|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00191 |
PLN00191 |
enolase |
5-182 |
2.97e-123 |
|
enolase
Pssm-ID: 215095 [Multi-domain] Cd Length: 457 Bit Score: 355.17 E-value: 2.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSPD-DPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVN 83
Cdd:PLN00191 278 KKYDLDFKEENnDGSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSLEDVQIVGDDLLVTNPKRVAKAIQ 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 84 EKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRI 163
Cdd:PLN00191 358 EKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQIKTGAPCRSERLAKYNQLLRI 437
|
170
....*....|....*....
gi 39644850 164 EEELGSKAKFAGRNFRNPL 182
Cdd:PLN00191 438 EEELGDEAVYAGENFRKPV 456
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
5-182 |
1.40e-113 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 324.82 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSPD-DPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRIAKA 81
Cdd:pfam00113 116 GKYDLDFKGEKsDKSKKLTSAQLADLYEELVKKYPIVSIEDPFDEDDWEAWKYLTERLGdkVQIVGDDLTVTNPKRLKTA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 82 VNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLL 161
Cdd:pfam00113 196 IEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRSGETEDTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLL 275
|
170 180
....*....|....*....|.
gi 39644850 162 RIEEELGSKAKFAGRNFRNPL 182
Cdd:pfam00113 276 RIEEELGSEAKYAGRSFRKPL 296
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
1-166 |
2.49e-113 |
|
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: 328.29 E-value: 2.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 1 FFRSGKYDLDfkspDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRI 78
Cdd:cd03313 245 FYDEGKYVYD----SDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGdkIQIVGDDLFVTNPERL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 79 AKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYN 158
Cdd:cd03313 321 KKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPCRSERTAKYN 400
|
....*...
gi 39644850 159 QLLRIEEE 166
Cdd:cd03313 401 QLLRIEEE 408
|
|
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-180 |
3.33e-104 |
|
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439918 [Multi-domain] Cd Length: 426 Bit Score: 305.41 E-value: 3.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 1 FFRSGKYDLDFKSpddpsRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRI 78
Cdd:COG0148 248 FYKDGKYHLKGEG-----KELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGdkVQLVGDDLFVTNPKRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 79 AKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYN 158
Cdd:COG0148 323 KKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSPSRSERVAKYN 402
|
170 180
....*....|....*....|...
gi 39644850 159 QLLRIEEELGSKAKFAGRN-FRN 180
Cdd:COG0148 403 QLLRIEEELGDAARYAGRSaFKR 425
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
5-182 |
2.93e-82 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 249.58 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSpddpsRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRIAKAV 82
Cdd:TIGR01060 251 GKYVYKGEN-----KQLTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGdkVQIVGDDLFVTNTEILREGI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 83 NEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLR 162
Cdd:TIGR01060 326 EMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAKYNQLLR 405
|
170 180
....*....|....*....|
gi 39644850 163 IEEELGSKAKFAGRNFRNPL 182
Cdd:TIGR01060 406 IEEELGDSARYAGKNSFYRF 425
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00191 |
PLN00191 |
enolase |
5-182 |
2.97e-123 |
|
enolase
Pssm-ID: 215095 [Multi-domain] Cd Length: 457 Bit Score: 355.17 E-value: 2.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSPD-DPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVN 83
Cdd:PLN00191 278 KKYDLDFKEENnDGSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSLEDVQIVGDDLLVTNPKRVAKAIQ 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 84 EKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRI 163
Cdd:PLN00191 358 EKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQIKTGAPCRSERLAKYNQLLRI 437
|
170
....*....|....*....
gi 39644850 164 EEELGSKAKFAGRNFRNPL 182
Cdd:PLN00191 438 EEELGDEAVYAGENFRKPV 456
|
|
| PTZ00081 |
PTZ00081 |
enolase; Provisional |
6-177 |
1.50e-115 |
|
enolase; Provisional
Pssm-ID: 240259 [Multi-domain] Cd Length: 439 Bit Score: 335.09 E-value: 1.50e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 6 KYDLDFKSPDDP-SRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRIAKAV 82
Cdd:PTZ00081 265 VYDLDFKNPNNDkSNKLTGEELVELYLDLVKKYPIVSIEDPFDQDDWEAYAKLTAAIGqkVQIVGDDLLVTNPTRIKKAI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 83 NEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLR 162
Cdd:PTZ00081 345 EKKACNALLLKVNQIGTVTEAIEAAKLAQKNGWGVMVSHRSGETEDTFIADLVVGLGTGQIKTGAPCRSERLAKYNQLLR 424
|
170
....*....|....*
gi 39644850 163 IEEELGSKAKFAGRN 177
Cdd:PTZ00081 425 IEEELGSNAVYAGEN 439
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
5-182 |
1.40e-113 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 324.82 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSPD-DPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRIAKA 81
Cdd:pfam00113 116 GKYDLDFKGEKsDKSKKLTSAQLADLYEELVKKYPIVSIEDPFDEDDWEAWKYLTERLGdkVQIVGDDLTVTNPKRLKTA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 82 VNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLL 161
Cdd:pfam00113 196 IEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRSGETEDTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLL 275
|
170 180
....*....|....*....|.
