|
Name |
Accession |
Description |
Interval |
E-value |
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-359 |
0e+00 |
|
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: 584.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 6 IETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFEQPDYVQETLVTERFIIQQHLIPLLLTEALEQPQ 85
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 86 EVSTIFEEVKGNWMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIQEDLPQLLKQVQLAVEKGYQRVKLKI 165
Cdd:cd03317 81 EVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQLLKQIERYLEEGYKRIKLKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 166 RPGYDVEPVALIRQHFPNLPLMVDANSAYTLADLPQLQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSL 245
Cdd:cd03317 161 KPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 246 KDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFASQPTFSFPGDISATERYFY 325
Cdd:cd03317 241 EDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALASLPNFTYPGDISASSRYFE 320
|
330 340 350
....*....|....*....|....*....|....
gi 2574945156 326 EDIITEPFILEQGTMTVPQGLGIGVTLSQTNLLK 359
Cdd:cd03317 321 EDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-334 |
2.10e-117 |
|
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: 343.36 E-value: 2.10e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 9 YQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFEQPDYVQETLVTERFIIQQHLIPLLLTEaLEQPQEVS 88
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINKE-FEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 89 TIFEEVKGNWMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGiQEDLPQLLKQVQLAVEKGYQRVKLKIRPG 168
Cdd:TIGR01928 80 ELVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSG-LANDEQMLKQIESLKATGYKRIKLKITPQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 169 YDVEPVALIRQHFPNLPLMVDANSAYTLADLPQLQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSLKDC 248
Cdd:TIGR01928 159 IMHQLVKLRRLRFPQIPLVIDANESYDLQDFPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 249 QVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFASQPTFSFPGDISATERYFYEDI 328
Cdd:TIGR01928 239 RNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASLGGNDYPGDVSPSGYYFDQDI 318
|
....*.
gi 2574945156 329 ITEPFI 334
Cdd:TIGR01928 319 VAPSIR 324
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-360 |
9.47e-110 |
|
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: 324.85 E-value: 9.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 1 MNIQSIETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFEqpdYVQETLVTerfIIQQHLIPLLLTEA 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGG---TGAEAVAA---ALEEALAPLLIGRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 81 LEQPQEVS-TIFEEVKGNWMGKAALETAIWDLYAKRQQKSLTEFFG-PTRRKIPVGISLGIqEDLPQLLKQVQLAVEKGY 158
Cdd:COG4948 75 PLDIEALWqRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGgKVRDRVPVYATLGI-DTPEEMAEEAREAVARGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 159 QRVKLKI---RPGYDVEPVALIRQHF-PNLPLMVDANSAYTLAD-LPQLQRLDHYQLAMIEQPFAADDFLDHAQLQRELK 233
Cdd:COG4948 154 RALKLKVggpDPEEDVERVRAVREAVgPDARLRVDANGAWTLEEaIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 234 TRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFAS-QPTFS 312
Cdd:COG4948 234 VPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAaLPNFD 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2574945156 313 FpGDISATeRYFYEDIITEPFILEQGTMTVPQGLGIGVTLSQTNLLKY 360
Cdd:COG4948 314 I-VELDGP-LLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
151-352 |
2.93e-54 |
|
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: 177.76 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 151 QLAVEKGYQRVKLKI---RPGYDVEPVALIRQHF-PNLPLMVDANSAYTLAD-LPQLQRLDHYQLAMIEQPFAADDFLDH 225
Cdd:pfam13378 8 RAVEARGFRAFKLKVggpDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEaIRLARALEELGLLWIEEPVPPDDLEGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 226 AQLQRELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMfESGVGRALNLQF 305
Cdd:pfam13378 88 ARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPIGLAASLHL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2574945156 306 ASQPTFSFPGDISATERYFYEDIITEPFILEQGTMTVPQGLGIGVTL 352
