|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00191 |
PLN00191 |
enolase |
2-432 |
0e+00 |
|
enolase
Pssm-ID: 215095 [Multi-domain] Cd Length: 457 Bit Score: 832.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 2 SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKqRYLGKGVLKAVDHINSRIAPALIssG 81
Cdd:PLN00191 27 TITKVKARQIIDSRGNPTVEVDLHTSKGMFRAAVPSGASTGIYEALELRDGDK-DYLGKGVLKAVKNVNEIIAPALI--G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 82 ISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN 161
Cdd:PLN00191 104 MDPTDQTQIDNFMLELDGTPNKGKLGANAILAVSLAVCKAGAAEKGVPLYKHIADLAGNKKLVLPVPAFNVINGGSHAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 162 KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMV 241
Cdd:PLN00191 184 KLAMQEFMILPVGASSFKEAMQMGSEVYHHLKAVIKKKYGQDACNVGDEGGFAPNIQDNKEGLELLKEAIEKAGYTGKIK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 242 IGMDVAASEFY-RDGKYDLDFKSPA-DPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDD 319
Cdd:PLN00191 264 IGMDVAASEFYtKDKKYDLDFKEENnDGSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSLEDVQIVGDD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 320 LTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPC 399
Cdd:PLN00191 344 LLVTNPKRVAKAIQEKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQIKTGAPC 423
|
410 420 430
....*....|....*....|....*....|...
gi 119348 400 RSERLAKYNQLMRIEEELGDEARFAGHNFRNPS 432
Cdd:PLN00191 424 RSERLAKYNQLLRIEEELGDEAVYAGENFRKPV 456
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
5-416 |
0e+00 |
|
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: 785.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 5 KIWAREILDSRGNPTVEVDLYTA-KGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIssGIS 83
Cdd:cd03313 1 KIKAREILDSRGNPTVEVEVTTEdGGVGRAAVPSGASTGEHEAVELRDGDKSRYLGKGVLKAVKNVNEIIAPALI--GMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 84 VVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAgnsDLILPVPAFNVINGGSHAGNKL 163
Cdd:cd03313 79 VTDQRAIDKLLIELDGTPNKSKLGANAILGVSLAVAKAAAAALGLPLYRYLGGLA---AYVLPVPMFNVINGGAHAGNKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 164 AMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT--EKMV 241
Cdd:cd03313 156 DFQEFMIVPVGAPSFSEALRMGAEVYHTLKKVLKKKGGLLATNVGDEGGFAPNLSSNEEALDLLVEAIEKAGYEpgKKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 242 IGMDVAASEFYRDGKYDLDfkspADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQIVGDD 319
Cdd:cd03313 236 IALDVAASEFYDEGKYVYD----SDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGdkIQIVGDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 320 LTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPC 399
Cdd:cd03313 312 LFVTNPERLKKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPC 391
|
410
....*....|....*..
gi 119348 400 RSERLAKYNQLMRIEEE 416
Cdd:cd03313 392 RSERTAKYNQLLRIEEE 408
|
|
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-430 |
0e+00 |
|
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439918 [Multi-domain] Cd Length: 426 Bit Score: 747.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 1 MS-IEKIWAREILDSRGNPTVEVDLYTAKGLF-RAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALI 78
Cdd:COG0148 1 MSrIEDVHAREILDSRGNPTVEVEVTLEDGAVgRAAVPSGASTGSHEAVELRDGDKSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 79 ssGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHiaqLAGNSDLILPVPAFNVINGGSH 158
Cdd:COG0148 81 --GMDATDQRAIDRAMIELDGTPNKSRLGANAILGVSLAVAKAAAAALGLPLYRY---LGGVNAKTLPVPMMNIINGGAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 159 AGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKygKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT- 237
Cdd:COG0148 156 ADNNVDIQEFMIMPVGAPSFSEALRMGAEVFHALKKVLKEK--GLSTAVGDEGGFAPNLKSNEEALELILEAIEKAGYKp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 238 -EKMVIGMDVAASEFYRDGKYDLdfkspADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQ 314
Cdd:COG0148 234 gEDIALALDVAASEFYKDGKYHL-----KGEGKELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGdkVQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 315 IVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIK 394
