|
Name |
Accession |
Description |
Interval |
E-value |
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
6-373 |
0e+00 |
|
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: 642.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 6 IVSIETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPWWGGESVETMQVIIEKYIAPVVVGRRVD 85
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 86 QITAIMADIEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESRLNFS 165
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 166 FKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIP 245
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENREALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 246 IMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEPGINFG 325
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 38198158 326 TELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDAVKTWTRN 373
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRRD 368
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
5-369 |
0e+00 |
|
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: 515.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 5 SIVSIETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPWWGGESVETMQVIIEKYIAPVVVGRRV 84
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 85 DQITAIMADIEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESRLNF 164
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 165 SFKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPI 244
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 245 PIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEPGINF 324
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 38198158 325 GTELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDAVKT 369
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
6-368 |
1.53e-119 |
|
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: 350.28 E-value: 1.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 6 IVSIETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPwwggesVETMQVIIEKYIAPVVVGRRVD 85
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTG------AEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 86 QITAIMADIEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESRLNfS 165
Cdd:COG4948 77 DIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFR-A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 166 FKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIP 245
Cdd:COG4948 156 LKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 246 IMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEPGINFG 325
Cdd:COG4948 236 IAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 38198158 326 tELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDAVK 368
Cdd:COG4948 316 -ELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALA 357
|
|
| 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 ... |
8-334 |
7.39e-68 |
|
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: 216.67 E-value: 7.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 8 SIETTILDVPLVRPHKFATTSMTAQPLLLVAIRTsDGVIGYGEGVVPggPWWGGESVETMQVIIeKYIAPVVVGRRVdQI 87
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIEL-DGITGYGEAAPT--PRVTGETVESVLAAL-KSVRPALIGGDP-RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 88 TAIMADIEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESRLNfSFK 167
Cdd:cd03319 76 EKLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFP-LLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 168 LKMGaLDPAVDVARIVSIAQALdGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIM 247
Cdd:cd03319 155 IKLG-GDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 248 ADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEpgINFgTE 327
Cdd:cd03319 233 ADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAK--ADF-VD 309
|
....*..
gi 38198158 328 LFGPLLF 334
Cdd:cd03319 310 LDGPLLL 316
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
9-328 |
3.75e-66 |
|
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: 210.28 E-value: 3.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 9 IETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGvvpggpwwggesvetmqviiekyiapvvvgrrvdqit 88
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEA------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 89 aimadiekvvanarfAKAAVDVALHDAWARSLGVPVHTLLGGaFRESVDVTWALGAAPADEIIEEAHEKLESRLNFsFKL 168
Cdd:cd03315 44 ---------------TKAAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRT-FKL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 169 KMGAlDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMA 248
Cdd:cd03315 107 KVGR-DPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 249 DESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEPGINFGTEL 328