Cdd:pfam13378 167 AAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVEL 213
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
3-351 |
1.67e-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: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 3 IQSIETYQVRLPLKTPFVTSYGRleekaFDLFV-ITDEQGNQGFGELVAFEQPDYVQEtlvterfIIQQHLIPLLLteaL 81
Cdd:cd03316 2 ITDVETFVLRVPLPEPGGAVTWR-----NLVLVrVTTDDGITGWGEAYPGGRPSAVAA-------AIEDLLAPLLI---G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 82 EQPQEVSTIFEEVKGN--WMGK--------AALETAIWDLYAKRQQKSLTEFFG-PTRRKIPV-GISLGIQEDLPQLLKQ 149
Cdd:cd03316 67 RDPLDIERLWEKLYRRlfWRGRggvamaaiSAVDIALWDIKGKAAGVPVYKLLGgKVRDRVRVyASGGGYDDSPEELAEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 150 VQLAVEKGYQRVKLKI--------RPGYDVEPVALIRQHF-PNLPLMVDANSAYTLADLPQL-QRLDHYQLAMIEQPFAA 219
Cdd:cd03316 147 AKRAVAEGFTAVKLKVggpdsggeDLREDLARVRAVREAVgPDVDLMVDANGRWDLAEAIRLaRALEEYDLFWFEEPVPP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 220 DDFLDHAQLQRELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVwLGGMFESGVGR 299
Cdd:cd03316 227 DDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRV-APHGAGGPIGL 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2574945156 300 ALNLQF-ASQPTF----SFPGDIsaterYFYEDIITEPFILEQGTMTVPQGLGIGVT 351
Cdd:cd03316 306 AASLHLaAALPNFgileYHLDDL-----PLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
6-317 |
1.31e-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: 172.53 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 6 IETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGElvafeqpdyvqetlvterfiiqqhlipllltealeqpq 85
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 86 evstifeevkgnwMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIQEDlPQLLKQVQLAVEKGYQRVKLKI 165
Cdd:cd03315 43 -------------ATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEP-AEVAEEARRALEAGFRTFKLKV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 166 R--PGYDVEPVALIRQHFPN-LPLMVDANSAYTLADLPQ-LQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDEN 241
Cdd:cd03315 109 GrdPARDVAVVAALREAVGDdAELRVDANRGWTPKQAIRaLRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADES 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2574945156 242 IRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQF-ASQPTFSFPGDI 317
Cdd:cd03315 189 AFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLaAALRAVTLPGEL 265
|
|
| 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 ... |
5-308 |
1.46e-51 |
|
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: 173.91 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 5 SIETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEqGNQGFGELVAFeqpDYVQ-ETLVTerfIIQQ--HLIPLLLTEAL 81
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPT---PRVTgETVES---VLAAlkSVRPALIGGDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 82 EQPQEVSTIFEEVKGNWMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPV-GISLGIQEDlPQLLKQVQLAVEKGYQR 160
Cdd:cd03319 74 RLEKLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLEtDYTISIDTP-EAMAAAAKKAAKRGFPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 161 VKLKI--RPGYDVEPVALIRQHFPNLPLMVDANSAYTLADLPQ-LQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRIC 237
Cdd:cd03319 153 LKIKLggDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVElLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIM 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2574945156 238 LDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFASQ 308
Cdd:cd03319 233 ADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAA 303
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
3-353 |
6.26e-44 |
|
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: 155.55 E-value: 6.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 3 IQSIETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFEQPDYVQETLVTERFIIQQHLIPLLLTEALE 82
Cdd:cd03318 2 IEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 83 QPQEVSTIFEE-VKGNWMGKAALETAIWDLYAKRQQKSLTEFFGPTRRK-IPVGISLG---IQEDLPQLLKQVQlavEKG 157
