|
Name |
Accession |
Description |
Interval |
E-value |
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-365 |
0e+00 |
|
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: 526.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 2 KIDAIEAVIVDVPTKRPIQMSITTVHQQSYVIVRVY-SEGLVGVGEGGSVGGPVWSAECAETIKIIVERYLAPHLLGTDA 80
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTtSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 81 FNVSGALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLASGDTKRDLDSAVEMIERRRHN 160
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 161 RFKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRV 240
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 241 AIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPF 320
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
2CHR_A 321 GCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQ 365
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
3-368 |
1.91e-126 |
|
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: 367.97 E-value: 1.91e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 3 IDAIEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVGEGGSVGG-PVWSAECAETIKIIVERYLAPHLLGTDAF 81
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGgLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 82 NVSGALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLASGDTKRDLDSAVEMIERRRHNR 161
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 162 FKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVA 241
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENREALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 242 IMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPFG 321
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
2CHR_A 322 CELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQYAR 368
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRR 367
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-366 |
2.71e-103 |
|
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: 308.67 E-value: 2.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 1 MKIDAIEAVIVDVPTKRPIQMSITTVHQQSYVIVRV--------YSEGLVGVGEggsvggpvwsaecAETIKIIVERYLA 72
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVetddgitgWGEAVPGGTG-------------AEAVAAALEEALA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 73 PHLLGTDAFNVSGALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLASGDTKRDLDSAVE 152
Cdd:COG4948 68 PLLIGRDPLDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 153 MIERRrHNRFKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALR 232
Cdd:COG4948 148 AVARG-FRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 233 RLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLY 312
Cdd:COG4948 227 ELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
2CHR_A 313 STVPSLPFgCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQY 366
Cdd:COG4948 307 AALPNFDI-VELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
145-362 |
3.12e-53 |
|
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: 175.45 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 145 RDLDSAVEMIERRRHNRFKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVG 224
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 225 RENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLdSTIG 304
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG-GPIG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
2CHR_A 305 TSVALQLYSTVPSLPFGCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDK 362
Cdd:pfam13378 160 LAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-357 |
7.45e-53 |
|
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: 178.57 E-value: 7.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 2 KIDAIEAVIVDVPTKRPIQmsitTVHQQSYVIVRV--------YSEGlvgvgeggsvggpvWSAECAETIKIIVERYLAP 73
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG----AVTWRNLVLVRVttddgitgWGEA--------------YPGGRPSAVAAAIEDLLAP 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 74 HLLGTDAFNVSGALQTMARAVTGN------ASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTlaSGDTKRDL 147
Cdd:cd03316 63 LLIGRDPLDIERLWEKLYRRLFWRgrggvaMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYAS--GGGYDDSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 148 DSAVEMIERRR---HNRFKVKLGFRS-----PQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELI 219
Cdd:cd03316 141 EELAEEAKRAVaegFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 220 EQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI--ASYGGT 297
Cdd:cd03316 221 EEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVrvAPHGAG 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
2CHR_A 298 mldSTIGTSVALQLYSTVPSLPFgCELIGPFV-LADTLSHEPLEIRDYELQVPTGVGHGMT 357
Cdd:cd03316 301 ---GPIGLAASLHLAAALPNFGI-LEYHLDDLpLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| 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 ... |
5-311 |
1.01e-52 |
|
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: 177.38 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 5 AIEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVgeggsvggpvwsAECA-------ETIKIIVE--RYLAPHL 75