Cdd:cd03315 186 DESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGEL 265
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
6-361 |
5.08e-66 |
|
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: 213.24 E-value: 5.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 6 IVSIETTILDVPLVRPHKfattSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPwwggesvETMQVIIEKYIAPVVVGRRVD 85
Cdd:cd03316 2 ITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGEAYPGGRP-------SAVAAAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 86 QITAIMADIEKVVANAR------FAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALG--AAPADEIIEEAHEK 157
Cdd:cd03316 71 DIERLWEKLYRRLFWRGrggvamAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGgyDDSPEELAEEAKRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 158 LEsrLNFS-FKLKMGALD-----PAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQ 231
Cdd:cd03316 151 VA--EGFTaVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 232 IEVLAELSRLLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--ACHGATsieGPIGT 309
Cdd:cd03316 229 LEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVrvAPHGAG---GPIGL 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 38198158 310 AASLHFACAEPgiNFGT-ELFGPLLFS-EELLQEPLKYSEGQLHLPAGPGLGVE 361
Cdd:cd03316 306 AASLHLAAALP--NFGIlEYHLDDLPLrEDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
149-366 |
2.29e-64 |
|
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: 203.95 E-value: 2.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 149 EIIEEAHEKLESRLNFSFKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTP 228
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 229 ADQIEVLAELSRLLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIAC--HGATsieGP 306
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVapHSGG---GP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 307 IGTAASLHFACAEPGINFGTELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDA 366
Cdd:pfam13378 158 IGLAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
9-369 |
8.52e-50 |
|
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: 170.88 E-value: 8.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 9 IETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPWWGGESVETMQVIIEKYIAPVVVGRRVDQIT 88
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 89 AIMADIEKVVANaRFAKAAVDVALHDAWARSLGVPVHTLLGGAfRESVDVTWALGAAPA-DEIIEEAHEKLES---Rlnf 164
Cdd:cd03317 81 EVSERLAPIKGN-NMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVGVSIGIQDDvEQLLKQIERYLEEgykR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 165 sFKLKmgaLDPAVDVARIVSIAQALdGHAGVRVDVN-----ARWDRftaLRYLPQLadgGVELIEQPTPADQIEVLAELS 239
Cdd:cd03317 156 -IKLK---IKPGWDVEPLKAVRERF-PDIPLMADANsaytlADIPL---LKRLDEY---GLLMIEQPLAADDLIDHAELQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 240 RLLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIA--CHGAtsIEGPIGTAASLHFAc 317
Cdd:cd03317 225 KLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPvwCGGM--LESGIGRAHNVALA- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 38198158 318 AEPGINF-----GTELFgpllFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDAVKT 369
Cdd:cd03317 302 SLPNFTYpgdisASSRY----FEEDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
9-320 |
4.41e-49 |
|
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: 165.19 E-value: 4.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 9 IETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEgvvpggpwwggesvetmqviiekyiapvvvgrrvdqit 88
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 89 aimadiekvvanarfAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALgaapadeiieeaheklesrlnfsfkl 168
Cdd:cd00308 43 ---------------VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGSI-------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 169 kmgaldpavdvARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMA 248
Cdd:cd00308 82 -----------ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38198158 249 DESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEP 320
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALP 222
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
33-363 |
9.38e-36 |
|
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: 133.61 E-value: 9.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 33 PLLLVAIRTSDGVIGYGEGVVPGGpwwgGESVETMQVIIEKYIapvvVGRRVDQITaimaDIEKVVANARF--------- 103
Cdd:cd03325 13 RWLFVKIETDEGVVGWGEPTVEGK----ARTVEAAVQELEDYL----IGKDPMNIE----HHWQVMYRGGFyrggpvlms 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 104 AKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDV-TWALGAAPADeiIEEAHEKLESRlnfSFK-LKMGALDP------ 175