Cdd:cd03318 82 NIGAAMALLDRaVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDsLPVAWTLAsgdTERDIAEAEEMLE---AGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 158 YQRVKLKI---RPGYDVEPVALIRQHFPN-LPLMVDANSAYTLAD-LPQLQRLDHYQLAMIEQPFAADDFLDHAQLQREL 232
Cdd:cd03318 159 HRRFKLKMgarPPADDLAHVEAIAKALGDrASVRVDVNQAWDESTaIRALPRLEAAGVELIEQPVPRENLDGLARLRSRN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 233 KTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQ-FASQPTF 311
Cdd:cd03318 239 RVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHlFATLPSL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2574945156 312 SFPGDISATeRYFYEDIITEPFILEQGTMTVPQGLGIGVTLS 353
Cdd:cd03318 319 PFGCELFGP-LLLAEDLLEEPLAYRDGELHVPTGPGLGVRLD 359
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-306 |
3.75e-33 |
|
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: 123.21 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 6 IETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGElvafeqpdyvqetlvterfiiqqhlipllltealeqpq 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 86 evstifeevkgnwmGKAALETAIWDLYAKRqqkslteffgptrRKIPVGISLGiqedlpqllkqvqlavekGYQRVKlkI 165
Cdd:cd00308 43 --------------VISGIDMALWDLAAKA-------------LGVPLAELLG------------------GGSRDR--V 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 166 RPGYDVEPVALIRQHFPNLP-LMVDANSAYTLADLPQL-QRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIR 243
Cdd:cd00308 76 PAYGSIERVRAVREAFGPDArLAVDANGAWTPKEAIRLiRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVT 155
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2574945156 244 SLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFA 306
Cdd:cd00308 156 TVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLA 218
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
9-308 |
1.23e-28 |
|
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: 111.97 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 9 YQVRLPLKTPFVTSYGRLEEkaFDLFVI--TDEQGNQGFGElVAfeqpdyvqetlvterfiiqqhliPLLLtealeqpqe 86
Cdd:cd03320 4 YPYSLPLSRPLGTSRGRLTR--RRGLLLrlEDLTGPVGWGE-IA-----------------------PLPL--------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 87 vstifeevkgnwmgKAALETAIWDLyakrqqKSLTEFFGPTRRKIPVG--ISLGIQEDLPQllkqVQLAVEKGYQRVKLK 164
Cdd:cd03320 49 --------------AFGIESALANL------EALLVGFTRPRNRIPVNalLPAGDAAALGE----AKAAYGGGYRTVKLK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 165 IR---PGYDVEPVALIRQHFP-NLPLMVDANSAYTLADLPQ-LQRLDHYQLAMIEQPFAADDFldHAQLQRELKTRICLD 239
Cdd:cd03320 105 VGatsFEEDLARLRALREALPaDAKLRLDANGGWSLEEALAfLEALAAGRIEYIEQPLPPDDL--AELRRLAAGVPIALD 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2574945156 240 ENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGMFESGVGRALNLQFASQ 308
Cdd:cd03320 183 ESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAA 251
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
151-234 |
1.82e-21 |
|
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: 87.72 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 151 QLAVEKGYQRVKLKI--RPGYDVEPVALIRQHF-PNLPLMVDANSAYTLADLPQ-LQRLDHYQLAMIEQPFAADDFLDHA 226
Cdd:smart00922 10 RAVAEAGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAIRaLEALDELGLEWIEEPVPPDDLEGLA 89
|
....*...
gi 2574945156 227 QLQRELKT 234
Cdd:smart00922 90 ELRRATPI 97
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
3-281 |
2.08e-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: 85.23 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 3 IQSIETYQVRLPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFeQPDYVQET--LVTE--RFIIQQHLIPLLLT 78
Cdd:cd03321 3 ITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYLFTY-TPAALKSLkqLLDDmaALLVGEPLAPAELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 79 EALEQPQEVSTIFEEVKgnwMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIqeDLPQL-LKQVQLAVEKG 157
Cdd:cd03321 82 RALAKRFRLLGYTGLVR---MAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGL--DGAKLaTERAVTAAEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 158 YQRVKLKIrpGY-----DVEPVALIRQHFP-NLPLMVDANSAYTLAD-LPQLQRLDHYQLAMIEQPFAADDFLDHAQLQR 230
