|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-368 |
8.27e-90 |
|
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: 274.39 E-value: 8.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 1 MIIKKVDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGEGIPrrfvTGEILAESLAFLKKVLIPEICRLPLL 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVP----GGTGAEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 81 FRPSIYANLARVGQQLGAAnypaiWCAVEMAWLDAASKTCGQPLAEILGFQSQRAAIYSAVLPMASEQQMARFFELVKLK 160
Cdd:COG4948 77 DIEALWQRLYRALPGNPAA-----KAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 161 KMRFLKLKVGTS---TDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAA 237
Cdd:COG4948 152 GFRALKLKVGGPdpeEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 238 VAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFALTTD 317
Cdd:COG4948 232 TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCML-ESGIGLAAALHLAAALP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1162405749 318 HLAYVEGSfAPYLLAKDVVRQPVFFENGGLarALP-GPGLGIQVEDHILEEL 368
Cdd:COG4948 311 NFDIVELD-GPLLLADDLVEDPLRIEDGYL--TVPdGPGLGVELDEDALARY 359
|
|
| 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 ... |
5-314 |
5.04e-73 |
|
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: 229.77 E-value: 5.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 5 KVDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDaGVTGYGEGIPRRFVTGEILAESLAFLKKVlIPEICRLPLLFRps 84
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKSV-RPALIGGDPRLE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 85 iyANLARVGQQLGAAnyPAIWCAVEMAWLDAASKTCGQPLAEILGFQSQRAAIYSAVLPMASEQQMARffELVKLKKMRF 164
Cdd:cd03319 77 --KLLEALQELLPGN--GAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAA--AAKKAAKRGF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 165 --LKLKVGTS--TDPELLKSVRQQLGwEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAI 240
Cdd:cd03319 151 plLKIKLGGDleDDIERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162405749 241 PIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFAL 314
Cdd:cd03319 230 PIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMV-ESSLSIAAAAHLAA 302
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
3-364 |
1.11e-59 |
|
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: 197.15 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 3 IKKVDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGEGIP--RRFVTGEILAESLAFLKKVLIPEICRLPLL 80
Cdd:cd03318 2 IEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTpgGPAWGGESPETIKAIIDRYLAPLLIGRDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 81 FRPSIYANLARvgqqLGAANYPAIwCAVEMAWLDAASKTCGQPLAEILGfQSQRAAIySAVLPMAS---EQQMARFFELV 157
Cdd:cd03318 82 NIGAAMALLDR----AVAGNLFAK-AAIEMALLDAQGRRLGLPVSELLG-GRVRDSL-PVAWTLASgdtERDIAEAEEML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 158 KLKKMRFLKLKVGTS---TDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRV 234
Cdd:cd03318 155 EAGRHRRFKLKMGARppaDDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 235 SAAVAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFAL 314
Cdd:cd03318 235 RSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTML-ESSIGTAASAHLFA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1162405749 315 TTDHLAYVEGSFAPYLLAKDVVRQPVFFENGGLarALP-GPGLGIQV-EDHI 364
Cdd:cd03318 314 TLPSLPFGCELFGPLLLAEDLLEEPLAYRDGEL--HVPtGPGLGVRLdEDKV 363
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
163-360 |
1.06e-52 |
|
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: 174.29 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 163 RFLKLKVGTST---DPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVA 239
Cdd:pfam13378 16 RAFKLKVGGPDpeeDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 240 IPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQlgCHVGETSILAAAGRHFALTTDHL 319
Cdd:pfam13378 96 VPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVA--PHSGGGPIGLAASLHLAAAVPNL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1162405749 320 AYVEGSFAPYLLAKDVVRQPVFFENGGLarALP-GPGLGIQV 360
Cdd:pfam13378 174 LIQEYFLDPLLLEDDLLTEPLEVEDGRV--AVPdGPGLGVEL 213