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVySWIGGDRPSD--VAEAARARREA---GFTaVKMNATEElqwidt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 176 --AVD--VARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADES 251
Cdd:cd03325 156 skKVDaaVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 252 VQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--ACHGAtsiEGPIGTAASLHFACAEP--------- 320
Cdd:cd03325 236 LFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDValAPHCP---LGPIALAASLHVDASTPnfliqeqsl 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 38198158 321 GINFGTelfGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELN 363
Cdd:cd03325 313 GIHYNE---GDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
36-367 |
6.78e-32 |
|
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: 123.97 E-value: 6.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 36 LVAIRTSDGVIGYGEgvVPGG------------PWWGGESVETMQVIIEKyiAPVVVGRRVDQITAIMADIEKVVANArf 103
Cdd:cd03323 32 IVELTDDNGNTGVGE--SPGGaealealleaarSLVGGDVFGAYLAVLES--VRVAFADRDAGGRGLQTFDLRTTVHV-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 104 aKAAVDVALHDAWARSLGVPVHTLLGGAFRESV------------------DVTWALGAAPA---DEIIEEAhEKLESRL 162
Cdd:cd03323 106 -VTAFEVALLDLLGQALGVPVADLLGGGQRDSVpflaylfykgdrhktdlpYPWFRDRWGEAltpEGVVRLA-RAAIDRY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 163 NF-SFKLKMGALDPAVDVARIVSIAQALDGHAgVRVDVNARWDRFTALRYLPQLaDGGVELIEQPTPAdqIEVLAELSRL 241
Cdd:cd03323 184 GFkSFKLKGGVLPGEEEIEAVKALAEAFPGAR-LRLDPNGAWSLETAIRLAKEL-EGVLAYLEDPCGG--REGMAEFRRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 242 LPIPiMADESVQTPHDAL-EIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--ACHGATSIEgpIGTAASLHFACA 318
Cdd:cd03323 260 TGLP-LATNMIVTDFRQLgHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLgwGMHSNNHLG--ISLAMMTHVAAA 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 38198158 319 EPGINFGTELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDAV 367
Cdd:cd03323 337 APGLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKL 385
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
35-363 |
3.24e-31 |
|
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: 120.90 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 35 LLVAIRTSDGVIGYGEGVvpggpwwGGESVetmQVIIEKYIAPVVVGRRVdqitaimADIEKV--------VANAR---- 102
Cdd:cd03327 12 LFVEIETDDGTVGYANTT-------GGPVA---CWIVDQHLARFLIGKDP-------SDIEKLwdqmyratLAYGRkgia 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 103 -FAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWA-LGAAPADEIIEEAHEKLESrlnfSFK-LKM----GALDP 175
Cdd:cd03327 75 mAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYLKE----GYRgMKMrfgyGPSDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 176 AVDVARIVSIAQALDGHAG----VRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADES 251
Cdd:cd03327 151 HAGLRKNVELVRAIREAVGydvdLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 252 VQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIAC--HGatsiegpiGTAASLHFACAEPGINF----- 324
Cdd:cd03327 231 EYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVvpHA--------SQIYNYHFIMSEPNSPFaeylp 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 38198158 325 ------GTELFGPLlfseeLLQEPLKySEGQLHLPAGPGLGVELN 363
Cdd:cd03327 303 nspdevGNPLFYYI-----FLNEPVP-VNGYFDLSDKPGFGLELN 341
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
35-368 |
9.87e-31 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 120.39 E-value: 9.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 35 LLVAIRTSDGVIGYGEGVVPGGpwwgGESVETMQVIIEKYIapvvVGRRVDQITaimaDIEKVVANARF---------AK 105
Cdd:PRK14017 16 LFLKIETDEGIVGWGEPVVEGR----ARTVEAAVHELADYL----IGKDPRRIE----DHWQVMYRGGFyrggpilmsAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 106 AAVDVALHDAWARSLGVPVHTLLGGAFRESVDV-TWALGAAPADeIIEEAHEKLESrlnfSFK-LKMGALDP-------- 175
Cdd:PRK14017 84 AGIDQALWDIKGKALGVPVHELLGGLVRDRIRVySWIGGDRPAD-VAEAARARVER----GFTaVKMNGTEElqyidspr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 176 AVD--VARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADESVQ 253
Cdd:PRK14017 159 KVDaaVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 254 TPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKA--AGIACHGATsieGPIGTAASLHFACAEP---------GI 322
Cdd:PRK14017 239 SRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAydVALAPHCPL---GPIALAACLQVDAVSPnafiqeqslGI 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 38198158 323 --NFGTELFGPLLFseellQEPLKYSEGQLHLPAGPGLGVELNMDAVK 368
Cdd:PRK14017 316 hyNQGADLLDYVKN-----KEVFAYEDGFVAIPTGPGLGIEIDEAKVR 358
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
115-316 |
1.61e-28 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 111.97 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 115 AWArSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESrlnfSFKLKMGALDPAVDVARIVSIAQALDGHAG 194