Cdd:COG0148 309 LVGDDLFVTNPKRLKKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIK 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 119348 395 TGAPCRSERLAKYNQLMRIEEELGDEARFAGHN-FRN 430
Cdd:COG0148 389 TGSPSRSERVAKYNQLLRIEEELGDAARYAGRSaFKR 425
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
3-431 |
0e+00 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 615.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 3 IEKIWAREILDSRGNPTVEVDLYTAKGLF-RAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIssG 81
Cdd:TIGR01060 1 IVDIRAREILDSRGNPTVEVEVILEDGTFgRAAVPSGASTGEREALELRDGDKKRYLGKGVLKAVENVNEIIAPELI--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 82 ISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHiaqLAGNSDLILPVPAFNVINGGSHAGN 161
Cdd:TIGR01060 79 MDATDQREIDQILIELDGTPNKSKLGANAILGVSMAVAKAAADSLGLPLYRY---LGGFNAYVLPVPMMNIINGGAHADN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 162 KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYgkDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT--EK 239
Cdd:TIGR01060 156 NLDFQEFMIMPVGAPSFREALRMGAEVFHALKKLLKEKG--LATGVGDEGGFAPNLASNEEALEIIVEAIEKAGYKpgED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 240 MVIGMDVAASEFY--RDGKYDLDFKSpadpsRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQI 315
Cdd:TIGR01060 234 VALALDCAASEFYdeEDGKYVYKGEN-----KQLTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGdkVQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 316 VGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKT 395
Cdd:TIGR01060 309 VGDDLFVTNTEILREGIEMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKT 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 119348 396 GAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNP 431
Cdd:TIGR01060 389 GSLSRSERIAKYNQLLRIEEELGDSARYAGKNSFYR 424
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
143-432 |
0e+00 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 508.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 143 LILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSE 222
Cdd:pfam00113 2 YVLPVPMMNVINGGSHAGNNLAFQEFMILPTGAPSFSEAMRMGAEVYHHLKSVLKAKYGQSATNVGDEGGFAPNLQSNKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 223 ALELVKEAIDKAGYTEKMVIGMDVAASEFY--RDGKYDLDFKSP-ADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQD 299
Cdd:pfam00113 82 ALDLIVEAIEKAGYKGKIKIAMDVASSEFYnkKDGKYDLDFKGEkSDKSKKLTSAQLADLYEELVKKYPIVSIEDPFDED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 300 DWAAWSKFTANVG--IQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETE 377
Cdd:pfam00113 162 DWEAWKYLTERLGdkVQIVGDDLTVTNPKRLKTAIEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRSGETE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119348 378 DTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPS 432
Cdd:pfam00113 242 DTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLLRIEEELGSEAKYAGRSFRKPL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00191 |
PLN00191 |
enolase |
2-432 |
0e+00 |
|
enolase
Pssm-ID: 215095 [Multi-domain] Cd Length: 457 Bit Score: 832.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 2 SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKqRYLGKGVLKAVDHINSRIAPALIssG 81
Cdd:PLN00191 27 TITKVKARQIIDSRGNPTVEVDLHTSKGMFRAAVPSGASTGIYEALELRDGDK-DYLGKGVLKAVKNVNEIIAPALI--G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 82 ISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN 161
Cdd:PLN00191 104 MDPTDQTQIDNFMLELDGTPNKGKLGANAILAVSLAVCKAGAAEKGVPLYKHIADLAGNKKLVLPVPAFNVINGGSHAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 162 KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMV 241
Cdd:PLN00191 184 KLAMQEFMILPVGASSFKEAMQMGSEVYHHLKAVIKKKYGQDACNVGDEGGFAPNIQDNKEGLELLKEAIEKAGYTGKIK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 242 IGMDVAASEFY-RDGKYDLDFKSPA-DPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDD 319
Cdd:PLN00191 264 IGMDVAASEFYtKDKKYDLDFKEENnDGSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSLEDVQIVGDD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 320 LTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPC 399
Cdd:PLN00191 344 LLVTNPKRVAKAIQEKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQIKTGAPC 423
|
410 420 430
....*....|....*....|....*....|...