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
3-358 |
7.77e-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: 176.26 E-value: 7.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 3 IKKVDIWHLnlafKAPVKHNLATHYGSENIVVKLTTDAGVTGYGEGiprrfVTGEILAESLAFLKKVLIPEICRLPLLFR 82
Cdd:cd03316 2 ITDVETFVL----RVPLPEPGGAVTWRNLVLVRVTTDDGITGWGEA-----YPGGRPSAVAAAIEDLLAPLLIGRDPLDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 83 PSIYANLARVG--QQLGAANYPAIwCAVEMAWLDAASKTCGQPLAEILG-FQSQRAAIY-SAVLPMASEQQMARffELVK 158
Cdd:cd03316 73 ERLWEKLYRRLfwRGRGGVAMAAI-SAVDIALWDIKGKAAGVPVYKLLGgKVRDRVRVYaSGGGYDDSPEELAE--EAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 159 LKKM--RFLKLKVG--------TSTDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDF 228
Cdd:cd03316 150 AVAEgfTAVKLKVGgpdsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 229 EGLQRVSAAVAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQlgCHVGETSILAAA 308
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVA--PHGAGGPIGLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1162405749 309 GRHFALTTDHLAYVEGSFAPYLLAKDVVRQPVFFENgGLARALPGPGLGI 358
Cdd:cd03316 308 SLHLAAALPNFGILEYHLDDLPLREDLFKNPPEIED-GYVTVPDRPGLGV 356
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
3-368 |
1.74e-47 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 165.35 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 3 IKKVDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGEGI-PRRFVTGEILAESLaflkKVLIPEICRLPLLF 81
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTtIGGLWWGGESPETI----KANIDTYLAPVLVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 82 R--PSIYANLARVGQQLGAANYPAiwCAVEMAWLDAASKTCGQPLAEILG--FQSQRAAIYS-AVLPmaSEQQMARFFEL 156
Cdd:TIGR02534 77 RdaTEIAAIMADLEKVVAGNRFAK--AAVDTALHDAQARRLGVPVSELLGgrVRDSVDVTWTlASGD--TDRDIAEAEER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 157 VKLKKMRFLKLKVGT---STDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQR 233
Cdd:TIGR02534 153 IEEKRHRSFKLKIGArdpADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENREALAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 234 VSAAVAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFA 313
Cdd:TIGR02534 233 LTRRFNVPIMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTML-EGPIGTIASAHFF 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1162405749 314 LTTDHLAYVEGSFAPYLLAKDVVRQPVFFENGGLarALP-GPGLGIQVEDHILEEL 368
Cdd:TIGR02534 312 ATFPALSFGTELFGPLLLKDEILTEPLQYEDFQL--HLPqGPGLGVEVDEDKVNFY 365
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
10-367 |
3.79e-43 |
|
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: 153.16 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 10 HLNLAFKAPVKhnlaTHYGSEN----IVVKLTTDAGVTGYGEG--IPRRFVTGEILAESLAFLKKVLIPEICRLPLLFRP 83
Cdd:cd03317 5 HVRMPLKFPFE----TSFGTLNerefLIVELTDEEGITGYGEVvaFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 84 SIYANLARV-GQQLGAAnypaiwcAVEMAWLDAASKTCGQPLAEILGFQSQRAAIYSAVLPMASEQQMARFFELVKLKKM 162
Cdd:cd03317 81 EVSERLAPIkGNNMAKA-------GLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQLLKQIERYLEEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 163 RFLKLKVGTSTDPELLKSVRQQLGwEIDIRVDANAAWSPpEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPI 242
Cdd:cd03317 154 KRIKLKIKPGWDVEPLKAVRERFP-DIPLMADANSAYTL-ADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 243 IADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFAlTTDHLAYv 322
Cdd:cd03317 232 CLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGML-ESGIGRAHNVALA-SLPNFTY- 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1162405749 323 EGSFAP---YlLAKDVVRQPVFFENgGLARALPGPGLGIQVEDHILEE 367
Cdd:cd03317 309 PGDISAssrY-FEEDIITPPFELEN-GIISVPTGPGIGVTVDREALKK 354
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
107-315 |
5.95e-42 |
|
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: 147.87 E-value: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 107 AVEMAWLDAASKTCGQPLAEILGFQSQRAAIySAVLPMASEQQMARFFELVKLKKMRFLKLKVG--TSTDPELLKSVRQQ 184
Cdd:cd03315 47 AVDMALWDLWGKRLGVPVYLLLGGYRDRVRV-AHMLGLGEPAEVAEEARRALEAGFRTFKLKVGrdPARDVAVVAALREA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 185 LGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDARRLIEMRACQ 264