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELDGITGY------------GEAAptprvtgETVESVLAalKSVRPAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 76 LGTDAFNVSgALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLASGDTKRDLDSAVEMIE 155
Cdd:cd03319 69 IGGDPRLEK-LLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 156 RRrHNRFKVKLGfRSPQDDLIHMEALSNSLGsKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLS 235
Cdd:cd03319 148 RG-FPLLKIKLG-GDLEDDIERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2CHR_A 236 DNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQL 311
Cdd:cd03319 225 DKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHL 300
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
6-324 |
6.05e-51 |
|
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: 170.99 E-value: 6.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 6 IEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGlvgvgeggsvggpvwsaecaetikiiverylaphllgtdafnvsg 85
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDD--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 86 alqtmarAVTGNASA-KAAVEMALLDLKARALGVSIaELLGGPLRSAIPIAWTLASGDTKRDLDsAVEMIERRRHNRFKV 164
Cdd:cd03315 36 -------GLVGWAEAtKAAVDMALWDLWGKRLGVPV-YLLLGGYRDRVRVAHMLGLGEPAEVAE-EARRALEAGFRTFKL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 165 KLGfRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMA 244
Cdd:cd03315 107 KVG-RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 245 DESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPFGCEL 324
Cdd:cd03315 186 DESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGEL 265
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
94-316 |
2.83e-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: 133.99 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 94 VTGNASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLAsgdtkrdldsavemierrrhnrfkvklgfrspqd 173
Cdd:cd00308 37 VVGWGEVISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSIE---------------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 174 dliHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLSTLAS 253
Cdd:cd00308 83 ---RVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
2CHR_A 254 AFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVP 316
Cdd:cd00308 160 ALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALP 222
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-364 |
1.19e-34 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 130.43 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 6 IEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVGEGGSVGGPVW-SAECAETIKIIVERYLAPHLLGTDaFNVS 84
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFyTEETNATAWHILKDYLLPLLLGRE-FSHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 85 GALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGpLRSAIPIAWTLASGDTKRDLDSAVEMIERRRHNRFKV 164
Cdd:cd03317 80 EEVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDDVEQLLKQIERYLEEGYKRIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 165 KLgfrSPQDDLIHMEALSNSLGsKAYLRVDVNQAWDEQVASVyIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMA 244
Cdd:cd03317 159 KI---KPGWDVEPLKAVRERFP-DIPLMADANSAYTLADIPL-LKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 245 DESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLystvPSLPfgcel 324
Cdd:cd03317 234 DESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVAL----ASLP----- 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
2CHR_A 325 igPFVLADTLS-----------HEPLEIRDYELQVPTGVGHGMTLDEDKVR 364
Cdd:cd03317 305 --NFTYPGDISassryfeediiTPPFELENGIISVPTGPGIGVTVDREALK 353
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-125 |
2.33e-34 |
|
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: 122.97 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 5 AIEAVIVDVPTK-RPIQMSITTVHQQSYVIVRVYSEGLVGVGEGGSVGgpvwsAECAETIKIIVERYLAPHLLGTDAFNV 83
Cdd:pfam02746 1 AIEVFVVDVGWPlRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSY-----GGRAETIKAILDDHLAPLLIGRDAANI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
2CHR_A 84 SGALQTMARAVTGNASAKAAVEMALLDLKARALGVSIAELLG 125
Cdd:pfam02746 76 SDLWQLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
99-324 |
6.34e-29 |
|
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: 112.74 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 99 SAKAAVEMALLDLKARALGvsiaellGGPLRSAIPIAWTLASGDTkrdLDSAVEMIERRRHNR-FKVKLGFRSPQDDLIH 177
Cdd:cd03320 47 PLAFGIESALANLEALLVG-------FTRPRNRIPVNALLPAGDA---AALGEAKAAYGGGYRtVKLKVGATSFEEDLAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 178 MEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNnrVAIMADESLSTLASAFDL 257
Cdd:cd03320 117 LRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAG--VPIALDESLRRLDDPLAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2CHR_A 258 ARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPFGCEL 324
Cdd:cd03320 195 AAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAACGL 261
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
60-359 |