gi 119348 400 RSERLAKYNQLMRIEEELGDEARFAGHNFRNPS 432
Cdd:PLN00191 424 RSERLAKYNQLLRIEEELGDEAVYAGENFRKPV 456
|
|
| PTZ00081 |
PTZ00081 |
enolase; Provisional |
1-427 |
0e+00 |
|
enolase; Provisional
Pssm-ID: 240259 [Multi-domain] Cd Length: 439 Bit Score: 810.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 1 MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIss 80
Cdd:PTZ00081 2 STIKSIKAREILDSRGNPTVEVDLTTEKGVFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVENVNEIIAPALI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 81 GISVVEQEKLDNLMLE-LDGTEN-----KSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGN--SDLILPVPAFNV 152
Cdd:PTZ00081 80 GKDVTDQKKLDKLMVEqLDGTKNewgwcKSKLGANAILAVSMAVARAAAAAKGVPLYKYLAQLAGKptDKFVLPVPCFNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 153 INGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAID 232
Cdd:PTZ00081 160 INGGKHAGNKLAFQEFMIAPVGAPSFKEALRMGAEVYHSLKSVIKKKYGLDATNVGDEGGFAPNIKDPEEALDLLVEAIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 233 KAGYTEKMVIGMDVAASEFYRDGK--YDLDFKSPADP-SRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTA 309
Cdd:PTZ00081 240 KAGYEGKVKICMDVAASEFYDKEKkvYDLDFKNPNNDkSNKLTGEELVELYLDLVKKYPIVSIEDPFDQDDWEAYAKLTA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 310 NVG--IQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVG 387
Cdd:PTZ00081 320 AIGqkVQIVGDDLLVTNPTRIKKAIEKKACNALLLKVNQIGTVTEAIEAAKLAQKNGWGVMVSHRSGETEDTFIADLVVG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 119348 388 LCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHN 427
Cdd:PTZ00081 400 LGTGQIKTGAPCRSERLAKYNQLLRIEEELGSNAVYAGEN 439
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
5-416 |
0e+00 |
|
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: 785.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 5 KIWAREILDSRGNPTVEVDLYTA-KGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIssGIS 83
Cdd:cd03313 1 KIKAREILDSRGNPTVEVEVTTEdGGVGRAAVPSGASTGEHEAVELRDGDKSRYLGKGVLKAVKNVNEIIAPALI--GMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 84 VVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAgnsDLILPVPAFNVINGGSHAGNKL 163
Cdd:cd03313 79 VTDQRAIDKLLIELDGTPNKSKLGANAILGVSLAVAKAAAAALGLPLYRYLGGLA---AYVLPVPMFNVINGGAHAGNKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 164 AMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT--EKMV 241
Cdd:cd03313 156 DFQEFMIVPVGAPSFSEALRMGAEVYHTLKKVLKKKGGLLATNVGDEGGFAPNLSSNEEALDLLVEAIEKAGYEpgKKIA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 242 IGMDVAASEFYRDGKYDLDfkspADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQIVGDD 319
Cdd:cd03313 236 IALDVAASEFYDEGKYVYD----SDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGdkIQIVGDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 320 LTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPC 399
Cdd:cd03313 312 LFVTNPERLKKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPC 391
|
410
....*....|....*..
gi 119348 400 RSERLAKYNQLMRIEEE 416
Cdd:cd03313 392 RSERTAKYNQLLRIEEE 408
|
|
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-430 |
0e+00 |
|
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439918 [Multi-domain] Cd Length: 426 Bit Score: 747.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 1 MS-IEKIWAREILDSRGNPTVEVDLYTAKGLF-RAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALI 78
Cdd:COG0148 1 MSrIEDVHAREILDSRGNPTVEVEVTLEDGAVgRAAVPSGASTGSHEAVELRDGDKSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 79 ssGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHiaqLAGNSDLILPVPAFNVINGGSH 158
Cdd:COG0148 81 --GMDATDQRAIDRAMIELDGTPNKSRLGANAILGVSLAVAKAAAAALGLPLYRY---LGGVNAKTLPVPMMNIINGGAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 159 AGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKygKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT- 237
Cdd:COG0148 156 ADNNVDIQEFMIMPVGAPSFSEALRMGAEVFHALKKVLKEK--GLSTAVGDEGGFAPNLKSNEEALELILEAIEKAGYKp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 238 -EKMVIGMDVAASEFYRDGKYDLdfkspADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQ 314
Cdd:COG0148 234 gEDIALALDVAASEFYKDGKYHL-----KGEGKELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGdkVQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 315 IVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIK 394
Cdd:COG0148 309 LVGDDLFVTNPKRLKKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIK 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 119348 395 TGAPCRSERLAKYNQLMRIEEELGDEARFAGHN-FRN 430
Cdd:COG0148 389 TGSPSRSERVAKYNQLLRIEEELGDAARYAGRSaFKR 425
|
|
| eno |
PRK00077 |
enolase; Provisional |
