAP-----LP-----LAFGIES---ALANLEA--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 85 dhvnrvmdvqlpghpyvksaidiacwdilgkatgmPLWQLMGGAETAPVlvNSSISTGSPEQMLALIARAaQKGYTVHSA 164
Cdd:cd03320 62 -----------------------------------LLVGFTRPRNRIPV--NALLPAGDAAALGEAKAAY-GGGYRTVKL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 165 KVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKAR--DWVEQPCETlDQCAHVASRVCN-PIMLD 241
Cdd:cd03320 104 KVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGriEYIEQPLPP-DDLAELRRLAAGvPIALD 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568320502 242 ECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDFGVSVGWQMHIEDVGGSALADTAAIHLAASTP 312
Cdd:cd03320 183 ESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALP 253
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
2-369 |
1.46e-19 |
|
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: 88.92 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 2 KITRITVCQL---DMPLT------EPYFLSggrlkfekldsTFVRIDTDEGVSGWGEgcpwghtyLPAHGPGIRAgIETL 72
Cdd:cd03323 1 KITEMRVTPVaghDSPLLnlsgahEPFFTR-----------NIVELTDDNGNTGVGE--------SPGGAEALEA-LLEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 73 APALLGLDPRSPDHvNRVMDVQLPGHP-----------------YVKSAIDIACWDILGKATGMPLWQLMGGA--ETAPV 133
Cdd:cd03323 61 ARSLVGGDVFGAYL-AVLESVRVAFADrdaggrglqtfdlrttvHVVTAFEVALLDLLGQALGVPVADLLGGGqrDSVPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 134 LV------NSSISTG-------------SPEQMLALiARAAQK--GYTVHSAKVGGTDTGLDIDRIEAISEGLPkGHKVT 192
Cdd:cd03323 140 LAylfykgDRHKTDLpypwfrdrwgealTPEGVVRL-ARAAIDryGFKSFKLKGGVLPGEEEIEAVKALAEAFP-GARLR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 193 FDVNRAWQPGVAVEVLNSVKAR-DWVEQPCETLDQCAHVASRVCNPIMLDECLHTFgDHLN-AWQRGACEGVKVKPNRVG 270
Cdd:cd03323 218 LDPNGAWSLETAIRLAKELEGVlAYLEDPCGGREGMAEFRRATGLPLATNMIVTDF-RQLGhAIQLNAVDIPLADHHFWG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 271 GLTKARQI----RDFGVsvGWQMHIEDVGGSALAdtAAIHLAASTPaaNRLASWLCHY-HLDVDPVPGQGARNAGGAAVP 345
Cdd:cd03323 297 GMRGSVRVaqvcETWGL--GWGMHSNNHLGISLA--MMTHVAAAAP--GLITACDTHWiWQDGQVITGEPLRIKDGKVAV 370
|
410 420
....*....|....*....|....
gi 568320502 346 PSLPGLGVAPEEGALGDPVAVYQR 369
Cdd:cd03323 371 PDKPGLGVELDRDKLAKAHELYQR 394
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-353 |
3.69e-19 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 87.64 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 1 MKITRITVCQLdmpltEPYFLsggrlkfekldstFVRIDTDEGVSGWGEGCPWGHtylpAHGpgIRAGIETLAPALLGLD 80
Cdd:PRK14017 1 MKITKLETFRV-----PPRWL-------------FLKIETDEGIVGWGEPVVEGR----ART--VEAAVHELADYLIGKD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 81 PRSPDHVNRVM--DVQLPGHPYVKSA---IDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAA 155
Cdd:PRK14017 57 PRRIEDHWQVMyrGGFYRGGPILMSAiagIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 156 QKGYTvhSAKVGGT------DTGLDID----RIEAISEGLPKGHKVTFD----VNRAwQPGVAVEVLNSVKARdWVEQPC 221
Cdd:PRK14017 137 ERGFT--AVKMNGTeelqyiDSPRKVDaavaRVAAVREAVGPEIGIGVDfhgrVHKP-MAKVLAKELEPYRPM-FIEEPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 222 --ETLDQCAHVASRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRD----FGVSVGwqMHIEdVG 295