2.12e-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: 113.57 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 60 AETIKIIVERyLAPHLLGTDAFNVSGALQTMAR-------AVTGnaSAKAAVEMALLDLKARALGVSIAELLGGPLRSAI 132
Cdd:cd03325 37 ARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRggfyrggPVLM--SAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 133 PiAWTLASGDtkrDLDSAVEMIERRRHNRFK-VKLG----------FRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDE 201
Cdd:cd03325 114 R-VYSWIGGD---RPSDVAEAARARREAGFTaVKMNateelqwidtSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 202 QVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQK 281
Cdd:cd03325 190 PMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 282 IAAVAEASGIASYGGTMLdSTIGTSVALQLYSTVPSLpFGCE---LIGPFVLADTLSH----EPLEIRDYELQVPTGVGH 354
Cdd:cd03325 270 IAAMAEAYDVALAPHCPL-GPIALAASLHVDASTPNF-LIQEqslGIHYNEGDDLLDYlvdpEVFDMENGYVKLPTGPGL 347
|
....*
2CHR_A 355 GMTLD 359
Cdd:cd03325 348 GIEID 352
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
11-313 |
3.10e-24 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 101.46 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 11 VDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVGEGGSVGGPVW-SAECAETIKIIVERYLAPHLLGTdaFNVSGALQT 89
Cdd:TIGR01928 3 VSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWyTHETIATVKHIIEDFFEPNINKE--FEHPSEALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 90 MARAVTGNASAKAAVEMALLDLKARALGVSIAELLGGpLRSAIPIAWTLA---SGDTKRDLDSAVEMierrRHNRFKVKL 166
Cdd:TIGR01928 81 LVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGK-LRDKAPAGAVSGlanDEQMLKQIESLKAT----GYKRIKLKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 167 gfrSPQDDLIHMEALSnslgsKAY----LRVDVNQAWDEQVASVyIPELEALGVELIEQPVGRENTQALRRLSDNNRVAI 242
Cdd:TIGR01928 156 ---TPQIMHQLVKLRR-----LRFpqipLVIDANESYDLQDFPR-LKELDRYQLLYIEEPFKIDDISMLDELAKGTITPI 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2CHR_A 243 MADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLYS 313
Cdd:TIGR01928 227 CLDESITSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALAS 297
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
63-366 |
5.10e-23 |
|
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: 98.67 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 63 IKIIVERYLAPHLLGTDAFNVSGALQTMARA-------VTGNASAkaAVEMALLDLKARALGVSIAELLGGPLRSAIpIA 135
Cdd:cd03322 42 VKAYLREHLKPLLIGRDANRIEDIWQYLYRGaywrrgpVTMNAIA--AVDMALWDIKGKAAGMPLYQLLGGKSRDGI-MV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 136 WTLASGdtkRDLDSAVEMIERRrhnrfkVKLGFRSPQDDLIHM-EALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEAL 214
Cdd:cd03322 119 YSHASG---RDIPELLEAVERH------LAQGYRAIRVQLPKLfEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 215 GVELIEQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI--A 292
Cdd:cd03322 190 RLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrtG 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2CHR_A 293 SYGGTMLdSTIGTSVALQLYSTVPSlpFGCELIGPFV--LADTLSHEPlEIRDYELQVPTGVGHGMTLDEDKVRQY 366
Cdd:cd03322 270 WHGPTDL-SPVGMAAALHLDLWVPN--FGIQEYMRHAeeTLEVFPHSV-RFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
66-291 |
1.21e-22 |
|
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: 97.48 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 66 IVERYLAPHLLGTDAFNVSGALQTMARAVTGN------ASAKAAVEMALLDLKARALGVSIAELLGGpLRSAIPIAWTla 139
Cdd:cd03328 55 LVDGLLAPVVEGRDALDPPAAWEAMQRAVRNAgrpgvaAMAISAVDIALWDLKARLLGLPLARLLGR-AHDSVPVYGS-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 140 SGDTKRDLDSAVEMIERRRHNRF---KVKLGfRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGV 216
Cdd:cd03328 132 GGFTSYDDDRLREQLSGWVAQGIprvKMKIG-RDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGV 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2CHR_A 217 ELIEQPVGRENTQALRRLSDNN--RVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI 291
Cdd:cd03328 211 TWFEEPVSSDDLAGLRLVRERGpaGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHV 287
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
60-369 |
6.88e-22 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 95.73 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 60 AETIKIIVERyLAPHLLGTDAFNVSGALQTMARAvtG-------NASAKAAVEMALLDLKARALGVSIAELLGGPLRSAI 132
Cdd:PRK14017 38 ARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRG--GfyrggpiLMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 133 PI-AWtlASGDTKRDLdsaVEMIERRRHNRFK-VKLG----------FRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWD 200
Cdd:PRK14017 115 RVySW--IGGDRPADV---AEAARARVERGFTaVKMNgteelqyidsPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 201 EQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLStlaSAFDLAR---DRSVDVFSLKLCNMGGVS 277
Cdd:PRK14017 190 KPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLF---SRWDFKRvleAGGVDIIQPDLSHAGGIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 278 ATQKIAAVAEASGIA-----SYGGTMLDSTigtsvaLQLYSTVP-------SL----PFGCELIGpfVLADTlshEPLEI 341
Cdd:PRK14017 267 ECRKIAAMAEAYDVAlaphcPLGPIALAAC------LQVDAVSPnafiqeqSLgihyNQGADLLD--YVKNK---EVFAY 335
|
330 340
....*....|....*....|....*...