Cdd:cd03320 55 ALA-NLEALLVGFTRPRNRIPVNALLPAGDAAALGEAKAAYGGGYR----TVKLKVGATSFEEDLARLRALREALPADAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 195 VRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEvlAELSRLLPIPIMADESVQTPHDALEIARRSAADVIALKT 274
Cdd:cd03320 130 LRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLA--ELRRLAAGVPIALDESLRRLDDPLALAAAGALGALVLKP 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 38198158 275 TKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFA 316
Cdd:cd03320 208 ALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLA 249
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
4-368 |
1.84e-27 |
|
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: 111.03 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 4 LSIVSIETTILDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIG--YGEGVVPGGPWWGGESVETM-QVIIEKYIAPVVV 80
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGhsYLFTYTPAALKSLKQLLDDMaALLVGEPLAPAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 81 GRRVDQITAIMADIEKVvanaRFAKAAVDVALHDAWARSLGVPVHTLLGGAFReSVDVTWALGAAPADEIIEEAHEKLES 160
Cdd:cd03321 81 ERALAKRFRLLGYTGLV----RMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAVTAAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 161 RLNfSFKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSR 240
Cdd:cd03321 156 GFH-AVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 241 LLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIachgatSIEGPIGTAASLHFACAEP 320
Cdd:cd03321 235 ALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGI------PMSSHLFQEISAHLLAVTP 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 38198158 321 GINF--GTELFGPllfseeLLQEPLKYSEGQLHLPAGPGLGVELNMDAVK 368
Cdd:cd03321 309 TAHWleYVDWAGA------ILEPPLKFEDGNAVIPDEPGNGIIWREKAVR 352
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
34-366 |
1.18e-25 |
|
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: 105.98 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 34 LLLVAIRTSDGVIGYGEGVVPGGPwwggESVETMqviIEKYIAPVVVGRRVDQITAIMADIEK-------VVANArfAKA 106
Cdd:cd03322 16 FVTLKITTDQGVTGLGDATLNGRE----LAVKAY---LREHLKPLLIGRDANRIEDIWQYLYRgaywrrgPVTMN--AIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 107 AVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLESrlnfSFKlkmgaldpAVDVaRIVSIA 186
Cdd:cd03322 87 AVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQ----GYR--------AIRV-QLPKLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 187 QALDGHAGVRV----DVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADESVQTPHDALEIA 262
Cdd:cd03322 154 EAVREKFGFEFhllhDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 263 RRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--ACHGATSIEgPIGTAASLHFACAEPgiNFGTELFGPllFSEELLQ 340
Cdd:cd03322 234 QERLIDYIRTTVSHAGGITPARKIADLASLYGVrtGWHGPTDLS-PVGMAAALHLDLWVP--NFGIQEYMR--HAEETLE 308
|
330 340
....*....|....*....|....*....
gi 38198158 341 ---EPLKYSEGQLHLPAGPGLGVELNMDA 366
Cdd:cd03322 309 vfpHSVRFEDGYLHPGEEPGLGVEIDEKA 337
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
14-316 |
2.87e-24 |
|
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: 101.46 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 14 LDVPLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGPWWGGESVETMQVIIEKYIAPVVVGRrVDQITAIMaD 93
Cdd:TIGR01928 3 VSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINKE-FEHPSEAL-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 94 IEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGAfRESVDVTWALGAAPADEIIEEAhEKLESRLNFSFKLKmgaL 173
Cdd:TIGR01928 81 LVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKL-RDKAPAGAVSGLANDEQMLKQI-ESLKATGYKRIKLK---I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 174 DPAVDVARIVSIAQALDGHAGVrVDVNARWDRfTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADESVQ 253
Cdd:TIGR01928 156 TPQIMHQLVKLRRLRFPQIPLV-IDANESYDL-QDFPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESIT 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38198158 254 TPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFA 316
Cdd:TIGR01928 234 SLDDARNLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALA 296
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
174-356 |
3.24e-22 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 95.81 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 174 DPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQL-ADGGVELIEQPTPAdqIEVLAELSRLLPIPIMADESV 252
Cdd:PRK02901 116 TLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT--VEELAELRRRVGVPIAADESI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 253 QTPHDALEIARRSAADVIALKTTKCGGLQRsrdIVAIAKAAGIACHGATSIEGPIGTAASLHFACAEPGINFGTELFGPL 332
Cdd:PRK02901 194 RRAEDPLRVARAGAADVAVLKVAPLGGVRA---ALDIAEQIGLPVVVSSALDTSVGIAAGLALAAALPELDHACGLATGG 270
|
170 180
....*....|....*....|....
