|
Name |
Accession |
Description |
Interval |
E-value |
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-425 |
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: 849.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVI 79
Cdd:COG0148 1 MSRIEDVHAREILDSRGNPTVEVEVTLEDGAVGRAAVPSGASTGSHEAVELRDGDkSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 80 GLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSV 159
Cdd:COG0148 81 GMDATDQRAIDRAMIELDGTPNKSRLGANAILGVSLAVAKAAAAALGLPLYRYLGGVNAKTLPVPMMNIINGGAHADNNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 160 DVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVAL 239
Cdd:COG0148 161 DIQEFMIMPVGAPSFSEALRMGAEVFHALKKVLKEKGLSTAVGDEGGFAPNLKS-NEEALELILEAIEKAGYKPGEDIAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 240 ALDVAATEFYTAGQgYKF--EGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTN 317
Cdd:COG0148 240 ALDVAASEFYKDGK-YHLkgEGKELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGDKVQLVGDDLFVTN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 318 PERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERV 397
Cdd:COG0148 319 PKRLKKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSPSRSERV 398
|
410 420
....*....|....*....|....*...
gi 518772133 398 AKYNQLLRIEDALGDSARYAGDVAFPRF 425
Cdd:COG0148 399 AKYNQLLRIEEELGDAARYAGRSAFKRL 426
|
|
| eno |
PRK00077 |
enolase; Provisional |
1-426 |
0e+00 |
|
enolase; Provisional
Pssm-ID: 234617 [Multi-domain] Cd Length: 425 Bit Score: 826.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVI 79
Cdd:PRK00077 1 MSKIEDIIAREILDSRGNPTVEVEVTLEDGAFGRAAVPSGASTGEREAVELRDGDkSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 80 GLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSV 159
Cdd:PRK00077 81 GLDALDQRAIDKAMIELDGTPNKSKLGANAILGVSLAVAKAAADSLGLPLYRYLGGPNAKVLPVPMMNIINGGAHADNNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 160 DVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVAL 239
Cdd:PRK00077 161 DIQEFMIMPVGAPSFKEALRMGAEVFHTLKKVLKEKGLSTAVGDEGGFAPNLKS-NEEALDLILEAIEKAGYKPGEDIAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 240 ALDVAATEFYTAGQgYKFEGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPE 319
Cdd:PRK00077 240 ALDCAASEFYKDGK-YVLEGEGLTSEEMIDYLAELVDKYPIVSIEDGLDENDWEGWKLLTEKLGDKVQLVGDDLFVTNTK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 320 RLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAK 399
Cdd:PRK00077 319 RLKKGIEKGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVVSHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAK 398
|
410 420
....*....|....*....|....*..
gi 518772133 400 YNQLLRIEDALGDSARYAGDVAFPRFS 426
Cdd:PRK00077 399 YNQLLRIEEELGDAARYAGKKAFKNLK 425
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
7-408 |
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: 720.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 7 VGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGGD-RYGGKGVQKAVEGVLDEIAPAVIGLDAVE 85
Cdd:cd03313 2 IKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTGEHEAVELRDGDKsRYLGKGVLKAVKNVNEIIAPALIGMDVTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 86 QRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSVDVQEFM 165
Cdd:cd03313 82 QRAIDKLLIELDGTPNKSKLGANAILGVSLAVAKAAAAALGLPLYRYLGGLAAYVLPVPMFNVINGGAHAGNKLDFQEFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 166 IAPIGAPTFKEALRWGAEVYHALKSELKSKG--LATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVALALDV 243
Cdd:cd03313 162 IVPVGAPSFSEALRMGAEVYHTLKKVLKKKGglLATNVGDEGGFAPNLSS-NEEALDLLVEAIEKAGYEPGKKIAIALDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 244 AATEFYTAGQGY--KFEGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPERL 321
Cdd:cd03313 241 AASEFYDEGKYVydSDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGDKIQIVGDDLFVTNPERL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 322 EDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAKYN 401
Cdd:cd03313 321 KKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPCRSERTAKYN 400
|
....*..