Cdd:cd03321 157 FHAVKTKI--GYptadeDLAVVRSIRQAVGdGVGLMVDYNQSLTVPEaIERGQALDQEGLTWIEEPTLQHDYEGHARIAS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2574945156 231 ELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQ 281
Cdd:cd03321 235 ALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAE 285
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
66-353 |
1.14e-17 |
|
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: 82.77 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 66 FIIQQHLIPLLL------TEALEQPQEVSTIFEEVKGNWMGK-AALETAIWDLYAKRQQKSLTEFFG-PTRRKIPVGISL 137
Cdd:cd03327 36 WIVDQHLARFLIgkdpsdIEKLWDQMYRATLAYGRKGIAMAAiSAVDLALWDLLGKIRGEPVYKLLGgRTRDKIPAYASG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 138 GIQEDLPQLLKQVQLAVEKGYQrvKLKIRPGY-----------DVEPVALIRQHF-PNLPLMVDA----NSAYTLADLPQ 201
Cdd:cd03327 116 LYPTDLDELPDEAKEYLKEGYR--GMKMRFGYgpsdghaglrkNVELVRAIREAVgYDVDLMLDCymswNLNYAIKMARA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 202 LQRldhYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQ 281
Cdd:cd03327 194 LEK---YELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAE 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2574945156 282 ENDLLV--WLGGMFesgvgralNLQF-ASQPT--FS--FPGDISATERYFYEDIITEPFILEQGTMTVPQGLGIGVTLS 353
Cdd:cd03327 271 AYGVPVvpHASQIY--------NYHFiMSEPNspFAeyLPNSPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
3-292 |
9.23e-17 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 80.18 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 3 IQSIETYQVRLPLKTPFVTSYG-RLEEKAfdLFVITDEQGNQGFGELVAFeqPDYVQetlvTERFIIQQ--HLIPLL--- 76
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGsRSEARV--VVVELEEEGIKGTGECTPY--PRYGE----SDASVMAQimSVVPQLekg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 77 LT-EALEQ--PQevstifeevkgnwmGKA--ALETAIWDLYAKRQQKSLTEFFG---PTRRKIPVGISLGIQEdlpQLLK 148
Cdd:PRK15129 73 LTrEALQKllPA--------------GAArnAVDCALWDLAARQQQQSLAQLIGitlPETVTTAQTVVIGTPE---QMAN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 149 QVQLAVEKGYQRVKLKIRPGYDVEPVALIRQHFPNLPLMVDANSAYT---LADLPQLqrLDHYQLAMIEQPFAADdflDH 225
Cdd:PRK15129 136 SASALWQAGAKLLKVKLDNHLISERMVAIRSAVPDATLIVDANESWRaegLAARCQL--LADLGVAMLEQPLPAQ---DD 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2574945156 226 AQLQRELKT-RICLDENIRSlKDCQVALAlGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGM 292
Cdd:PRK15129 211 AALENFIHPlPICADESCHT-RSSLKALK-GRYEMVNIKLDKTGGLTEALALATEARAQGFALMLGCM 276
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
102-365 |
4.02e-11 |
|
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: 63.88 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 102 AALETAIWDLYAKRQQKSLTEFFGPTRRK-IPVGISL-----GIQEDLP---------------QLLKQVQLAVEK-GYQ 159
Cdd:cd03323 107 TAFEVALLDLLGQALGVPVADLLGGGQRDsVPFLAYLfykgdRHKTDLPypwfrdrwgealtpeGVVRLARAAIDRyGFK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 160 RVKLK---IRPGYDVEPVALIRQHFPNLPLMVDANSAYTLADLPQLQRLDHYQLAMIEQPFAADDFLdhAQLQRelKTRI 236
Cdd:cd03323 187 SFKLKggvLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIRLAKELEGVLAYLEDPCGGREGM--AEFRR--ATGL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 237 CLDEN--IRSLKDCQVALALGScrsinLKIPRV-----GGIHEALKIATFCQENDLLVwlgGMFES---GVGRALNLQFA 306
Cdd:cd03323 263 PLATNmiVTDFRQLGHAIQLNA-----VDIPLAdhhfwGGMRGSVRVAQVCETWGLGW---GMHSNnhlGISLAMMTHVA 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2574945156 307 SqptfSFPGDISATERYFY----EDIITEPFILEQGTMTVPQGLGIGVTLSQTNLLKYS-QYQK 365
Cdd:cd03323 335 A----AAPGLITACDTHWIwqdgQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHeLYQR 394
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
98-352 |
1.46e-10 |
|
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: 62.03 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 98 WMGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIQEDLPQLLKQVQLA------VEKGYQRVKLKI-RPGY- 169
Cdd:cd03329 93 DRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYASTMVGDDLEGLESPEAYAdfaeecKALGYRAIKLHPwGPGVv 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 170 --DVEPVALIRQHF-PNLPLMVDANSAYTLADLPQLQR-LDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSL 245