gi 38198158 333 LFSEElLQEPLKYSEGQLHLPAGP 356
Cdd:PRK02901 271 LFEED-VADPLLPVDGFLPVRRVT 293
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
70-320 |
3.82e-22 |
|
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: 95.94 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 70 IIEKYIAPVVVGRRVDQITAIMADIEKVVAN------ARFAKAAVDVALHDAWARSLGVPVHTLLGgAFRESVDVTWALG 143
Cdd:cd03328 55 LVDGLLAPVVEGRDALDPPAAWEAMQRAVRNagrpgvAAMAISAVDIALWDLKARLLGLPLARLLG-RAHDSVPVYGSGG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 144 AAPADEiiEEAHEKLESRLNFSF---KLKMGAlDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGV 220
Cdd:cd03328 134 FTSYDD--DRLREQLSGWVAQGIprvKMKIGR-DPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 221 ELIEQPTPADQIEVLAELSRLLP--IPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--A 296
Cdd:cd03328 211 TWFEEPVSSDDLAGLRLVRERGPagMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVdlS 290
|
250 260
....*....|....*....|....
gi 38198158 297 CHGATSIegpigtaaSLHFACAEP 320
Cdd:cd03328 291 AHCAPAL--------HAHVACAVP 306
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
6-365 |
4.44e-22 |
|
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: 95.93 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 6 IVSIETTILDVPLVRPHKFATTSM----TAQPLLLVAIRTSDGVIGYgegvvpggpWWGGESVeTMQVIIEKYIAPVVVG 81
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHpgpaGTRKLALLTIETDEGAKGH---------AFGGRPV-TDPALVDRFLKKVLIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 82 RRVDQITAIMADI-EKVVANARFAKAAVDVALHDAWARSLGVPVHTLLGGaFRESVDV---TWALGAAPADEIIEEAHEK 157
Cdd:cd03329 72 QDPLDRERLWQDLwRLQRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAyasTMVGDDLEGLESPEAYADF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 158 LESRLNFSFK-LKMGALDPAVdVARIVSIAQALDGHAGVRV----DVNARWDRFTALRYLPQLADGGVELIEQPTPADQI 232
Cdd:cd03329 151 AEECKALGYRaIKLHPWGPGV-VRRDLKACLAVREAVGPDMrlmhDGAHWYSRADALRLGRALEELGFFWYEDPLREASI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 233 EVLAELSRLLPIPIMADESVQTPHDAL-EIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGIAC--HGatsiegpiGT 309
Cdd:cd03329 230 SSYRWLAEKLDIPILGTEHSRGALESRaDWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVelHG--------NG 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38198158 310 AASLHFACAEPGINFgtelfgpllFSEELLQEPLKY---------------SEGQLHLPAGPGLGVELNMD 365
Cdd:cd03329 302 AANLHVIAAIRNTRY---------YERGLLHPSQKYdvyagylsvlddpvdSDGFVHVPKGPGLGVEIDFD 363
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
8-129 |
1.83e-21 |
|
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: 88.30 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 8 SIETTILDV-PLVRPHKFATTSMTAQPLLLVAIRTSDGVIGYGEGVVPGGpwwggeSVETMQVIIEKYIAPVVVGRRVDQ 86
Cdd:pfam02746 1 AIEVFVVDVgWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGG------RAETIKAILDDHLAPLLIGRDAAN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 38198158 87 ITAIMADIEKVVANARFAKAAVDVALHDAWARSLGVPVHTLLG 129
Cdd:pfam02746 75 ISDLWQLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
147-244 |
5.85e-19 |
|