gi 518772133 402 QLLRIED 408
Cdd:cd03313 401 QLLRIEE 407
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
4-425 |
0e+00 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 712.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 4 IEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVIGLD 82
Cdd:TIGR01060 1 IVDIRAREILDSRGNPTVEVEVILEDGTFGRAAVPSGASTGEREALELRDGDkKRYLGKGVLKAVENVNEIIAPELIGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 83 AVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSVDVQ 162
Cdd:TIGR01060 81 ATDQREIDQILIELDGTPNKSKLGANAILGVSMAVAKAAADSLGLPLYRYLGGFNAYVLPVPMMNIINGGAHADNNLDFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 163 EFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVALALD 242
Cdd:TIGR01060 161 EFMIMPVGAPSFREALRMGAEVFHALKKLLKEKGLATGVGDEGGFAPNLAS-NEEALEIIVEAIEKAGYKPGEDVALALD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 243 VAATEFYTAGQG-YKFEGSVR--SADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPE 319
Cdd:TIGR01060 240 CAASEFYDEEDGkYVYKGENKqlTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGDKVQIVGDDLFVTNTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 320 RLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAK 399
Cdd:TIGR01060 320 ILREGIEMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAK 399
|
410 420
....*....|....*....|....*.
gi 518772133 400 YNQLLRIEDALGDSARYAGDVAFPRF 425
Cdd:TIGR01060 400 YNQLLRIEEELGDSARYAGKNSFYRF 425
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
138-418 |
4.23e-151 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 430.36 E-value: 4.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 138 AHVLPVPMMNILNGGAHADTSVDVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKG--LATGLGDEGGFAPDLaGGT 215
Cdd:pfam00113 1 SYVLPVPMMNVINGGSHAGNNLAFQEFMILPTGAPSFSEAMRMGAEVYHHLKSVLKAKYgqSATNVGDEGGFAPNL-QSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 216 REALDLIAAAVAKTGYRLgtDVALALDVAATEFYTAGQG---YKFEGS------VRSADEMAKFYAELLTGYPLVSIEDP 286
Cdd:pfam00113 80 KEALDLIVEAIEKAGYKG--KIKIAMDVASSEFYNKKDGkydLDFKGEksdkskKLTSAQLADLYEELVKKYPIVSIEDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 287 LAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRS 366
Cdd:pfam00113 158 FDEDDWEAWKYLTERLGDKVQIVGDDLTVTNPKRLKTAIEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518772133 367 GETEDTTIADLAVAVGSGQIKTGAPARSERVAKYNQLLRIEDALGDSARYAG 418
Cdd:pfam00113 238 GETEDTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLLRIEEELGSEAKYAG 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Eno |
COG0148 |
Enolase [Carbohydrate transport and metabolism]; Enolase is part of the Pathway/BioSystem: ... |
1-425 |
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: 849.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVI 79
Cdd:COG0148 1 MSRIEDVHAREILDSRGNPTVEVEVTLEDGAVGRAAVPSGASTGSHEAVELRDGDkSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 80 GLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSV 159
Cdd:COG0148 81 GMDATDQRAIDRAMIELDGTPNKSRLGANAILGVSLAVAKAAAAALGLPLYRYLGGVNAKTLPVPMMNIINGGAHADNNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 160 DVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVAL 239
Cdd:COG0148 161 DIQEFMIMPVGAPSFSEALRMGAEVFHALKKVLKEKGLSTAVGDEGGFAPNLKS-NEEALELILEAIEKAGYKPGEDIAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 240 ALDVAATEFYTAGQgYKF--EGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTN 317
Cdd:COG0148 240 ALDVAASEFYKDGK-YHLkgEGKELTSEEMIDYYADLVDKYPIVSIEDGLAEDDWDGWKLLTEKLGDKVQLVGDDLFVTN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 318 PERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERV 397
Cdd:COG0148 319 PKRLKKGIEEGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSPSRSERV 398
|
410 420
....*....|....*....|....*...