2CHR_A 342 RDYELQVPTGVGHGMTLDEDKVRQYARV 369
Cdd:PRK14017 336 EDGFVAIPTGPGLGIEIDEAKVRERAKT 363
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
85-369 |
4.88e-21 |
|
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: 93.54 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 85 GALQTMARAVTgnASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTL--ASGDTKRDLDS------------- 149
Cdd:cd03323 92 RGLQTFDLRTT--VHVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPFLAYLfyKGDRHKTDLPYpwfrdrwgealtp 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 150 ------AVEMIERRRHNRFKVKLGFRSPQDDLIHMEALSNSLgSKAYLRVDVNQAWDEQVASVYIPELEALgVELIEQPV 223
Cdd:cd03323 170 egvvrlARAAIDRYGFKSFKLKGGVLPGEEEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDPC 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 224 -GRENTQALRRLSD----NNRVAIMADEslstLASAFdlaRDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI--ASYGG 296
Cdd:cd03323 248 gGREGMAEFRRATGlplaTNMIVTDFRQ----LGHAI---QLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLgwGMHSN 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2CHR_A 297 TMLDstIGTSVALQLYSTVPSLPFGCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQYARV 369
Cdd:cd03323 321 NHLG--ISLAMMTHVAAAAPGLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHEL 391
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-366 |
5.35e-18 |
|
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: 84.07 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 1 MKIDAIEAVIVDVPTKRPIQMSITTVHQQSYVIVRVYSEGLVGVGEG----GSVGGPVWSAECAETIKIIVERYLAPHLL 76
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYlftyTPAALKSLKQLLDDMAALLVGEPLAPAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 77 G---TDAFNVSGA--LQTMAravtgnasaKAAVEMALLDLKARALGVSIAELLGG---PLRSAIPIAWTLASGDTKRdld 148
Cdd:cd03321 81 EralAKRFRLLGYtgLVRMA---------AAGIDMAAWDALAKVHGLPLAKLLGGnprPVQAYDSHGLDGAKLATER--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 149 sAVEMIERRRHNrFKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENT 228
Cdd:cd03321 149 -AVTAAEEGFHA-VKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 229 QALRRLSDNNRVAIMADESlstLASAFDLAR---DRSVDVFSLKLCNMGGVSATQKIAAVAEASGIAsyggtmLDSTIGT 305
Cdd:cd03321 227 EGHARIASALRTPVQMGEN---WLGPEEMFKalsAGACDLVMPDLMKIGGVTGWLRASALAEQAGIP------MSSHLFQ 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
2CHR_A 306 SVALQLYSTVPSlpfgCELIGPFVLADTLSHEPLEIRDYELQVPTGVGHGMTLDEDKVRQY 366
Cdd:cd03321 298 EISAHLLAVTPT----AHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
60-291 |
6.29e-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: 83.92 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 60 AETIKIIVERYLAPHLLGTDAFNVSGALQTMARAVTGNA------SAKAAVEMALLDLKARALGVSIAELLGGPLRSAIP 133
Cdd:cd03327 31 GPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGrkgiamAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 134 IAWT-LASGDTKRDLDSAVEMIERRrHNRFKVKLGFrSPQD-------DLIHMEALSNSLGSKAYLRVDVNQAWDEQVAS 205
Cdd:cd03327 111 AYASgLYPTDLDELPDEAKEYLKEG-YRGMKMRFGY-GPSDghaglrkNVELVRAIREAVGYDVDLMLDCYMSWNLNYAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 206 VYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAV 285
Cdd:cd03327 189 KMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAAL 268
|
....*.