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: 80.79 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 147 ADEIIEEAHEKLESRLNFSFKLKMGAlDPAVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQP 226
Cdd:smart00922 1 PEELAEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 38198158 227 TPADQIEVLAELSRLLPI 244
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
39-366 |
2.59e-15 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 76.49 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 39 IRTSDGVIGYGEGVVPGgpwwggesvETMQVI--IEKYIAPVVVGRRVDQITAI----------------MADIekvvan 100
Cdd:PRK15072 22 ITTDDGVTGLGDATLNG---------RELAVAsyLQDHVCPLLIGRDAHRIEDIwqylyrgaywrrgpvtMSAI------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 101 arfakAAVDVALHDAWARSLGVPVHTLLGGAFRESVDVTWALGAAPADEIIEEAHEKLEsrLNF-SFKLKMGAldPAVDV 179
Cdd:PRK15072 87 -----AAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLE--LGYkAIRVQCGV--PGLKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 180 ARIVSIAQALDGHAGVRVDVNA--RWDRFTALRYLPQLADG-----GVEL-----------------------------I 223
Cdd:PRK15072 158 TYGVSKGKGLAYEPATKGLLPEeeLWSTEKYLRFVPKLFEAvrnkfGFDLhllhdvhhrltpieaarlgkslepyrlfwL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 224 EQPTPADQIEVLAELSRLLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI--ACHGAT 301
Cdd:PRK15072 238 EDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVrtGSHGPT 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38198158 302 SIEgPIGTAASLHFACAEPgiNFGT-ELFGPLLFSEELLQEPLKYSEGQLHLPAGPGLGVELNMDA 366
Cdd:PRK15072 318 DLS-PVCMAAALHFDLWVP--NFGIqEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKL 380
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
35-365 |
3.09e-14 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 73.22 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 35 LLVAIRTSDGVIGYGegVVPGGpwwggesvETMQVIIEKYIAPVVVGRRVdqitaimADIEK----------------VV 98
Cdd:PRK15440 59 LVVEVEAENGQVGFA--VSTAG--------EMGAFIVEKHLNRFIEGKCV-------SDIELiwdqmlnatlyygrkgLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 99 ANArfaKAAVDVALHDAWARSLGVPVHTLLGGAFRESVdVTWALGAAPadeiieeaheKLESRLNF---SFKLKMGaldP 175
Cdd:PRK15440 122 MNT---ISCVDLALWDLLGKVRGLPVYKLLGGAVRDEL-QFYATGARP----------DLAKEMGFiggKMPLHHG---P 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 176 AvdvarivsiaqalDGHAGVRVDVNA--------------RWDRFTAL--RYLPQLADG----GVELIEQPTPADQIEVL 235
Cdd:PRK15440 185 A-------------DGDAGLRKNAAMvadmrekvgddfwlMLDCWMSLdvNYATKLAHAcapyGLKWIEECLPPDDYWGY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 236 AELSRLLPIPIMadesVQT-PHDA--------LEIARrsaADVIALKTTKCGGLQRSRDIVAIAKAagiacHGATSIegP 306
Cdd:PRK15440 252 RELKRNAPAGMM----VTSgEHEAtlqgfrtlLEMGC---IDIIQPDVGWCGGLTELVKIAALAKA-----RGQLVV--P 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38198158 307 IGTAA-SLHFACAEPGINFGTELF-GPL------LFSEELLQEPLKYSeGQLHLPAG--PGLGVELNMD 365
Cdd:PRK15440 318 HGSSVySHHFVITRTNSPFSEFLMmSPDadtvvpQFDPILLDEPVPVN-GRIHKSVLdkPGFGVELNRD 385
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
41-340 |
1.71e-13 |
|
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: 70.22 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 41 TSDGVIGYGEgVVPGgPWWGGESVETMQVIIEKYIAPVVVGrrvdQITAIMADIEKVVANARFAKAAVDVAlhDAWARSL 120