Cdd:PRK14017 213 lpENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAmaeaYDVALA--PHCP-LG 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568320502 296 GSALAdtAAIHLAASTPaaNRLA---SWLCHYH-----LD--VDPVPgqgARNAGGAAVPPSLPGLGV 353
Cdd:PRK14017 290 PIALA--ACLQVDAVSP--NAFIqeqSLGIHYNqgadlLDyvKNKEV---FAYEDGFVAIPTGPGLGI 350
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-313 |
3.79e-15 |
|
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: 75.23 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 9 CQLDMPLTEPYFLSGGRLkfEKLDSTFVRIdTDEGVSGWGEGCP--WGHTylpahgpgiragiETLAPAL---LGLDPR- 82
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLL--ARREGLIVRL-TDEGRTGWGEIAPlpGFGT-------------ETLAEALdfcRALIEEi 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 83 SPDHVNRVmDVQLPghpyvksaidiACwdilGKATGMPLWQLMGGAETAPvlvNSSI-----STGSPEqmLALIARAAQK 157
Cdd:TIGR01927 65 TRGDIEAI-DDQLP-----------SV----AFGFESALIELESGDELPP---ASNYyvallPAGDPA--LLLLRSAKAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 158 GYTVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKAR-----DWVEQPCETLDQCAHVAS 232
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNlrgriAFLEEPLPDADEMSAFSE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 233 RVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDFGVSVGWQMHIEDVGGSALADTAAIHLAA-ST 311
Cdd:TIGR01927 204 ATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAkLS 283
|
..
gi 568320502 312 PA 313
Cdd:TIGR01927 284 PD 285
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
36-359 |
6.67e-15 |
|
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: 75.17 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 36 VRIDTDEGVSGWGEGCPWGHTYLPAhgPGIRagiETLAPALLGLDPrspdhvNRVMDV--QLPGHPYVK---------SA 104
Cdd:cd03322 19 LKITTDQGVTGLGDATLNGRELAVK--AYLR---EHLKPLLIGRDA------NRIEDIwqYLYRGAYWRrgpvtmnaiAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 105 IDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAAQKGYT---VHSAKVggtdtgldidrIEAI 181
Cdd:cd03322 88 VDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRairVQLPKL-----------FEAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 182 SEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPCETLDQCA--HVASRVCNPIMLDECLHTFGDHLNAWQRG 257
Cdd:cd03322 157 REKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRlfWMEDPTPAENQEAfrLIRQHTATPLAVGEVFNSIWDWQNLIQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 258 ACEGVKVKPNRVGGLTKARQIRD----FGVSVGWQMHiEDVggSALADTAAIHLAASTPaaNRLASWLCHYHLDVDPVPG 333
Cdd:cd03322 237 LIDYIRTTVSHAGGITPARKIADlaslYGVRTGWHGP-TDL--SPVGMAAALHLDLWVP--NFGIQEYMRHAEETLEVFP 311
|
330 340
....*....|....*....|....*.
gi 568320502 334 QGARNAGGAAVPPSLPGLGVAPEEGA 359
Cdd:cd03322 312 HSVRFEDGYLHPGEEPGLGVEIDEKA 337
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
35-126 |
1.15e-14 |
|
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: 69.81 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 35 FVRIDTDEGVSGWGEGCPWGHTYLpahgpGIRAGIET-LAPALLGLDPRSPDHVNRVMDVQLPGHPYVKSAIDIACWDIL 113
Cdd:pfam02746 30 IVRIETSEGVVGIGEATSYGGRAE-----TIKAILDDhLAPLLIGRDAANISDLWQLMYRAALGNMSAKAAIDMALWDLK 104
|
90
....*....|...