1-430 |
0e+00 |
|
enolase; Provisional
Pssm-ID: 234617 [Multi-domain] Cd Length: 425 Bit Score: 719.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 1 MSIEKIWAREILDSRGNPTVEVDLYTAKGLF-RAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIs 79
Cdd:PRK00077 2 SKIEDIIAREILDSRGNPTVEVEVTLEDGAFgRAAVPSGASTGEREAVELRDGDKSRYLGKGVLKAVENVNEEIAPALI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 80 sGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHiaqLAGNSDLILPVPAFNVINGGSHA 159
Cdd:PRK00077 81 -GLDALDQRAIDKAMIELDGTPNKSKLGANAILGVSLAVAKAAADSLGLPLYRY---LGGPNAKVLPVPMMNIINGGAHA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 160 GNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKyGKdATNVGDEGGFAPNILENSEALELVKEAIDKAGYT-- 237
Cdd:PRK00077 157 DNNVDIQEFMIMPVGAPSFKEALRMGAEVFHTLKKVLKEK-GL-STAVGDEGGFAPNLKSNEEALDLILEAIEKAGYKpg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 238 EKMVIGMDVAASEFYRDGKYDLDFKSpadpsryITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQI 315
Cdd:PRK00077 235 EDIALALDCAASEFYKDGKYVLEGEG-------LTSEEMIDYLAELVDKYPIVSIEDGLDENDWEGWKLLTEKLGdkVQL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 316 VGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKT 395
Cdd:PRK00077 308 VGDDLFVTNTKRLKKGIEKGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVVSHRSGETEDTTIADLAVATNAGQIKT 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 119348 396 GAPCRSERLAKYNQLMRIEEELGDEARFAGHN-FRN 430
Cdd:PRK00077 388 GSLSRSERIAKYNQLLRIEEELGDAARYAGKKaFKN 423
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
3-431 |
0e+00 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 615.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 3 IEKIWAREILDSRGNPTVEVDLYTAKGLF-RAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIssG 81
Cdd:TIGR01060 1 IVDIRAREILDSRGNPTVEVEVILEDGTFgRAAVPSGASTGEREALELRDGDKKRYLGKGVLKAVENVNEIIAPELI--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 82 ISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHiaqLAGNSDLILPVPAFNVINGGSHAGN 161
Cdd:TIGR01060 79 MDATDQREIDQILIELDGTPNKSKLGANAILGVSMAVAKAAADSLGLPLYRY---LGGFNAYVLPVPMMNIINGGAHADN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 162 KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYgkDATNVGDEGGFAPNILENSEALELVKEAIDKAGYT--EK 239
Cdd:TIGR01060 156 NLDFQEFMIMPVGAPSFREALRMGAEVFHALKKLLKEKG--LATGVGDEGGFAPNLASNEEALEIIVEAIEKAGYKpgED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 240 MVIGMDVAASEFY--RDGKYDLDFKSpadpsRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVG--IQI 315
Cdd:TIGR01060 234 VALALDCAASEFYdeEDGKYVYKGEN-----KQLTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGdkVQI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 316 VGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKT 395
Cdd:TIGR01060 309 VGDDLFVTNTEILREGIEMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKT 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 119348 396 GAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNP 431
Cdd:TIGR01060 389 GSLSRSERIAKYNQLLRIEEELGDSARYAGKNSFYR 424
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
143-432 |
0e+00 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 508.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 143 LILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSE 222
Cdd:pfam00113 2 YVLPVPMMNVINGGSHAGNNLAFQEFMILPTGAPSFSEAMRMGAEVYHHLKSVLKAKYGQSATNVGDEGGFAPNLQSNKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 223 ALELVKEAIDKAGYTEKMVIGMDVAASEFY--RDGKYDLDFKSP-ADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQD 299
Cdd:pfam00113 82 ALDLIVEAIEKAGYKGKIKIAMDVASSEFYnkKDGKYDLDFKGEkSDKSKKLTSAQLADLYEELVKKYPIVSIEDPFDED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 300 DWAAWSKFTANVG--IQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETE 377
Cdd:pfam00113 162 DWEAWKYLTERLGdkVQIVGDDLTVTNPKRLKTAIEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRSGETE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119348 378 DTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPS 432
Cdd:pfam00113 242 DTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLLRIEEELGSEAKYAGRSFRKPL 296
|
|
| Enolase_N |
pfam03952 |
Enolase, N-terminal domain; |
3-134 |
1.51e-85 |
|
Enolase, N-terminal domain;
Pssm-ID: 461105 [Multi-domain] Cd Length: 131 Bit Score: 257.30 E-value: 1.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 3 IEKIWAREILDSRGNPTVEVDLYTAKG-LFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALIssG 81
Cdd:pfam03952 1 ITKVKAREILDSRGNPTVEVEVTLEDGtFGRAAVPSGASTGEHEAVELRDGDKSRYGGKGVLKAVENVNEIIAPALI--G 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 119348 82 ISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHI 134