gi 518772133 398 AKYNQLLRIEDALGDSARYAGDVAFPRF 425
Cdd:COG0148 399 AKYNQLLRIEEELGDAARYAGRSAFKRL 426
|
|
| eno |
PRK00077 |
enolase; Provisional |
1-426 |
0e+00 |
|
enolase; Provisional
Pssm-ID: 234617 [Multi-domain] Cd Length: 425 Bit Score: 826.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVI 79
Cdd:PRK00077 1 MSKIEDIIAREILDSRGNPTVEVEVTLEDGAFGRAAVPSGASTGEREAVELRDGDkSRYLGKGVLKAVENVNEEIAPALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 80 GLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSV 159
Cdd:PRK00077 81 GLDALDQRAIDKAMIELDGTPNKSKLGANAILGVSLAVAKAAADSLGLPLYRYLGGPNAKVLPVPMMNIINGGAHADNNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 160 DVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVAL 239
Cdd:PRK00077 161 DIQEFMIMPVGAPSFKEALRMGAEVFHTLKKVLKEKGLSTAVGDEGGFAPNLKS-NEEALDLILEAIEKAGYKPGEDIAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 240 ALDVAATEFYTAGQgYKFEGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPE 319
Cdd:PRK00077 240 ALDCAASEFYKDGK-YVLEGEGLTSEEMIDYLAELVDKYPIVSIEDGLDENDWEGWKLLTEKLGDKVQLVGDDLFVTNTK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 320 RLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAK 399
Cdd:PRK00077 319 RLKKGIEKGAANSILIKVNQIGTLTETLDAIELAKRAGYTAVVSHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAK 398
|
410 420
....*....|....*....|....*..
gi 518772133 400 YNQLLRIEDALGDSARYAGDVAFPRFS 426
Cdd:PRK00077 399 YNQLLRIEEELGDAARYAGKKAFKNLK 425
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
7-408 |
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: 720.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 7 VGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGGD-RYGGKGVQKAVEGVLDEIAPAVIGLDAVE 85
Cdd:cd03313 2 IKAREILDSRGNPTVEVEVTTEDGGVGRAAVPSGASTGEHEAVELRDGDKsRYLGKGVLKAVKNVNEIIAPALIGMDVTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 86 QRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSVDVQEFM 165
Cdd:cd03313 82 QRAIDKLLIELDGTPNKSKLGANAILGVSLAVAKAAAAALGLPLYRYLGGLAAYVLPVPMFNVINGGAHAGNKLDFQEFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 166 IAPIGAPTFKEALRWGAEVYHALKSELKSKG--LATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVALALDV 243
Cdd:cd03313 162 IVPVGAPSFSEALRMGAEVYHTLKKVLKKKGglLATNVGDEGGFAPNLSS-NEEALDLLVEAIEKAGYEPGKKIAIALDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 244 AATEFYTAGQGY--KFEGSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPERL 321
Cdd:cd03313 241 AASEFYDEGKYVydSDEGKKLTSEELIDYYKELVKKYPIVSIEDPFDEDDWEGWAKLTAKLGDKIQIVGDDLFVTNPERL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 322 EDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAKYN 401
Cdd:cd03313 321 KKGIEKKAANALLIKVNQIGTLTETIEAIKLAKKNGYGVVVSHRSGETEDTFIADLAVALGAGQIKTGAPCRSERTAKYN 400
|
....*..