gi 568320502 114 GKATGMPLWQLMG 126
Cdd:pfam02746 105 AKVLNLPLADLLG 117
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-353 |
6.06e-13 |
|
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: 69.35 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 2 KITRITVCQLDMPLTEPYF-----LSGGRlkfEKLDSTFVRIDTDEGVSGwgegcpwgHTYLPAHGPGIRAGIETLAPAL 76
Cdd:cd03329 1 KITDVEVTVFEYPTQPVSFdgghhHPGPA---GTRKLALLTIETDEGAKG--------HAFGGRPVTDPALVDRFLKKVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 77 LGLDPRSPD-------HVNRVMDVQLPGhpyvksAIDIACWDILGKATGMPLWQLMGGAETApVLVNSSISTGSPEQMLA 149
Cdd:cd03329 70 IGQDPLDRErlwqdlwRLQRGLTDRGLG------LVDIALWDLAGKYLGLPVHRLLGGYREK-IPAYASTMVGDDLEGLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 150 LIARAAQ----------KGYTVHSAKVGGTDtgLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WV 217
Cdd:cd03329 143 SPEAYADfaeeckalgyRAIKLHPWGPGVVR--RDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGffWY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 218 EQPCETLDQCAHV--ASRVCNPIMLDECLHTFGDHLNAWQR-GACEGVKVKPNRVGGLTKARQIRDFGVSVGwqMHIEDV 294
Cdd:cd03329 221 EDPLREASISSYRwlAEKLDIPILGTEHSRGALESRADWVLaGATDFLRADVNLVGGITGAMKTAHLAEAFG--LDVELH 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 295 GGSAladtAAIHLAASTPAANRLASWLCH----------YHLDV-DPVPGQGARNAggaavpPSLPGLGV 353
Cdd:cd03329 299 GNGA----ANLHVIAAIRNTRYYERGLLHpsqkydvyagYLSVLdDPVDSDGFVHV------PKGPGLGV 358
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
33-353 |
7.64e-13 |
|
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: 68.90 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 33 STFVRIDTDEGVSGWGEGcpwghtylpAHGPGIRAGIET-LAPALLGLDPRSPDHVNRVMDVQlpGHPY--------VKS 103
Cdd:cd03327 11 WLFVEIETDDGTVGYANT---------TGGPVACWIVDQhLARFLIGKDPSDIEKLWDQMYRA--TLAYgrkgiamaAIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 104 AIDIACWDILGKATGMPLWQLMGGAETAPVLVNSS-ISTGSPEQMLALIARAAQKGYT------VHSAKVGgtDTGL--D 174
Cdd:cd03327 80 AVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYLKEGYRgmkmrfGYGPSDG--HAGLrkN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 175 IDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQPCETLDQCAHVASRVCNPIMLDECLHTFG--DH 250
Cdd:cd03327 158 VELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYElrWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTvyGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 251 LNAWQRGACEGVKVKPNRVGGLTKARQI----RDFGVSV---GWQMHiedvggsaladtaAIHLAAS---TPAANRLA-- 318
Cdd:cd03327 238 KRLLEGRAVDILQPDVNWVGGITELKKIaalaEAYGVPVvphASQIY-------------NYHFIMSepnSPFAEYLPns 304
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568320502 319 -----SWLCHYHLDVDPVPgqgarnAGGAAVPPSLPGLGV 353
Cdd:cd03327 305 pdevgNPLFYYIFLNEPVP------VNGYFDLSDKPGFGL 338
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
144-231 |
2.56e-12 |
|
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: 62.30 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 144 PEQMLALIARA-AQKGYTVHSAKVGGtDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--WVEQP 220
Cdd:smart00922 1 PEELAEAARRAvAEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGleWIEEP 79
|
90
....*....|.
gi 568320502 221 CETLDQCAHVA 231
Cdd:smart00922 80 VPPDDLEGLAE 90
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-159 |
1.04e-11 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 65.70 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 1 MKITRITVCqldmpLTEPyflsgGRlkfekldsTFV--RIDTDEGVSGWGEGCPWGH-----TYLPAHgpgiragietLA 73
Cdd:PRK15072 1 MKIVDAEVI-----VTCP-----GR--------NFVtlKITTDDGVTGLGDATLNGRelavaSYLQDH----------VC 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 74 PALLGLDPRspdhvnRVMDV-Q-LPGHPYVK---------SAIDIACWDILGKATGMPLWQLMGGAETAPVLVNSSISTG 142
Cdd:PRK15072 53 PLLIGRDAH------RIEDIwQyLYRGAYWRrgpvtmsaiAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGR 126
|
170
....*....|....*..