Cdd:cd03329 173 rrDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLGRaLEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 246 KDCQVALAL-GSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGGmfesgvGRALNLQFAsqptfsfpGDISATEryF 324
Cdd:cd03329 253 LESRADWVLaGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHG------NGAANLHVI--------AAIRNTR--Y 316
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2574945156 325 YEDIITEPFILE----------------QGTMTVPQGLGIGVTL 352
Cdd:cd03329 317 YERGLLHPSQKYdvyagylsvlddpvdsDGFVHVPKGPGLGVEI 360
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
14-308 |
3.02e-10 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 60.80 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 14 PLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAFeqPDYVQETLVTERFIIQQhlIPLLLTEAleqpqEVSTIFEE 93
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEIAPL--PWFGSETLEEALAFCQQ--LPGEITPE-----QIFSIPDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 94 VKGNWMGkaaLETAiWDLyAKRQQKSLTEFFGPTRRKIPVGislgiqedlPQLLKQVQLAVEKGYQRVKLKIRPGYDVEP 173
Cdd:PRK02714 84 LPACQFG---FESA-LEN-ESGSRSNVTLNPLSYSALLPAG---------EAALQQWQTLWQQGYRTFKWKIGVDPLEQE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 174 VALIRQHFPNLP----LMVDANSAYTLAD----LPQLQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSL 245
Cdd:PRK02714 150 LKIFEQLLERLPagakLRLDANGGLSLEEakrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2574945156 246 KDCQVALALGsCRSINLKIPRVGGIHEALKiaTFCQENDLLVWLGGMFESGVGRALNLQFASQ 308
Cdd:PRK02714 230 AQLQQCYQQG-WRGIFVIKPAIAGSPSRLR--QFCQQHPLDAVFSSVFETAIGRKAALALAAE 289
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
137-235 |
6.15e-10 |
|
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: 60.05 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 137 LGIQED-LPQLLKQvqlAVEKGYQRVKLKIrpGYDVEP----VALIRQHF-PNLPLMVDANSAYtlaDLPQ----LQRLD 206
Cdd:cd03324 193 LGYSDEkLRRLCKE---ALAQGFTHFKLKV--GADLEDdirrCRLAREVIgPDNKLMIDANQRW---DVPEaiewVKQLA 264
|
90 100
....*....|....*....|....*....
gi 2574945156 207 HYQLAMIEQPFAADDFLDHAQLQRELKTR 235
Cdd:cd03324 265 EFKPWWIEEPTSPDDILGHAAIRKALAPL 293
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
126-343 |
1.55e-09 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 126 PTRRKIPVGISLG--IQEDLPQLLKQVQlavekGYQRVKLKI-RPGY----DVEPVALIRQHF-PNLPLMVDANSAYT-- 195
Cdd:PRK02901 74 PVRDRVPVNATVPavDAAQVPEVLARFP-----GCRTAKVKVaEPGQtladDVARVNAVRDALgPDGRVRVDANGGWSvd 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 196 --LADLPQLQRLDhyQLAMIEQPFAADDFLdhAQLQRELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEA 273
Cdd:PRK02901 149 eaVAAARALDADG--PLEYVEQPCATVEEL--AELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAA 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2574945156 274 LKIATFCqenDLLVWLGGMFESGVGRALNLQFA-SQPTFSFPGDIsATERYFYEDiITEPFILEQGTMTVP 343
Cdd:PRK02901 225 LDIAEQI---GLPVVVSSALDTSVGIAAGLALAaALPELDHACGL-ATGGLFEED-VADPLLPVDGFLPVR 290
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
19-352 |
3.19e-09 |
|
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: 57.83 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 19 FVTSYGRleekAFDLFVITDEQGNQGFGELVAFEQPDYVQETLvterfiiQQHLIPLLLTEaleQPQEVSTIFEEV-KGN 97
Cdd:cd03322 8 IVTCPGR----NFVTLKITTDQGVTGLGDATLNGRELAVKAYL-------REHLKPLLIGR---DANRIEDIWQYLyRGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 98 WMGK--------AALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIQEDLPQLLKQVQLAVEKGYQRVKLKIRPGY 169
Cdd:cd03322 74 YWRRgpvtmnaiAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQLPKLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 170 DVepvalIRQHF-PNLPLMVDANSAYTLADLPQLQR-LDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDENIRSLKD 247
Cdd:cd03322 154 EA-----VREKFgFEFHLLHDVHHRLTPNQAARFGKdVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 248 CQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDL-LVWLGGMFESGVGRALNLQ-------FASQPTFSFPGDISA 319
Cdd:cd03322 229 WQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrTGWHGPTDLSPVGMAAALHldlwvpnFGIQEYMRHAEETLE 308
|
330 340 350
....*....|....*....|....*....|...