gi 518772133 402 QLLRIED 408
Cdd:cd03313 401 QLLRIEE 407
|
|
| eno |
TIGR01060 |
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis ... |
4-425 |
0e+00 |
|
phosphopyruvate hydratase; Alternate name: enolase [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 213580 [Multi-domain] Cd Length: 425 Bit Score: 712.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 4 IEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVIGLD 82
Cdd:TIGR01060 1 IVDIRAREILDSRGNPTVEVEVILEDGTFGRAAVPSGASTGEREALELRDGDkKRYLGKGVLKAVENVNEIIAPELIGMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 83 AVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNGGAHADTSVDVQ 162
Cdd:TIGR01060 81 ATDQREIDQILIELDGTPNKSKLGANAILGVSMAVAKAAADSLGLPLYRYLGGFNAYVLPVPMMNIINGGAHADNNLDFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 163 EFMIAPIGAPTFKEALRWGAEVYHALKSELKSKGLATGLGDEGGFAPDLAGgTREALDLIAAAVAKTGYRLGTDVALALD 242
Cdd:TIGR01060 161 EFMIMPVGAPSFREALRMGAEVFHALKKLLKEKGLATGVGDEGGFAPNLAS-NEEALEIIVEAIEKAGYKPGEDVALALD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 243 VAATEFYTAGQG-YKFEGSVR--SADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPE 319
Cdd:TIGR01060 240 CAASEFYDEEDGkYVYKGENKqlTSEEMIEYYEELVEKYPIISIEDGLSEEDWEGWAELTKRLGDKVQIVGDDLFVTNTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 320 RLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAK 399
Cdd:TIGR01060 320 ILREGIEMGVANSILIKPNQIGTLTETLDAIELAKKAGYTAVISHRSGETEDTTIADLAVATNAGQIKTGSLSRSERIAK 399
|
410 420
....*....|....*....|....*.
gi 518772133 400 YNQLLRIEDALGDSARYAGDVAFPRF 425
Cdd:TIGR01060 400 YNQLLRIEEELGDSARYAGKNSFYRF 425
|
|
| PTZ00081 |
PTZ00081 |
enolase; Provisional |
1-418 |
0e+00 |
|
enolase; Provisional
Pssm-ID: 240259 [Multi-domain] Cd Length: 439 Bit Score: 581.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGtLTRAAVPSGASTGEHEAVELRDGG-DRYGGKGVQKAVEGVLDEIAPAVI 79
Cdd:PTZ00081 1 MSTIKSIKAREILDSRGNPTVEVDLTTEKG-VFRAAVPSGASTGIYEALELRDGDkSRYLGKGVLKAVENVNEIIAPALI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 80 GLDAVEQRTVDQVLLD-LDGTPD-----KSRLGANALLGVSLAVARAAAESSGLELFRYL----GGPNAH-VLPVPMMNI 148
Cdd:PTZ00081 80 GKDVTDQKKLDKLMVEqLDGTKNewgwcKSKLGANAILAVSMAVARAAAAAKGVPLYKYLaqlaGKPTDKfVLPVPCFNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 149 LNGGAHADTSVDVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSK-GL-ATGLGDEGGFAPDLAGgTREALDLIAAAV 226
Cdd:PTZ00081 160 INGGKHAGNKLAFQEFMIAPVGAPSFKEALRMGAEVYHSLKSVIKKKyGLdATNVGDEGGFAPNIKD-PEEALDLLVEAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 227 AKTGYRlgTDVALALDVAATEFYTA-GQGY-------KFEGS-VRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVS 297
Cdd:PTZ00081 239 KKAGYE--GKVKICMDVAASEFYDKeKKVYdldfknpNNDKSnKLTGEELVELYLDLVKKYPIVSIEDPFDQDDWEAYAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 298 LTDQIGEKVQLVGDDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADL 377