Cdd:cd03315 126 VGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDAFRELALGAAD 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1162405749 265 IFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAAGRHFALT 315
Cdd:cd03315 206 AVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMI-ESGLGTLANAHLAAA 255
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-316 |
1.29e-35 |
|
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: 129.75 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 6 VDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGEGIprrfvtgeilaeslaflkkvlipeicrlpllfrpsi 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEVI------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 86 yanlarvgqqlgaanypaiwCAVEMAWLDAASKTCGQPLAEILGfqsqrAAIYSAVLPMASEqqmarffelvklkkmrfl 165
Cdd:cd00308 45 --------------------SGIDMALWDLAAKALGVPLAELLG-----GGSRDRVPAYGSI------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 166 klkvgtstdpELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIAD 245
Cdd:cd00308 82 ----------ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAAD 151
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162405749 246 ESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGChVGETSILAAAGRHFALTT 316
Cdd:cd00308 152 ESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHG-TLESSIGTAAALHLAAAL 221
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-340 |
5.52e-33 |
|
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: 125.34 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 9 WHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGE--GIPRRFVTGEILAESLAFLKKVLIPEIcrLPLLFRPSIY 86
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEvvAFQTPWYTHETIATVKHIIEDFFEPNI--NKEFEHPSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 87 ANLARvgqqlGAANYPAIWCAVEMAWLDAASKTCGQPLAEILGfQSQRAAIYSAVLPMASEQQMARffELVKLKKMRF-- 164
Cdd:TIGR01928 79 LELVR-----SLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQG-KLRDKAPAGAVSGLANDEQMLK--QIESLKATGYkr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 165 LKLKVGTSTDPELLKSVRQQLGwEIDIRVDANAAWSPPEaMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIA 244
Cdd:TIGR01928 151 IKLKITPQIMHQLVKLRRLRFP-QIPLVIDANESYDLQD-FPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 245 DESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVgETSILAAagRHFALTTDHLAYVEG 324
Cdd:TIGR01928 229 DESITSLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGML-ETGISRA--FNVALASLGGNDYPG 305
|
330
....*....|....*...
gi 1162405749 325 SFAP--YLLAKDVVRQPV 340
Cdd:TIGR01928 306 DVSPsgYYFDQDIVAPSI 323
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
5-313 |
3.87e-27 |
|
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: 108.12 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 5 KVDIWHLNLAFKAPVKHNLATHYgsENIVVKLTTDAGVTGYGEgiprrfvtgeilaeslaflkkvlipeICRLPLLFrps 84
Cdd:cd03320 2 RLYPYSLPLSRPLGTSRGRLTRR--RGLLLRLEDLTGPVGWGE--------------------------IAPLPLAF--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 85 iyanlarvgqqlgaanypaiwcAVEMAWLDaasktcgqPLAEILGFQSQRAAIY-SAVLPMASEQQMARffelVKLKKM- 162
Cdd:cd03320 51 ----------------------GIESALAN--------LEALLVGFTRPRNRIPvNALLPAGDAAALGE----AKAAYGg 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 163 --RFLKLKVGTS---TDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRvsAA 237
Cdd:cd03320 97 gyRTVKLKVGATsfeEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRR--LA 174
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162405749 238 VAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGChVGETSILAAAGRHFA 313
Cdd:cd03320 175 AGVPIALDESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSS-ALESSIGLGALAHLA 249
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
34-360 |
5.16e-24 |
|
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: 101.25 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 34 VKLTTDAGVTGYGEGIprrfVTG--EILAESLAFLKKVLIPEICRL-----PLLFRPSIYanlaRVGQQLGAAnypaiWC 106