gi 2574945156 320 TERYFYEdiitepfiLEQGTMTVPQGLGIGVTL 352
Cdd:cd03322 309 VFPHSVR--------FEDGYLHPGEEPGLGVEI 333
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
3-307 |
1.77e-08 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 56.40 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 3 IQSIETYQVRLPLKTPFVTS---YGRLEEKAFDLfVITDEQGNQGFGELVAFE--QPDY--VQETLvteRFIIQ------ 69
Cdd:PLN02980 933 ISGMEYSLYRIQLCAPPTSAsvdFSQFHREGFIL-SLSLEDGSVGFGEVAPLEihEEDLldVEEQL---RFLLHvikgak 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 70 -QHLIPLL-------LTEALEQPQevSTIFEEVKgnwmgkAALETAIWDLYAKRQQKSLTEFFGPTRRKipvgislgiqE 141
Cdd:PLN02980 1009 iSFMLPLLkgsfsswIWSELGIPP--SSIFPSVR------CGLEMAILNAIAVRHGSSLLNILDPYQKD----------E 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 142 DLPQLLKQVQLA-------------------VEKGYQRVKLKIrpGYDVEPV--ALIRQHFP-----NLPLMVDANSAYT 195
Cdd:PLN02980 1071 NGSEQSHSVQICalldsngsplevayvarklVEEGFSAIKLKV--GRRVSPIqdAAVIQEVRkavgyQIELRADANRNWT 1148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 196 LADLPQL-QRLDHYQLAMIEQPFAADDflDHAQLQRELKTRICLDENIRSLKDCQ----VALALGSCRSINLKIPRVGGI 270
Cdd:PLN02980 1149 YEEAIEFgSLVKSCNLKYIEEPVQDED--DLIKFCEETGLPVALDETIDKFEECPlrmlTKYTHPGIVAVVIKPSVVGGF 1226
|
330 340 350
....*....|....*....|....*....|....*..
gi 2574945156 271 HEALKIATFCQENDLLVWLGGMFESGVGRALNLQFAS 307
Cdd:PLN02980 1227 ENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFAS 1263
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-125 |
2.20e-08 |
|
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: 51.70 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 5 SIETYQVR-LPLKTPFVTSYGRLEEKAFDLFVITDEQGNQGFGELVAfeqpdyVQETLVTERFIIQQHLIPLLLTEALeQ 83
Cdd:pfam02746 1 AIEVFVVDvGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATS------YGGRAETIKAILDDHLAPLLIGRDA-A 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2574945156 84 PQEVSTIFEE--VKGNWMGKAALETAIWDLYAKRQQKSLTEFFG 125
Cdd:pfam02746 74 NISDLWQLMYraALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
99-231 |
2.11e-07 |
|
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: 52.03 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 99 MGKAALETAIWDLYAKRQQKSLTEFFGPTRRKIPVGISLGIQE-DLPQLLKQVQLAVEKGYQRVKLKI--RPGYDVEPVA 175
Cdd:cd03328 94 MAISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTSyDDDRLREQLSGWVAQGIPRVKMKIgrDPRRDPDRVA 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2574945156 176 LIRQHF-PNLPLMVDANSAYTL-ADLPQLQRLDHYQLAMIEQPFAADDfLDHAQLQRE 231
Cdd:cd03328 174 AARRAIgPDAELFVDANGAYSRkQALALARAFADEGVTWFEEPVSSDD-LAGLRLVRE 230
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
102-353 |
5.80e-07 |
|
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: 50.79 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 102 AALETAIWDLYAKRQQKSLTEFFG-PTRRKIPV--GISLGIQEDLPQLLKQVQlavEKGYQRVKL-------------KI 165