Cdd:PTZ00081 317 LTAAIGQKVQIVGDDLLVTNPTRIKKAIEKKACNALLLKVNQIGTVTEAIEAAKLAQKNGWGVMVSHRSGETEDTFIADL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 518772133 378 AVAVGSGQIKTGAPARSERVAKYNQLLRIEDALGDSARYAG 418
Cdd:PTZ00081 397 VVGLGTGQIKTGAPCRSERLAKYNQLLRIEEELGSNAVYAG 437
|
|
| PLN00191 |
PLN00191 |
enolase |
1-418 |
0e+00 |
|
enolase
Pssm-ID: 215095 [Multi-domain] Cd Length: 457 Bit Score: 562.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGTLtRAAVPSGASTGEHEAVELRDGGDRYGGKGVQKAVEGVLDEIAPAVIG 80
Cdd:PLN00191 25 MATITKVKARQIIDSRGNPTVEVDLHTSKGMF-RAAVPSGASTGIYEALELRDGDKDYLGKGVLKAVKNVNEIIAPALIG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 81 LDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRY---LGGPNAHVLPVPMMNILNGGAHADT 157
Cdd:PLN00191 104 MDPTDQTQIDNFMLELDGTPNKGKLGANAILAVSLAVCKAGAAEKGVPLYKHiadLAGNKKLVLPVPAFNVINGGSHAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 158 SVDVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSK--GLATGLGDEGGFAPDLaGGTREALDLIAAAVAKTGYrlgT 235
Cdd:PLN00191 184 KLAMQEFMILPVGASSFKEAMQMGSEVYHHLKAVIKKKygQDACNVGDEGGFAPNI-QDNKEGLELLKEAIEKAGY---T 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 236 D-VALALDVAATEFYTAGQGYKFE--------GSVRSADEMAKFYAELLTGYPLVSIEDPLAEDDWDGWVSLTDQigEKV 306
Cdd:PLN00191 260 GkIKIGMDVAASEFYTKDKKYDLDfkeenndgSNKKSGDELIDLYKEFVSDYPIVSIEDPFDQDDWEHWAKLTSL--EDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 307 QLVGDDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRSGETEDTTIADLAVAVGSGQI 386
Cdd:PLN00191 338 QIVGDDLLVTNPKRVAKAIQEKACNALLLKVNQIGTVTESIEAVKMSKAAGWGVMTSHRSGETEDSFIADLAVGLATGQI 417
|
410 420 430
....*....|....*....|....*....|..
gi 518772133 387 KTGAPARSERVAKYNQLLRIEDALGDSARYAG 418
Cdd:PLN00191 418 KTGAPCRSERLAKYNQLLRIEEELGDEAVYAG 449
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
138-418 |
4.23e-151 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 430.36 E-value: 4.23e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 138 AHVLPVPMMNILNGGAHADTSVDVQEFMIAPIGAPTFKEALRWGAEVYHALKSELKSKG--LATGLGDEGGFAPDLaGGT 215
Cdd:pfam00113 1 SYVLPVPMMNVINGGSHAGNNLAFQEFMILPTGAPSFSEAMRMGAEVYHHLKSVLKAKYgqSATNVGDEGGFAPNL-QSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 216 REALDLIAAAVAKTGYRLgtDVALALDVAATEFYTAGQG---YKFEGS------VRSADEMAKFYAELLTGYPLVSIEDP 286
Cdd:pfam00113 80 KEALDLIVEAIEKAGYKG--KIKIAMDVASSEFYNKKDGkydLDFKGEksdkskKLTSAQLADLYEELVKKYPIVSIEDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 287 LAEDDWDGWVSLTDQIGEKVQLVGDDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMSHRS 366
Cdd:pfam00113 158 FDEDDWEAWKYLTERLGDKVQIVGDDLTVTNPKRLKTAIEKKIANALLLKVNQIGSLTESIAAVKMAKDAGWGVMVSHRS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518772133 367 GETEDTTIADLAVAVGSGQIKTGAPARSERVAKYNQLLRIEDALGDSARYAG 418
Cdd:pfam00113 238 GETEDTTIADLAVGLNAGQIKTGAPCRSERLAKYNQLLRIEEELGSEAKYAG 289
|
|
| Enolase_N |
pfam03952 |
Enolase, N-terminal domain; |
4-133 |
2.58e-78 |
|
Enolase, N-terminal domain;
Pssm-ID: 461105 [Multi-domain] Cd Length: 131 Bit Score: 238.43 E-value: 2.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 4 IEQVGAREILDSRGNPTVEVEIALDDGTLTRAAVPSGASTGEHEAVELRDG-GDRYGGKGVQKAVEGVLDEIAPAVIGLD 82