2CHR_A 286 AEASGI 291
Cdd:cd03327 269 AEAYGV 274
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
147-236 |
9.11e-17 |
|
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: 75.01 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 147 LDSAVEMIERRRHNRFKVKLGFRsPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRE 226
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGGG-PLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|
2CHR_A 227 NTQALRRLSD 236
Cdd:smart00922 84 DLEGLAELRR 93
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
127-349 |
2.38e-15 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 127 PLRSAIPIAWTLASGDTKRdldsAVEMIERRRHNR-FKVKLG--FRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQV 203
Cdd:PRK02901 74 PVRDRVPVNATVPAVDAAQ----VPEVLARFPGCRtAKVKVAepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 204 ASVYIPELEALG-VELIEQPV-GRENTQALRRLSDnnrVAIMADESLSTLASAFDLARDRSVDVFSLKLCNMGGVSAtqk 281
Cdd:PRK02901 150 AVAAARALDADGpLEYVEQPCaTVEELAELRRRVG---VPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRA--- 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2CHR_A 282 IAAVAEASGIASYGGTMLDSTIGTSVALQLYSTVPSLPFGCEL-IGPFVLADTLshEPLEIRDYELQVP 349
Cdd:PRK02901 224 ALDIAEQIGLPVVVSSALDTSVGIAAGLALAAALPELDHACGLaTGGLFEEDVA--DPLLPVDGFLPVR 290
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
66-291 |
2.53e-14 |
|
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: 73.20 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 66 IVERYLAPHLLGTDAFNVSGALQTMARAVTG-NASAKAAVEMALLDLKARALGVSIAELLGGpLRSAIPIAWTLASGDTK 144
Cdd:cd03329 60 LVDRFLKKVLIGQDPLDRERLWQDLWRLQRGlTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 145 RDLDSAVEMIERRRHnrfKVKLGFRS----------PQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEAL 214
Cdd:cd03329 139 EGLESPEAYADFAEE---CKALGYRAiklhpwgpgvVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEEL 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2CHR_A 215 GVELIEQPVGRENTQALRRLSDNNRVAIMADESLS-TLASAFDLARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI 291
Cdd:cd03329 216 GFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRgALESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGL 293
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
99-331 |
2.60e-10 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 60.92 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 99 SAKAAVEMALLDLKARALGVSIAELLGGPLRSAIPIAWTLASGDTKRDLDSAVEMIERRRHnRFKVKLgfrspQDDLI-- 176
Cdd:PRK15129 86 AARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAK-LLKVKL-----DNHLIse 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 177 HMEALsNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSdnNRVAIMADESLSTLASAFD 256
Cdd:PRK15129 160 RMVAI-RSAVPDATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFI--HPLPICADESCHTRSSLKA 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2CHR_A 257 LaRDRsVDVFSLKLCNMGGVSATQKIAAVAEASGIASYGGTMLDSTIGTSVALQLystVPSLPFgCELIGPFVLA 331
Cdd:PRK15129 237 L-KGR-YEMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPL---VPQVRF-ADLDGPTWLA 305
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
103-312 |
1.38e-09 |
|
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: 58.66 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 103 AVEMALLDLKArALGVSIAellggplrSAIPIAwTLASGDTKRDLDSAVEMIERRRhnrFKVKLGFRSPQDDLIHMEALS 182
Cdd:TIGR01927 82 GFESALIELES-GDELPPA--------SNYYVA-LLPAGDPALLLLRSAKAEGFRT---FKWKVGVGELAREGMLVNLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 183 NSLGSKAYLRVDVNQAW--DEQVA-SVYIPELEALGVELIEQPVGRENTqaLRRLSDNNRVAIMADESLSTLASAFDLAR 259
Cdd:TIGR01927 149 EALPDKAELRLDANGGLspDEAQQfLKALDPNLRGRIAFLEEPLPDADE--MSAFSEATGTAIALDESLWELPQLADEYG 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
2CHR_A 260 DRSVDVFSLKLCNMGGVSATQKIAAVAEASGIASyggtMLDSTIGTSVALQLY 312
Cdd:TIGR01927 227 PGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQA----VFSSVFESSIALGQL 275
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
70-366 |
3.47e-09 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 58.00 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 70 YLAPHLLGTDAFNVSGALQTMAR-------AVTgnASAKAAVEMALLDLKARALGVSIAELLGGPLRSAIpIAWTLASGd 142
Cdd:PRK15072 50 HVCPLLIGRDAHRIEDIWQYLYRgaywrrgPVT--MSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGV-MVYGHANG- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 143 tkRDLDSAVEMIerRRHnrfkVKLGFRS----------------PQDDLIHMEALSNSLG-------SKAYLRVdVNQAW 199
Cdd:PRK15072 126 --RDIDELLDDV--ARH----LELGYKAirvqcgvpglkttygvSKGKGLAYEPATKGLLpeeelwsTEKYLRF-VPKLF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 200 dEQVASVYIPEL-------------EA--LGVEL-------IEQPVGRENTQALRRLSDNNRVAIMADESLSTLASAFDL 257
Cdd:PRK15072 197 -EAVRNKFGFDLhllhdvhhrltpiEAarLGKSLepyrlfwLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 258 ARDRSVDVFSLKLCNMGGVSATQKIAAVAEASGI--ASYGGTMLdSTIGTSVALQLYSTVPSlpFGC-ELIGPFVLADTL 334
Cdd:PRK15072 276 IEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVrtGSHGPTDL-SPVCMAAALHFDLWVPN--FGIqEYMGHSEETLEV 352
|
330 340 350
....*....|....*....|....*....|..