Cdd:cd03325 83 SGIDQALWDIKGKVLGVPVHQLLGgQVRDRVRVysWIGGDRPSDVAEAARARR---EAGFTAVKMnateelqwidtskKV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 166 RPGydVEPVALIRQHF-PNLPLMVDAN---SAYTLADLpqLQRLDHYQLAMIEQPFAADDFLDHAQLQRELKTRICLDEN 241
Cdd:cd03325 160 DAA--VERVAALREAVgPDIDIGVDFHgrvSKPMAKDL--AKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGER 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 242 IRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLlvwlgGMF----ESGVGRALNLQF-ASQPTFsFPGD 316
Cdd:cd03325 236 LFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV-----ALAphcpLGPIALAASLHVdASTPNF-LIQE 309
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2574945156 317 ISATERYFYED------IITEPFILEQGTMTVPQGLGIGVTLS 353
Cdd:cd03325 310 QSLGIHYNEGDdlldylVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| PTZ00081 |
PTZ00081 |
enolase; Provisional |
208-283 |
2.08e-05 |
|
enolase; Provisional
Pssm-ID: 240259 [Multi-domain] Cd Length: 439 Bit Score: 46.19 E-value: 2.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2574945156 208 YQLAMIEQPFAADDFLDHAQLQREL--KTRICLDE-NIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQEN 283
Cdd:PTZ00081 297 YPIVSIEDPFDQDDWEAYAKLTAAIgqKVQIVGDDlLVTNPTRIKKAIEKKACNALLLKVNQIGTVTEAIEAAKLAQKN 375
|
|
| MAL |
cd03314 |
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ... |
230-291 |
1.68e-04 |
|
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL 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: 239430 [Multi-domain] Cd Length: 369 Bit Score: 43.16 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2574945156 230 RELKTRICLDENIRSLKDCQVALALGSCRSINLKIPRVGGIHEALKIATFCQENDLLVWLGG 291
Cdd:cd03314 258 RGVGVRIVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGGIDNTIDAVLYCKEHGVGAYLGG 319
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
102-258 |
5.37e-04 |
|
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: 41.61 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 102 AALETAIWDLYAKRQQKSLTEFF------GPTRRKIPVGISLGI---QEDLPQLLKQVQLAVEKGYQRVKLKIRP---GY 169
Cdd:cd03326 111 GALDMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVYAAGGYyypGDDLGRLRDEMRRYLDRGYTVVKIKIGGaplDE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 170 DVEPV-ALIRQHFPNLPLMVDANSAYTLADLPQLQR-LDHYQLAMIEQPfaaDDFLDHAqLQRELKTR----ICLDENIR 243
Cdd:cd03326 191 DLRRIeAALDVLGDGARLAVDANGRFDLETAIAYAKaLAPYGLRWYEEP---GDPLDYA-LQAELADHydgpIATGENLF 266
|
170
....*....|....*
gi 2574945156 244 SLKDCQVALALGSCR 258
Cdd:cd03326 267 SLQDARNLLRYGGMR 281
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
205-283 |
1.19e-03 |
|
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.
Pssm-ID: 239429 [Multi-domain] Cd Length: 408 Bit Score: 40.54 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574945156 205 LDHYQLAMIEQPFAADDFLDHAQLQREL--KTRICLDE----NIRSLKDcqvALALGSCRSINLKIPRVGGIHEALKIAT 278
Cdd:cd03313 274 VKKYPIVSIEDPFDEDDWEGWAKLTAKLgdKIQIVGDDlfvtNPERLKK---GIEKKAANALLIKVNQIGTLTETIEAIK 350
|
....*
gi 2574945156 279 FCQEN 283
Cdd:cd03313 351 LAKKN 355
|
|
| |