Cdd:pfam03952 1 ITKVKAREILDSRGNPTVEVEVTLEDGTFGRAAVPSGASTGEHEAVELRDGdKSRYGGKGVLKAVENVNEIIAPALIGMD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 518772133 83 AVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYL 133
Cdd:pfam03952 81 ATDQRAIDRALIELDGTENKSKLGANAILGVSLAVAKAAAAALGLPLYRYL 131
|
|
| PRK08350 |
PRK08350 |
hypothetical protein; Provisional |
1-151 |
3.70e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 169397 [Multi-domain] Cd Length: 341 Bit Score: 85.24 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 1 MAIIEQVGAREILDSRGNPTVEVEIALDDGtLTRAAVPSGASTGEHEAVELRdggdryggkgvqkAVEGVLDEIAPAVIG 80
Cdd:PRK08350 1 MTVIENIIGRVAVLRGGKYSVEVDVITDSG-FGRFAAPIDENPSLYIAEAHR-------------AVSEVDEIIGPELIG 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518772133 81 LDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVPMMNILNG 151
Cdd:PRK08350 67 FDASEQELIDSYLWEIDGTEDFSHIGANTALAVSVAVAKAAANSKNMPLYSYIGGTFTTELPVPILEFAED 137
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
212-386 |
1.33e-15 |
|
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: 75.83 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 212 AGGTREALDLIAAAVaktgyrlGTDVALALDVAATEFYTAGQGYkfegsvrsademakfyAELLTGYPLVSIEDPLAEDD 291
Cdd:cd00308 77 AYGSIERVRAVREAF-------GPDARLAVDANGAWTPKEAIRL----------------IRALEKYGLAWIEEPCAPDD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 292 WDGWVSLTDQIGekVQLVGDDLFVTNPERLEdGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGyKTMMSHRSGETED 371
Cdd:cd00308 134 LEGYAALRRRTG--IPIAADESVTTVDDALE-ALELGAVDILQIKPTRVGGLTESRRAADLAEAFG-IRVMVHGTLESSI 209
|
170
....*....|....*
gi 518772133 372 TTIADLAVAVGSGQI 386
Cdd:cd00308 210 GTAAALHLAAALPND 224
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
21-362 |
1.41e-09 |
|
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: 59.45 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 21 VEVEIALDDGTLTRAAVPSGASTGEHEA--VELRDGGDRYG-------GKGVQKAVEGVLDEIAPAVIGLDAveqRTVDQ 91
Cdd:COG4948 4 TDIEVYPVRLPLKRPFTISRGTRTERDVvlVRVETDDGITGwgeavpgGTGAEAVAAALEEALAPLLIGRDP---LDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 92 VLLDLDgtpDKSRLGANALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPVpmmnilnGGAHADTSVDVqefMIApiga 171
Cdd:COG4948 81 LWQRLY---RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPV-------YATLGIDTPEE---MAE---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 172 ptfkEALRWGAEVYHALKseLKSkglatglgdeGGFAPDlaggtrEALDLIAAAVAktgyRLGTDVALALDvaatefytA 251
Cdd:COG4948 144 ----EAREAVARGFRALK--LKV----------GGPDPE------EDVERVRAVRE----AVGPDARLRVD--------A 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 252 GQGYKFEGSVRSADEMAKfyaelltgYPLVSIEDPLAEDDWDGWVSLTDQIGekVQLVGDDLfVTNPERLEDGIAKGAAN 331
Cdd:COG4948 190 NGAWTLEEAIRLLRALED--------LGLEWIEQPLPAEDLEGLAELRRATP--VPIAADES-LTSRADFRRLIEAGAVD 258
|
330 340 350
....*....|....*....|....*....|.