Cdd:cd03325 17 VKIETDEGVVGWGEPT----VEGkaRTVEAAVQELEDYLIGKDPMNiehhwQVMYRGGFY----RGGPVLMSA-----IS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 107 AVEMAWLDAASKTCGQPLAEILGFQS-QRAAIYS----------AVLPMASEQQMARFFELVKLKKMRFLKLKVGTSTDP 175
Cdd:cd03325 84 GIDQALWDIKGKVLGVPVHQLLGGQVrDRVRVYSwiggdrpsdvAEAARARREAGFTAVKMNATEELQWIDTSKKVDAAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 176 ELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDAR 255
Cdd:cd03325 164 ERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 256 RLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKcqLGCHVGETSILAAAGRHFALTTDHLAYVEGS-FAPYLLAKD 334
Cdd:cd03325 244 ELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVA--LAPHCPLGPIALAASLHVDASTPNFLIQEQSlGIHYNEGDD 321
|
330 340 350
....*....|....*....|....*....|
gi 1162405749 335 V----VRQPVFFENGGLARALPGPGLGIQV 360
Cdd:cd03325 322 LldylVDPEVFDMENGYVKLPTGPGLGIEI 351
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
3-356 |
1.10e-20 |
|
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: 92.16 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 3 IKKVDIWHLNLAFKAPVKHNLATHYGSENIVVKLTTDAGVTGYGegipRRFVTGEILAESLAFLKKVLIPEICRLPLLFR 82
Cdd:cd03321 3 ITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHS----YLFTYTPAALKSLKQLLDDMAALLVGEPLAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 83 pSIYANLARVGQQLGAANYPAIWCA-VEMAWLDAASKTCGQPLAEILGFQSQRAAIYSAVLPMASEQQMARFFELVKLKk 161
Cdd:cd03321 79 -ELERALAKRFRLLGYTGLVRMAAAgIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATERAVTAAEEG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 162 MRFLKLKVGTST---DPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAV 238
Cdd:cd03321 157 FHAVKTKIGYPTadeDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 239 AIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIkcQLGCHV-GETS--ILAAAgrhfalT 315
Cdd:cd03321 237 RTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGI--PMSSHLfQEISahLLAVT------P 308
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1162405749 316 TDH-LAYVEgsfapylLAKDVVRQPVFFENG-GLARALPGPGL 356
Cdd:cd03321 309 TAHwLEYVD-------WAGAILEPPLKFEDGnAVIPDEPGNGI 344
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
34-366 |
5.97e-19 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 87.26 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 34 VKLTTDAGVTGYGEGIprrfVTG---------EILAESLaflkkvlipeICRLPL--------LFRPSIYanlaRVGQQL 96
Cdd:PRK14017 18 LKIETDEGIVGWGEPV----VEGrartveaavHELADYL----------IGKDPRriedhwqvMYRGGFY----RGGPIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 97 GAAnypaiWCAVEMAWLDAASKTCGQPLAEILGFQSQ-RAAIYSAV-------LPMASEQQMARFFELVKL---KKMRFL 165
Cdd:PRK14017 80 MSA-----IAGIDQALWDIKGKALGVPVHELLGGLVRdRIRVYSWIggdrpadVAEAARARVERGFTAVKMngtEELQYI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 166 KLKVGTSTDPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIAD 245
Cdd:PRK14017 155 DSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 246 ESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVGETSiLAAA----------------- 308
Cdd:PRK14017 235 ERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIA-LAAClqvdavspnafiqeqsl 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1162405749 309 GRHFALTTDHLAYVEGsfapyllaKDVVRqpvfFENGGLARaLPGPGLGIQV-EDHILE 366
Cdd:PRK14017 314 GIHYNQGADLLDYVKN--------KEVFA----YEDGFVAI-PTGPGLGIEIdEAKVRE 359
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
32-291 |
8.41e-19 |
|
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: 86.23 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 32 IVVKLTTDAGVTGYGEGIPRRFVTGEILAESLAFLKKVLIPEICRL-PLLFRPSIYAnlARVGQQLGAANypaiwcAVEM 110
Cdd:cd03327 12 LFVEIETDDGTVGYANTTGGPVACWIVDQHLARFLIGKDPSDIEKLwDQMYRATLAY--GRKGIAMAAIS------AVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 111 AWLDAASKTCGQPLAEILGfQSQRAAI---YSAVLPMASEQQMARFFELVKL----KKMRFL----KLKVGTSTDPELLK 179
Cdd:cd03327 84 ALWDLLGKIRGEPVYKLLG-GRTRDKIpayASGLYPTDLDELPDEAKEYLKEgyrgMKMRFGygpsDGHAGLRKNVELVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 180 SVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDARRLIE 259
Cdd:cd03327 163 AIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLE 242
|
250 260 270
....*....|....*....|....*....|..