gi 39644850 162 RIEEELGSKAKFAGRNFRNPL 182
Cdd:pfam00113 276 RIEEELGSEAKYAGRSFRKPL 296
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
1-166 |
2.49e-113 |
|
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: 328.29 E-value: 2.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 1 FFRSGKYDLDfkspDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRI 78
Cdd:cd03313 245 FYDEGKYVYD----SDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGdkIQIVGDDLFVTNPERL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 79 AKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYN 158
Cdd:cd03313 321 KKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPCRSERTAKYN 400
|
....*...
gi 39644850 159 QLLRIEEE 166
Cdd:cd03313 401 QLLRIEEE 408
|
|
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-180 |
3.33e-104 |
|
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439918 [Multi-domain] Cd Length: 426 Bit Score: 305.41 E-value: 3.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 1 FFRSGKYDLDFKSpddpsRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRI 78
Cdd:COG0148 248 FYKDGKYHLKGEG-----KELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGdkVQLVGDDLFVTNPKRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 79 AKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYN 158
Cdd:COG0148 323 KKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSPSRSERVAKYN 402
|
170 180
....*....|....*....|...
gi 39644850 159 QLLRIEEELGSKAKFAGRN-FRN 180
Cdd:COG0148 403 QLLRIEEELGDAARYAGRSaFKR 425
|
|
| eno |
PRK00077 |
enolase; Provisional |
1-183 |
5.16e-101 |
|
enolase; Provisional
Pssm-ID: 234617 [Multi-domain] Cd Length: 425 Bit Score: 297.38 E-value: 5.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 1 FFRSGKYDLDFKSpddpsryISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRI 78
Cdd:PRK00077 248 FYKDGKYVLEGEG-------LTSEEMIDYLAELVDKYPIVSIEDGLDENDWEGWKLLTEKLGdkVQLVGDDLFVTNTKRL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 79 AKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYN 158
Cdd:PRK00077 321 KKGIEKGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVVSHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAKYN 400
|
170 180
....*....|....*....|....*
gi 39644850 159 QLLRIEEELGSKAKFAGRNFRNPLA 183
Cdd:PRK00077 401 QLLRIEEELGDAARYAGKKAFKNLK 425
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
5-182 |
2.93e-82 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 249.58 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 5 GKYDLDFKSpddpsRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAG--IQVVGDDLTVTNPKRIAKAV 82
Cdd:TIGR01060 251 GKYVYKGEN-----KQLTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGdkVQIVGDDLFVTNTEILREGI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 83 NEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLR 162
Cdd:TIGR01060 326 EMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAKYNQLLR 405
|
170 180
....*....|....*....|
gi 39644850 163 IEEELGSKAKFAGRNFRNPL 182
Cdd:TIGR01060 406 IEEELGDSARYAGKNSFYRF 425
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
16-138 |
4.30e-23 |
|
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: 91.62 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 16 DPSRYISPDQLADLYKSfIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRiAKAVNEKSCNCLLLKVN 95
Cdd:cd00308 100 DANGAWTPKEAIRLIRA-LEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDA-LEALELGAVDILQIKPT 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 39644850 96 QIGSVTESLQACKLAQANGWGVMVSHRSG-ETEDTFIADLVVGL 138
Cdd:cd00308 178 RVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAAL 221
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
22-119 |
2.99e-08 |
|
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: 52.13 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 22 SPDQLADLYKSfIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDlTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVT 101
Cdd:COG4948 194 TLEEAIRLLRA-LEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAADE-SLTSRADFRRLIEAGAVDIVNIKLSKVGGLT 271
|
90
....*....|....*...
gi 39644850 102 ESLQACKLAQANGWGVMV 119
Cdd:COG4948 272 EALRIAALAEAHGVPVMP 289
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
16-120 |
8.53e-05 |
|
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: 41.94 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 16 DPSRYISPDQLADLYKSfIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDlTVTNPKRIAKAVNEKSCNCLLLKVN 95
Cdd:cd03315 135 DANRGWTPKQAIRALRA-LEDLGLDYVEQPLPADDLEGRAALARATDTPIMADE-SAFTPHDAFRELALGAADAVNIKTA 212
|
90 100
....*....|....*....|....*
gi 39644850 96 QIGSVTESLQACKLAQANGWGVMVS 120
Cdd:cd03315 213 KTGGLTKAQRVLAVAEALGLPVMVG 237
|
|
| 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 ... |
22-119 |
5.89e-03 |
|
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: 36.40 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39644850 22 SPDQLADLYKSFiKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDlTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVT 101
Cdd:cd03319 189 TPEEAVELLREL-AELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADE-SCFSAADAARLAGGGAYDGINIKLMKTGGLT 266
|
90
....*....|....*...
gi 39644850 102 ESLQACKLAQANGWGVMV 119
Cdd:cd03319 267 EALRIADLARAAGLKVMV 284
|
|
| |