gi 518772133 332 ALLVKVNQIGTLTETLDAVELAHRNGYKTMM 362
Cdd:COG4948 259 IVNIKLSKVGGLTEALRIAALAEAHGVPVMP 289
|
|
| PTZ00378 |
PTZ00378 |
hypothetical protein; Provisional |
50-410 |
3.27e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 173571 [Multi-domain] Cd Length: 518 Bit Score: 49.10 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 50 ELRDGGDRYGGKGVQKAVEGVLDEIAPAVIGLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAAESSGLEL 129
Cdd:PTZ00378 91 GERDGEADATLDPAEYTTEALQNSYFPRLLQLGARDQREFDSTLRAALSTSPLANVGSAVQWALSIVASLAAARCRSVPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 130 FRYLGG-----PNAHVLPVPMMNI--LNGGAHADTSVDVQEFMIAPI---GAPTFKEALRWGAEVYHALKSElkskglAT 199
Cdd:PTZ00378 171 FQYLRAlfgslTSVETFSMPQLCItfFGPGNPSTARLALKSVLFSPVmpsGTVLRERMQKIFAAFHHFCQSH------NS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 200 GLGDEGGFAPDLAGGTREALDLIAAAVAKTGYRLGTDVALALDVAATEFYTAGQGYKFEGSVRSA--------------- 264
Cdd:PTZ00378 245 SVRSDGSLHWDGFANLTDAVKLATEALRAVQLTPGTDVCLGLRMAASTTRVPATAVADGGAWKEAkddcevlyslfpgep 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 265 ----DEMAKFYAELLTGYP--LVSIEDPLAEDDWDGWVSLTDQIGEKVQLVGDDLFV-TNPERLEDGIAKGAANALLVKV 337
Cdd:PTZ00378 325 dvtgDQLSEYVREQLQAVPdiVVYVEDTHCDEDTFGLQRLQAALGDSIVLSGVDVYArSEYKKVESGLRGLWTSNIVLNP 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518772133 338 NQIGTLTETLDAVELAHRNGYKTM-MSHRSGETEDTTIADLAVAVGSGQIKTGAPARSERVAKYNQLLRIEDAL 410
Cdd:PTZ00378 405 CAIGTLSDVVEIVRAVGEDEGRAVtVLVQTLAGNAATAAHLAVAMGARFLCSGGLFSAHQCEVVSQLASRQDEL 478
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
212-380 |
1.06e-05 |
|
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: 46.40 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 212 AGGTREALDLIAAAVAktgyRLGTDVALALDvaatefytAGQGYkfegSVrsadEMAKFYAELLTGYPLVSIEDPLAEDD 291
Cdd:pfam13378 24 GPDPEEDVERVRAVRE----AVGPGVDLMVD--------ANGAW----SV----AEAIRLARALEELGLLWIEEPVPPDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 292 WDGWVSLTDQIGEKVQLvgdDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYkTMMSHrSGETED 371
Cdd:pfam13378 84 LEGLARLRRATPVPIAT---GESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGV-PVAPH-SGGGPI 158
|
....*....