gi 1162405749 260 MRACQIFNLRLSKCGGLLSTMRIKKMAEKAGI 291
Cdd:cd03327 243 GRAVDILQPDVNWVGGITELKKIAALAEAYGV 274
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
163-240 |
6.18e-18 |
|
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: 78.09 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 163 RFLKLKVGTST--DPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAI 240
Cdd:smart00922 18 RAVKVKVGGGPleDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
107-360 |
3.30e-17 |
|
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: 81.69 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 107 AVEMAWLDAASKTCGQPLAEILGFQSQRAAIY-----SAVLPMASEQQMARFFELvklkKMRFLKLKVGTS--TDPELLK 179
Cdd:cd03328 98 AVDIALWDLKARLLGLPLARLLGRAHDSVPVYgsggfTSYDDDRLREQLSGWVAQ----GIPRVKMKIGRDprRDPDRVA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 180 SVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQ--RVSAAVAIPIIADESVCTEEDARRL 257
Cdd:cd03328 174 AARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRlvRERGPAGMDIAAGEYAYTLAYFRRL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 258 IEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGChvgetsiLAAAGRHFALTTDHLAYVEGSFapyllakDVVR 337
Cdd:cd03328 254 LEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHC-------APALHAHVACAVPRLRHLEWFH-------DHVR 319
|
250 260 270
....*....|....*....|....*....|
gi 1162405749 338 -QPVFFE------NGGLARALPGPGLGIQV 360
Cdd:cd03328 320 iERMLFDgapdpsGGALRPDLSRPGLGLEL 349
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
32-362 |
3.70e-17 |
|
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: 81.72 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 32 IVVKLTTDAGVTGYGEGIprrfVTGEILAESlAFLKKVLIPE-ICRLP--------LLFRPSIYANlarvgqqlGAANYP 102
Cdd:cd03322 17 VTLKITTDQGVTGLGDAT----LNGRELAVK-AYLREHLKPLlIGRDAnriediwqYLYRGAYWRR--------GPVTMN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 103 AIwCAVEMAWLDAASKTCGQPLAEILGFQSQRAAiysAVLPMASEQQMARFFELVK-LKKMRFLKLKVGTstdPELLKSV 181
Cdd:cd03322 84 AI-AAVDMALWDIKGKAAGMPLYQLLGGKSRDGI---MVYSHASGRDIPELLEAVErHLAQGYRAIRVQL---PKLFEAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 182 RQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDARRLIEMR 261
Cdd:cd03322 157 REKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 262 ACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKcqLGCHvGETS---ILAAAGRHFALTTDHLAYVEGS-FAPYLLAkdVVR 337
Cdd:cd03322 237 LIDYIRTTVSHAGGITPARKIADLASLYGVR--TGWH-GPTDlspVGMAAALHLDLWVPNFGIQEYMrHAEETLE--VFP 311
|
330 340
....*....|....*....|....*..
gi 1162405749 338 QPVFFENGGLaraLPG--PGLGIQVED 362
Cdd:cd03322 312 HSVRFEDGYL---HPGeePGLGVEIDE 335
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
15-274 |
1.83e-15 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 76.21 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 15 FKAPVKHNLATHYG----SENIVVKLTTDAGVTGYGEGIPRRFVTGEILAESLAFlkkvlipeiCR-LPLLFRPSIyanL 89
Cdd:PRK02714 10 YQRPFRQPLQTAHGlwriREGIILRLTDETGKIGWGEIAPLPWFGSETLEEALAF---------CQqLPGEITPEQ---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 90 ARVGQQLgaanyPAIWCAVEMAWLDAAsktcGQPLAEILGFQSqraaiYSAVLPM--ASEQQMARFFElvklKKMRFLKL 167
Cdd:PRK02714 78 FSIPDAL-----PACQFGFESALENES----GSRSNVTLNPLS-----YSALLPAgeAALQQWQTLWQ----QGYRTFKW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 168 KVG---TSTDPELLKSVRQQLGWEIDIRVDANAAWSPPEA---MARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIP 241
Cdd:PRK02714 140 KIGvdpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTP 219
|
250 260 270
....*....|....*....|....*....|....*....