gi 568320502 143 SPEQMLALIARAAQKGY 159
Cdd:PRK15072 127 DIDELLDDVARHLELGY 143
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
133-312 |
6.41e-11 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 62.68 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 133 VLVNSSISTGSPEQMLALIARAAqkGYTVHSAKVG--GTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNS 210
Cdd:PRK02901 79 VPVNATVPAVDAAQVPEVLARFP--GCRTAKVKVAepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 211 VKAR---DWVEQPCETLDQCAHVASRVCNPIMLDECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIRDF-GVSVg 286
Cdd:PRK02901 157 LDADgplEYVEQPCATVEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDIAEQiGLPV- 235
|
170 180 190
....*....|....*....|....*....|.
gi 568320502 287 wqmhiedVGGSALaDT-----AAIHLAASTP 312
Cdd:PRK02901 236 -------VVSSAL-DTsvgiaAGLALAAALP 258
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
41-275 |
1.34e-09 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 58.61 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 41 DEGVSGWGEGCPWghtylPAHG---PGIRAGIETLAPAL------LGLDPRSPDHVNRvmdvqlpghpyvkSAIDIACWD 111
Cdd:PRK15129 36 EEGIKGTGECTPY-----PRYGesdASVMAQIMSVVPQLekgltrEALQKLLPAGAAR-------------NAVDCALWD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 112 ILGKATGMPLWQLMGGAETAPVLVNSSISTGSPEQMLALIARAAQKGYTVHSAKVggtDTGLDIDRIEAISEGLPKGhKV 191
Cdd:PRK15129 98 LAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKL---DNHLISERMVAIRSAVPDA-TL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 192 TFDVNRAWQP-------------GVAVevlnsvkardwVEQPCETLDQCAhvasrVCN-----PIMLDECLHTFGDhLNA 253
Cdd:PRK15129 174 IVDANESWRAeglaarcqlladlGVAM-----------LEQPLPAQDDAA-----LENfihplPICADESCHTRSS-LKA 236
|
250 260
....*....|....*....|..
gi 568320502 254 WqRGACEGVKVKPNRVGGLTKA 275
Cdd:PRK15129 237 L-KGRYEMVNIKLDKTGGLTEA 257
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
70-252 |
5.28e-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: 57.40 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 70 ETLAPALLGLDPRS----------PDHVNRVM--DVQLPGH---PYVKSAIDIACWDILGKATGMPLWQLMG---GAETA 131
Cdd:cd03326 63 ERFIPRLLAAAPDSllddaggnldPARAWAAMmrNEKPGGHgerAVAVGALDMAVWDAVAKIAGLPLYRLLArryGRGQA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 132 PVLVNSSISTGSP---EQMLAL---IARAAQKGYTVHSAKVGGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAV 205
Cdd:cd03326 143 DPRVPVYAAGGYYypgDDLGRLrdeMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAI 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568320502 206 EVLNSVKARD--WVEQPCETLDQC--AHVASRVCNPIMLDECLHTFGDHLN 252
Cdd:cd03326 223 AYAKALAPYGlrWYEEPGDPLDYAlqAELADHYDGPIATGENLFSLQDARN 273
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
54-354 |
2.71e-08 |
|
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: 55.11 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 54 GHTYLPAHGPGIRAGieTLAPALLGLDPRSPDHVNRVMD--VQLPGHPYVK----SAIDIACWDILGKATGMPLWQLMGG 127
Cdd:cd03328 44 GYTYADAAAAALVDG--LLAPVVEGRDALDPPAAWEAMQraVRNAGRPGVAamaiSAVDIALWDLKARLLGLPLARLLGR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 128 AETA-PVLVNSSISTGSPEQMLALIARAAQKGYTVHSAKVgGTDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVE 206
Cdd:cd03328 122 AHDSvPVYGSGGFTSYDDDRLREQLSGWVAQGIPRVKMKI-GRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 207 VLNSVKARD--WVEQPCETLDQCAHVASRVCNPIMLD----ECLHTFGDHLNAWQRGACEGVKVKPNRVGGLTKARQIrd 280