gi 518772133 372 TTIADLAVA 380
Cdd:pfam13378 159 GLAASLHLA 167
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
49-364 |
5.73e-05 |
|
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: 44.91 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 49 VELRDGGDRYG-----GKGVQKAVEGVL-DEIAPAVIGLDAVEQRTVDQVLLDLDGTPDKSRLGANALLGVSLAVARAAA 122
Cdd:cd03316 29 VRVTTDDGITGwgeayPGGRPSAVAAAIeDLLAPLLIGRDPLDIERLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 123 ESSGLELFRYLGGPNAHVLPVpmmnILNGGAHADTSVDVQEFMiapigaptfKEALRWGaevYHALKseLKskglatglg 202
Cdd:cd03316 109 KAAGVPVYKLLGGKVRDRVRV----YASGGGYDDSPEELAEEA---------KRAVAEG---FTAVK--LK--------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 203 deGGFAPDLAGGTREALDLIAAaVAKTgyrLGTDVALALDvaatefytAGQGYkfegSVRSADEMAKfyaeLLTGYPLVS 282
Cdd:cd03316 162 --VGGPDSGGEDLREDLARVRA-VREA---VGPDVDLMVD--------ANGRW----DLAEAIRLAR----ALEEYDLFW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 283 IEDPLAEDDWDGWVSLTDQIGEKVQlVGDDLFvtNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGyKTMM 362
Cdd:cd03316 220 FEEPVPPDDLEGLARLRQATSVPIA-AGENLY--TRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHG-VRVA 295
|
..
gi 518772133 363 SH 364
Cdd:cd03316 296 PH 297
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
214-363 |
1.01e-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: 43.87 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 214 GTREALDLiaAAVAKTGYRLGTDVALALDvaatefytAGQGYKFEGSVRSADEMakfyaellTGYPLVSIEDPLAEDDWD 293
Cdd:cd03315 109 GRDPARDV--AVVAALREAVGDDAELRVD--------ANRGWTPKQAIRALRAL--------EDLGLDYVEQPLPADDLE 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 294 GWVSLTDQIGekVQLVGDDLfVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNGYKTMMS 363
Cdd:cd03315 171 GRAALARATD--TPIMADES-AFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVG 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 ... |
19-362 |
4.28e-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: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 19 PTVEVEIALDDGTLTRAAVPSGASTGEheavelrdggdryggkgVQKAVEGVLDEIAPAVIGLDAVEQRTVDQVLldldg 98
Cdd:cd03319 26 ENVIVEIELDGITGYGEAAPTPRVTGE-----------------TVESVLAALKSVRPALIGGDPRLEKLLEALQ----- 83
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 99 tpdkSRLGAN--ALLGVSLAVARAAAESSGLELFRYLGGPNAHVLPvpmmnilnggahadTSVDVqefmiaPIGAP--TF 174
Cdd:cd03319 84 ----ELLPGNgaARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLE--------------TDYTI------SIDTPeaMA 139
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 175 KEALRWGAEVYHALKseLKskglatglgdeggfapdLAGGTREALDLIAAAVAKTGyrlgtDVALALDvaatefytAGQG 254
Cdd:cd03319 140 AAAKKAAKRGFPLLK--IK-----------------LGGDLEDDIERIRAIREAAP-----DARLRVD--------ANQG 187
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 255 YKFEGSVRSADEMAKfyaelltgYPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLvgdDLFVTNPERLEDGIAKGAANALL 334
Cdd:cd03319 188 WTPEEAVELLRELAE--------LGVELIEQPVPAGDDDGLAYLRDKSPLPIMA---DESCFSAADAARLAGGGAYDGIN 256
|
330 340
....*....|....*....|....*...
gi 518772133 335 VKVNQIGTLTETLDAVELAHRNGYKTMM 362
Cdd:cd03319 257 IKLMKTGGLTEALRIADLARAAGLKVMV 284
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| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
278-357 |
1.51e-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: 40.30 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518772133 278 YPLVSIEDPLAEDDWDGWVSLTDQIGEKVQLvgdDLFVTNPERLEDGIAKGAANALLVKVNQIGTLTETLDAVELAHRNG 357
Cdd:cd03317 203 YGLLMIEQPLAADDLIDHAELQKLLKTPICL---DESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHG 279
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