gi 1162405749 242 IIADESVCTeedarrLIEMRACQ------IFNLRLSKCG 274
Cdd:PRK02714 220 IALDESVAN------LAQLQQCYqqgwrgIFVIKPAIAG 252
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
33-357 |
4.37e-14 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 72.81 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 33 VVKLTTDAGVTGYGEGiPRRFVTGEILaesLAFLKKVLIPEicrlPLLFRPSIYANLARvgqQLGAANYPAIwCAVEMAW 112
Cdd:cd03329 36 LLTIETDEGAKGHAFG-GRPVTDPALV---DRFLKKVLIGQ----DPLDRERLWQDLWR---LQRGLTDRGL-GLVDIAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 113 LDAASKTCGQPLAEILGFQSQRAAIY------SAVLPMASEQQMARFFELVKLKKMRFLKLKV----GTSTDPELLKSVR 182
Cdd:cd03329 104 WDLAGKYLGLPVHRLLGGYREKIPAYastmvgDDLEGLESPEAYADFAEECKALGYRAIKLHPwgpgVVRRDLKACLAVR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 183 QQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDARR-LIEMR 261
Cdd:cd03329 184 EAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGALESRAdWVLAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 262 ACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKCQL-GCHVGETSILAAA--GRHFALTTDHLAYVEGSFAPYLLakdVVRQ 338
Cdd:cd03329 264 ATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELhGNGAANLHVIAAIrnTRYYERGLLHPSQKYDVYAGYLS---VLDD 340
|
330
....*....|....*....
gi 1162405749 339 PVffENGGLARALPGPGLG 357
Cdd:cd03329 341 PV--DSDGFVHVPKGPGLG 357
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
111-376 |
6.43e-13 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 68.84 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 111 AWLDAASKTCGQPLAEILgfqsqRAAI-YSAVLPMASEQQMARFfeLVKLKKMRFLKLKVG-----TSTDPELLKSVRQQ 184
Cdd:PRK02901 58 AWLASAIEAAYGGPPPPV-----RDRVpVNATVPAVDAAQVPEV--LARFPGCRTAKVKVAepgqtLADDVARVNAVRDA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 185 LGWEIDIRVDANAAWSPPEAMARIEAM-APYRLSAVEQPVAKedFEGLQRVSAAVAIPIIADESVCTEEDARRLIEMRAC 263
Cdd:PRK02901 131 LGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT--VEELAELRRRVGVPIAADESIRRAEDPLRVARAGAA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 264 QIFNLRLSKCGGLLSTMRIkkmAEKAGIKCQLGCHVgETSILAAAGRHFALTTDHLAYVEGSFAPYLLAKDVV--RQPVf 341
Cdd:PRK02901 209 DVAVLKVAPLGGVRAALDI---AEQIGLPVVVSSAL-DTSVGIAAGLALAAALPELDHACGLATGGLFEEDVAdpLLPV- 283
|
250 260 270
....*....|....*....|....*....|....*..