Cdd:TIGR01927 29 TDEGRTGWGE-IAPL-PGFGTETLAEALDFCRALIEEITRG----DIEAIDDQLPSVAFGFESALIELESG--DELPPAS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 121 GVPVHTLLGGafrESVDVTWALGAAPADEIieeaheklesrlnfsFKLKMGALDPAVDVARIVSIAQALDGHAGVRVDVN 200
Cdd:TIGR01927 101 NYYVALLPAG---DPALLLLRSAKAEGFRT---------------FKWKVGVGELAREGMLVNLLLEALPDKAELRLDAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 201 ARWDRFTA---LRYLPQLADGGVELIEQP-TPADQIevlAELSRLLPIPIMADESVQTPHDALEIARRSAADVIALKTTK 276
Cdd:TIGR01927 163 GGLSPDEAqqfLKALDPNLRGRIAFLEEPlPDADEM---SAFSEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38198158 277 CGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFAcAEPGINFGTELFGPLLFSEELLQ 340
Cdd:TIGR01927 240 IGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLA-AKLSPDPAAVGFTTALLRAQDLE 302
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
35-316 |
6.41e-13 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 68.89 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 35 LLVAIRTSDGVIGYGEgVVPGgPWWGGESVETMQVIIEKYiaPvvvgrrvDQIT-AIMADIEKVVANARFAkaavdvaLH 113
Cdd:PRK02714 31 IILRLTDETGKIGWGE-IAPL-PWFGSETLEEALAFCQQL--P-------GEITpEQIFSIPDALPACQFG-------FE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 114 DAWARSLGvpvhtllGGAFRESVDVTWAlGAAPADEIIEEAHEKLESRLNFSFKLKMGALDPAVDVARIVSIAQALDGHA 193
Cdd:PRK02714 93 SALENESG-------SRSNVTLNPLSYS-ALLPAGEAALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 194 GVRVDVNARWDRFTALRYLpQLAD----GGVELIEQPTPADQIEVLAELSRLLPIPIMADESVQTPHDALEIARRSAADV 269
Cdd:PRK02714 165 KLRLDANGGLSLEEAKRWL-QLCDrrlsGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANLAQLQQCYQQGWRGI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 38198158 270 IALKTTKCGGLQRSRDIvaiakaagiaCHG-------ATSIEGPIGTAASLHFA 316
Cdd:PRK02714 244 FVIKPAIAGSPSRLRQF----------CQQhpldavfSSVFETAIGRKAALALA 287
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
86-352 |
9.76e-10 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 59.38 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 86 QITAIMADIEKVVAN--------ARFAKAAVDVALHDAWARSLGVPVHTLLGGAFRESVDV--TWALGA----APADEII 151
Cdd:PRK15129 61 QIMSVVPQLEKGLTRealqkllpAGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTaqTVVIGTpeqmANSASAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 152 EEAHEKLesrlnfsFKLKmgaLDPAVDVARIVSIAQALDgHAGVRVDVNARWdRFTALRYLPQL-ADGGVELIEQPTPAD 230
Cdd:PRK15129 141 WQAGAKL-------LKVK---LDNHLISERMVAIRSAVP-DATLIVDANESW-RAEGLAARCQLlADLGVAMLEQPLPAQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 231 QIEVLAELsrLLPIPIMADESVQTPHDALEIARRSaaDVIALKTTKCGGLQRSRDIVAIAKAAGIA----CHGATSiegp 306
Cdd:PRK15129 209 DDAALENF--IHPLPICADESCHTRSSLKALKGRY--EMVNIKLDKTGGLTEALALATEARAQGFAlmlgCMLCTS---- 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 38198158 307 IGTAASLHFAcaePGINFgTELFGPLLFSEELlqEP-LKYSEGQLHL 352
Cdd:PRK15129 281 RAISAALPLV---PQVRF-ADLDGPTWLAVDV--EPaLQFTTGELHL 321
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
75-295 |