Cdd:pfam03952 79 MDATDQRAIDRALIELDGTENKSKLGANAILGVSLAVAKAAAAALGLPLYRYL 131
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
266-388 |
2.11e-19 |
|
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: 86.61 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 266 DPSRYITGDQLGALYQDfVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIErAVEEKACNCLLLKVN 345
Cdd:cd00308 100 DANGAWTPKEAIRLIRA-LEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALE-ALELGAVDILQIKPT 177
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 119348 346 QIGSVTEAIQACKLAQENGWGVMVSHRSG-ETEDTFIADLVVGL 388
Cdd:cd00308 178 RVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAAL 221
|
|
| PRK08350 |
PRK08350 |
hypothetical protein; Provisional |
3-422 |
4.02e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 169397 [Multi-domain] Cd Length: 341 Bit Score: 79.08 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 3 IEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEAlELRdgdkqrylgkgvlKAVDHINSRIAPALIssGI 82
Cdd:PRK08350 4 IENIIGRVAVLRGGKYSVEVDVITDSGFGRFAAPIDENPSLYIA-EAH-------------RAVSEVDEIIGPELI--GF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 83 SVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIaqlAGNSDLILPVPAFNVINGgshagnk 162
Cdd:PRK08350 68 DASEQELIDSYLWEIDGTEDFSHIGANTALAVSVAVAKAAANSKNMPLYSYI---GGTFTTELPVPILEFAED------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 163 lAMQEFMILpvgaesFRDAMRLGAEVyhtlkgvikdkygkDATNvgdeggfapNILENSEALELvkEAIDKAGYTEKMVI 242
Cdd:PRK08350 138 -ENFEYYVL------VRDLMEITDVV--------------DAVN---------KILENSKEVSL--EGLSKASEKAGDEL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 243 GMDVAASefyrdgkydLDFKSPADPSRYITgdqlgalyqdFVRNYPVVSIEDPFDQDDWAAWSKFTAnvGIQIVGDDLTv 322
Cdd:PRK08350 186 GLEVALG---------IAQKREMETEKVLN----------LVEDNNIAYIKPIGDEELFLELIAGTH--GVFIDGEYLF- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 323 tnpkRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGL-CTGQIktgapCRS 401
Cdd:PRK08350 244 ----RTRNILDRRYYNALSIKPINLGTLTDLYNLVNDVKSERITPILAEAKYESADEALPHLAVGLrCPAML-----IHK 314
|
410 420
....*....|....*....|.
gi 119348 402 ERLAKYNQLMRIEEELGDEAR 422
Cdd:PRK08350 315 DSVEKINELNRIAEDLGERGR 335
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
287-369 |
5.13e-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: 54.44 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 287 YPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDlTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWG 366
Cdd:COG4948 208 LGLEWIEQPLPAEDLEGLAELRRATPVPIAADE-SLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVP 286
|
...
gi 119348 367 VMV 369
Cdd:COG4948 287 VMP 289
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
181-370 |
1.70e-04 |
|
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: 43.10 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 181 AMRLGAEVYHTLKGViKDKYgkdatnvgdEGGFAPNILENSEALELVkEAIDKAGY-TEKMVIG----MDVAASEFYRDG 255
Cdd:cd03315 57 GKRLGVPVYLLLGGY-RDRV---------RVAHMLGLGEPAEVAEEA-RRALEAGFrTFKLKVGrdpaRDVAVVAALREA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 256 kYDLDFKSPADPSRYITGDQ-LGALYQdfVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDlTVTNPKRIERAVEE 334
Cdd:cd03315 126 -VGDDAELRVDANRGWTPKQaIRALRA--LEDLGLDYVEQPLPADDLEGRAALARATDTPIMADE-SAFTPHDAFRELAL 201
|
170 180 190
....*....|....*....|....*....|....*.
gi 119348 335 KACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVS 370
Cdd:cd03315 202 GAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVG 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 ... |
284-369 |
3.81e-04 |
|
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: 42.18 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 284 VRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDlTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQEN 363
Cdd:cd03319 200 LAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADE-SCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAA 278
|
....*.
gi 119348 364 GWGVMV 369
Cdd:cd03319 279 GLKVMV 284
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
286-367 |
3.79e-03 |
|
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: 39.14 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119348 286 NYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDlTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGW 365
Cdd:cd03317 202 EYGLLMIEQPLAADDLIDHAELQKLLKTPICLDE-SIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI 280
|
..
gi 119348 366 GV 367
Cdd:cd03317 281 PV 282
|
|
| |