2CHR_A 335 SHEPLEIRDYELQVPTGVGHGMTLDEDKVRQY 366
Cdd:PRK15072 353 FPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKY 384
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
162-253 |
2.65e-07 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 51.55 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 162 FKVKLGFRSPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALG---VELIEQPVGRENTQALRRLSDNN 238
Cdd:PRK02714 137 FKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDRRLsgkIEFIEQPLPPDQFDEMLQLSQDY 216
|
90
....*....|....*
2CHR_A 239 RVAIMADESLSTLAS 253
Cdd:PRK02714 217 QTPIALDESVANLAQ 231
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
98-290 |
2.30e-06 |
|
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: 48.93 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 98 ASAKAAVEMALLDLKARALGVSIAELLGGPLR--SAIPIAWTLASGD---TKRDLDSAVEMIER---RRHNRFKVKLGFR 169
Cdd:cd03326 107 AVAVGALDMAVWDAVAKIAGLPLYRLLARRYGrgQADPRVPVYAAGGyyyPGDDLGRLRDEMRRyldRGYTVVKIKIGGA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 170 SPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTQALRRLSDNNRVAIMADESLS 249
Cdd:cd03326 187 PLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLF 266
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2CHR_A 250 TLASAFDLAR------DRSVDVFSLKLCNmgGVSATQKIAAVAEASG 290
Cdd:cd03326 267 SLQDARNLLRyggmrpDRDVLQFDPGLSY--GLPEYLRMLDVLEAHG 311
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
71-222 |
5.84e-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: 44.64 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 71 LAPHLLGTDAFNVSGALQTMARAVTGNAS-------------AKAAVEMALLDLKARALGVSIAELLGG--P--LRSAIP 133
Cdd:cd03324 68 LAHLVVGRDLESIVADMGKFWRRLTSDSQlrwigpekgvihlATAAVVNAVWDLWAKAEGKPLWKLLVDmtPeeLVSCID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 134 IAWtLASGDTKrdlDSAVEMIERRRH-------------------------------------------NRFKVKLGfRS 170
Cdd:cd03324 148 FRY-ITDALTP---EEALEILRRGQPgkaareadllaegypayttsagwlgysdeklrrlckealaqgfTHFKLKVG-AD 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
2CHR_A 171 PQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQP 222
Cdd:cd03324 223 LEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEP 274
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
99-251 |
7.18e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 41.77 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 99 SAKAAVEMALLDLKARALGVSIAELLGgPLR---------SAIPIAWTLASGDTKRDLDSAVEMIERRRHNRFKVKLGFR 169
Cdd:PLN02980 1038 SVRCGLEMAILNAIAVRHGSSLLNILD-PYQkdengseqsHSVQICALLDSNGSPLEVAYVARKLVEEGFSAIKLKVGRR 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2CHR_A 170 -SPQDDLIHMEALSNSLGSKAYLRVDVNQAWDEQVASVYIPELEALGVELIEQPVGRENTqaLRRLSDNNRVAIMADESL 248
Cdd:PLN02980 1117 vSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDEDD--LIKFCEETGLPVALDETI 1194
|
...
2CHR_A 249 STL 251
Cdd:PLN02980 1195 DKF 1197
|
|
| |