Cdd:cd03328 201 LARAFADEGvtWFEEPVSSDDLAGLRLVRERGPAGMDiaagEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQA-- 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568320502 281 fgVSVGWQMHIEDVGGSALADTAaiHLAASTPAAnRLASWLcHYHLDVDPVPGQGA-RNAGGAAVP-PSLPGLGVA 354
Cdd:cd03328 279 --AALAAAHHVDLSAHCAPALHA--HVACAVPRL-RHLEWF-HDHVRIERMLFDGApDPSGGALRPdLSRPGLGLE 348
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
36-316 |
3.39e-06 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 48.47 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 36 VRIDTDEGVSGWGEGCPWghtylpahgPGIraGIETLAPALLGLDprspdhvnrvmdvQLPGHPYVKSAIDI-----ACW 110
Cdd:PRK02714 33 LRLTDETGKIGWGEIAPL---------PWF--GSETLEEALAFCQ-------------QLPGEITPEQIFSIpdalpACQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 111 DILGKAtgmplWQLMGGAETAPVLVNSSIST--GSPEQMLALIARAAQKGYTVHSAKVGGTDTGLDIDRIEAISEGLPKG 188
Cdd:PRK02714 89 FGFESA-----LENESGSRSNVTLNPLSYSAllPAGEAALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 189 HKVTFDVNRAWQPGVA------VEVLNSVKArDWVEQPC--ETLDQCAHVASRVCNPIMLDECLHTFgDHLNAWQRGACE 260
Cdd:PRK02714 164 AKLRLDANGGLSLEEAkrwlqlCDRRLSGKI-EFIEQPLppDQFDEMLQLSQDYQTPIALDESVANL-AQLQQCYQQGWR 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568320502 261 GVKV-KPNRVGgltKARQIRDFgvsvgWQMHIEDVGGS-----ALADTAAIHLAASTPAANR 316
Cdd:PRK02714 242 GIFViKPAIAG---SPSRLRQF-----CQQHPLDAVFSsvfetAIGRKAALALAAELSRPDR 295
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
104-353 |
1.12e-05 |
|
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: 46.95 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 104 AIDIACWDILGKATGMPLWQLMggAETAPVLVNSSIS---------------------------------------TGSP 144
Cdd:cd03324 113 AVVNAVWDLWAKAEGKPLWKLL--VDMTPEELVSCIDfryitdaltpeealeilrrgqpgkaareadllaegypayTTSA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 145 -------EQMLALIARAAQKGYTVHSAKVGGtDTGLDIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD-- 215
Cdd:cd03324 191 gwlgysdEKLRRLCKEALAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKpw 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 216 WVEQPCETLDQCAHVASR---------------VCNPIMLDECLhtfgdhlnawQRGACEGVKVKPNRVGGLTKARQI-- 278
Cdd:cd03324 270 WIEEPTSPDDILGHAAIRkalaplpigvatgehCQNRVVFKQLL----------QAGAIDVVQIDSCRLGGVNENLAVll 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 279 --RDFGVSVgwqmhIEDVGGSALADtAAIHL------AASTPAANRLASWLCHYHLD-VDPVpgqgaRNAGGAAVPPSLP 349
Cdd:cd03324 340 maAKFGVPV-----CPHAGGVGLCE-LVQHLsmidyiCVSGSKEGRVIEYVDHLHEHfVYPV-----VIQNGAYMPPTDP 408
|
....
gi 568320502 350 GLGV 353
Cdd:cd03324 409 GYSI 412
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
140-278 |
2.15e-03 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 40.23 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568320502 140 STGSPEQMLALIARAAQKGYTVHSAKVGGTDTGL-DIDRIEAISEGLPKGHKVTFDVNRAWQPGVAVEVLNSVKARD--W 216
Cdd:PLN02980 1087 SNGSPLEVAYVARKLVEEGFSAIKLKVGRRVSPIqDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNlkY 1166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568320502 217 VEQPCETLDQCAHVASRVCNPIMLDECLHTFGDH----LNAWQRGACEGVKVKPNRVGGLTKARQI 278
Cdd:PLN02980 1167 IEEPVQDEDDLIKFCEETGLPVALDETIDKFEECplrmLTKYTHPGIVAVVIKPSVVGGFENAALI 1232
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
103-128 |
3.91e-03 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 38.94 E-value: 3.91e-03
10 20
....*....|....*....|....*.
gi 568320502 103 SAIDIACWDILGKATGMPLWQLMGGA 128
Cdd:PRK15440 126 SCVDLALWDLLGKVRGLPVYKLLGGA 151
|
|
| |