gi 1162405749 342 feNGGLA--RALPGPGLgiqvedhiLEELAVSRDTID 376
Cdd:PRK02901 284 --DGFLPvrRVTPDPAR--------LAALAADPDRRQ 310
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
30-253 |
1.09e-11 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 64.83 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 30 ENIVVKLTtDAGVTGYGEGIPRRFVTGEILAESLAFLKKvLIPEICRlpllfrpsiyANLARVGQQLgaanyPAIWCAVE 109
Cdd:TIGR01927 22 EGLIVRLT-DEGRTGWGEIAPLPGFGTETLAEALDFCRA-LIEEITR----------GDIEAIDDQL-----PSVAFGFE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 110 MAwLDAASKTCGQPlaeilgfqsQRAAIYSAVLPMASEQqmARFFELVKLKKMRFLKLKVGT---STDPELLKSVRQQLG 186
Cdd:TIGR01927 85 SA-LIELESGDELP---------PASNYYVALLPAGDPA--LLLLRSAKAEGFRTFKWKVGVgelAREGMLVNLLLEALP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 187 WEIDIRVDANAAWSPPEAMARIEAMAPY---RLSAVEQPVAKEDFegLQRVSAAVAIPIIADESVCTEED 253
Cdd:TIGR01927 153 DKAELRLDANGGLSPDEAQQFLKALDPNlrgRIAFLEEPLPDADE--MSAFSEATGTAIALDESLWELPQ 220
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
32-308 |
2.18e-11 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 64.38 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 32 IVVKLTTDaGVTGYGEGIPR-RFvtGEILAESLAFLKKVLipeicrlpllfrPSIYANLARVG-QQL---GAANYpaiwc 106
Cdd:PRK15129 30 VVVELEEE-GIKGTGECTPYpRY--GESDASVMAQIMSVV------------PQLEKGLTREAlQKLlpaGAARN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 107 AVEMAWLDAASKTCGQPLAEILGFQSQRAAIYSAVLPMASEQQMARFFELVKLKKMRFLKLKVGTSTDPELLKSVRQQLG 186
Cdd:PRK15129 90 AVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISERMVAIRSAVP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 187 wEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAavAIPIIADESVCTEEDARRLI---EMrac 263
Cdd:PRK15129 170 -DATLIVDANESWRAEGLAARCQLLADLGVAMLEQPLPAQDDAALENFIH--PLPICADESCHTRSSLKALKgryEM--- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1162405749 264 qiFNLRLSKCGGLLSTMRIKKMAEKAGIKCQLGCHVGETSILAAA 308
Cdd:PRK15129 244 --VNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAA 286
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
32-369 |
3.64e-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: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 32 IVVKLTTDAGVTGYGEgiprrfVTGEilAESLAFLKKVLIPEICRLPLLFRPSIYANL----------ARVGQQLGAANY 101
Cdd:cd03323 31 NIVELTDDNGNTGVGE------SPGG--AEALEALLEAARSLVGGDVFGAYLAVLESVrvafadrdagGRGLQTFDLRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 102 PAIWCAVEMAWLDAASKTCGQPLAEILGfQSQRAAI-YSAVL---------PMASEQQMARFFE------LVKL-KKM-- 162
Cdd:cd03323 103 VHVVTAFEVALLDLLGQALGVPVADLLG-GGQRDSVpFLAYLfykgdrhktDLPYPWFRDRWGEaltpegVVRLaRAAid 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 163 RF----LKLKVGTSTDPELLKSVR--QQLGWEIDIRVDANAAWSPPEAMARIEAMApYRLSAVEQPVAKEdfEGLQRVSA 236
Cdd:cd03323 182 RYgfksFKLKGGVLPGEEEIEAVKalAEAFPGARLRLDPNGAWSLETAIRLAKELE-GVLAYLEDPCGGR--EGMAEFRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 237 AVAIPIIADESVCTEEDARRLIEMRACQIFnlrLSKC---GGLLSTMRIKKMAEKAGIKcqLGCHV-GETSILAAAGRHF 312
Cdd:cd03323 259 ATGLPLATNMIVTDFRQLGHAIQLNAVDIP---LADHhfwGGMRGSVRVAQVCETWGLG--WGMHSnNHLGISLAMMTHV 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1162405749 313 ALTTDHLAYVEGSFAPYLLAKDVVRQPVFFENGGLarALP-GPGLGIQVEDHILEELA 369
Cdd:cd03323 334 AAAAPGLITACDTHWIWQDGQVITGEPLRIKDGKV--AVPdKPGLGVELDRDKLAKAH 389
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
30-248 |
8.44e-11 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 63.72 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 30 ENIVVKLTTDAGVTGYGEGIPRRFVTGEIL--AESLAFLKKVLIPEIC--RLPLL---FRPSIYANLARVGQQLgaanYP 102
Cdd:PLN02980 962 EGFILSLSLEDGSVGFGEVAPLEIHEEDLLdvEEQLRFLLHVIKGAKIsfMLPLLkgsFSSWIWSELGIPPSSI----FP 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 103 AIWCAVEMAWLDAASKTCGQPLAEILGF---------QSQRAAIYSAVLPMASEQQMArfFELVKLKKMRF--LKLKVGT 171
Cdd:PLN02980 1038 SVRCGLEMAILNAIAVRHGSSLLNILDPyqkdengseQSHSVQICALLDSNGSPLEVA--YVARKLVEEGFsaIKLKVGR 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 172 STDP----ELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDfeGLQRVSAAVAIPIIADES 247
Cdd:PLN02980 1116 RVSPiqdaAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDED--DLIKFCEETGLPVALDET 1193
|
.