1.33e-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: 59.28 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 75 IAPVVVGRRVDQITAIMADIEKVVAN-------------ARFAKAAVDVALHDAWARSLGVPVHTLLGG----AFRESVD 137
Cdd:cd03324 68 LAHLVVGRDLESIVADMGKFWRRLTSdsqlrwigpekgvIHLATAAVVNAVWDLWAKAEGKPLWKLLVDmtpeELVSCID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 138 ---VTWALGAAPADEIIEEAHEKLESR------------------LNFS------------------FKLKMGAlDPAVD 178
Cdd:cd03324 148 fryITDALTPEEALEILRRGQPGKAAReadllaegypayttsagwLGYSdeklrrlckealaqgfthFKLKVGA-DLEDD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 179 VARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELS---RLLPIPIMADESVQTP 255
Cdd:cd03324 227 IRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRkalAPLPIGVATGEHCQNR 306
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 38198158 256 HDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKAAGI 295
Cdd:cd03324 307 VVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGV 346
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
104-366 |
3.24e-08 |
|
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: 54.71 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 104 AKAAVDVALHDAWARSLGVPVHTLLG-----GAFRESVDVTWALGAAPADEIIEEAHEKLESRLNFSF---KLKMGALDP 175
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAAGGYYYPGDDLGRLRDEMRRYLDRGYtvvKIKIGGAPL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 176 AVDVARIVSIAQALDGHAGVRVDVNARWDRFTALRYLPQLADGGVELIEQPTPADQIEVLAELSRLLPIPIMADESVQTP 255
Cdd:cd03326 189 DEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 256 HDALEIAR----RSAADVIALKTTKCGGLQRSRDIVAIAKAAGI---AC--HGATSIEgpIGTAASLHFACAE--PGInf 324
Cdd:cd03326 269 QDARNLLRyggmRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWsrrRFfpHGGHLMS--LHIAAGLGLGGNEsyPDV-- 344
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 38198158 325 gtelFGPLlfseELLQEPLKYSEGQLHLPAGPGLGVELNMDA 366
Cdd:cd03326 345 ----FQPF----GGFADGCKVENGYVRLPDAPGIGFEGKAEL 378
|
|
| MAL |
cd03314 |
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ... |
222-324 |
2.46e-06 |
|
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: 48.93 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 222 LIEQPTPA----DQIEVLAEL-----SRLLPIPIMADESVQTPHDALEIARRSAADVIALKTTKCGGLQRSRDIVAIAKA 292
Cdd:cd03314 231 RIEGPMDAgsreAQIERMAALraeldRRGVGVRIVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGGIDNTIDAVLYCKE 310
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 38198158 293 AGI-ACHGATSIEGPIGTAASLHFACA--------EPGINF 324
Cdd:cd03314 311 HGVgAYLGGSCNETDISARVTVHVALAtradqmlaKPGMGV 351
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
196-317 |
1.17e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 43.67 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38198158 196 RVDVNARWDRFTAL---RYLPQLADGGVELIEQP--TPADQievlAELSRLLPIPIMADESVQTPHDALEIARRSAADVI 270
Cdd:PRK05105 161 RLDANRGWTLEKAQqfaKYVPPDYRHRIAFLEEPckTPDDS----RAFARATGIAIAWDESLREPDFQFEAEPGVRAIVI 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 38198158 271 alKTTKCGGLQRSRDIVAIAKAAGIACHGATSIEGPIGTAASLHFAC 317
Cdd:PRK05105 237 --KPTLTGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLAA 281
|
|
| |