gi 1162405749 248 V 248
Cdd:PLN02980 1194 I 1194
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
165-291 |
4.43e-09 |
|
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: 57.74 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 165 LKLKVGTST--DPELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVA-IP 241
Cdd:cd03324 215 FKLKVGADLedDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALApLP 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1162405749 242 IiadeSVCTEEDA------RRLIEMRA---CQIFNLRLskcGGLLSTMRIKKMAEKAGI 291
Cdd:cd03324 295 I----GVATGEHCqnrvvfKQLLQAGAidvVQIDSCRL---GGVNENLAVLLMAAKFGV 346
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
175-369 |
5.06e-08 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 54.14 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 175 PELLKSVRQQLGWEIDIRVDANAAWSPPEAmARI-EAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEED 253
Cdd:PRK15072 193 PKLFEAVRNKFGFDLHLLHDVHHRLTPIEA-ARLgKSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWD 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 254 ARRLIEMRACQIFNLRLSKCGGLLSTMRIKKMAEKAGIKcqLGCHvGETSI----LAAAgRHFALTT------DHLAYVE 323
Cdd:PRK15072 272 CKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVR--TGSH-GPTDLspvcMAAA-LHFDLWVpnfgiqEYMGHSE 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1162405749 324 gsfapylLAKDVVRQPVFFENGGLaraLPG--PGLGIqvedHILEELA 369
Cdd:PRK15072 348 -------ETLEVFPHSYTFEDGYL---HPGdaPGLGV----DFDEKLA 381
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
17-129 |
1.16e-07 |
|
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: 49.78 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 17 APVKHNLATHYGSENIVVKLTTDAGVTGYGEGIPRRFVTGEILAESLAFLKKVLIPEIcrlpllfrPSIYANLARVGQQL 96
Cdd:pfam02746 14 RPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGGRAETIKAILDDHLAPLLIGRD--------AANISDLWQLMYRA 85
|
90 100 110
....*....|....*....|....*....|...
gi 1162405749 97 GAANYPAIwCAVEMAWLDAASKTCGQPLAEILG 129
Cdd:pfam02746 86 ALGNMSAK-AAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
107-290 |
1.98e-05 |
|
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: 46.23 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 107 AVEMAWLDAASKTCGQPLAEIL------GFQSQRAAIYSA---VLPMASEQQMARFFELVKLKKMRFLKLKVGTST---D 174
Cdd:cd03326 112 ALDMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVYAAggyYYPGDDLGRLRDEMRRYLDRGYTVVKIKIGGAPldeD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 175 PELLKSVRQQLGWEIDIRVDANAAWSPPEAMARIEAMAPYRLSAVEQPVAKEDFEGLQRVSAAVAIPIIADESVCTEEDA 254
Cdd:cd03326 192 LRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDA 271
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1162405749 255 RRLIE---MRACQ-IFNLRLSKCGGLLSTMRIKKMAEKAG 290
Cdd:cd03326 272 RNLLRyggMRPDRdVLQFDPGLSYGLPEYLRMLDVLEAHG 311
|
|
| MAL |
cd03314 |
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ... |
202-317 |
1.96e-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: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162405749 202 PEAMARIEAMAPYRlsaveqpvakedfEGLQRvsAAVAIPIIADESVCTEEDARRLIEMRACQIFNLRLSKCGGLLSTMR 281
Cdd:cd03314 239 GSREAQIERMAALR-------------AELDR--RGVGVRIVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGGIDNTID 303
|
90 100 110
....*....|....*....|....*....|....*.
gi 1162405749 282 IKKMAEKAGIKCQLGCHVGETSILAAAGRHFALTTD 317
Cdd:cd03314 304 AVLYCKEHGVGAYLGGSCNETDISARVTVHVALATR 339
|
|
| |
