|
Name |
Accession |
Description |
Interval |
E-value |
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
7-359 |
0e+00 |
|
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: 622.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 7 ITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSPWYTEETIGTCLHMLKDFFIPNVVGREFNHPS 86
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 87 EVPDSLARYKGNRMAKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPAGVVVGLAP-LDDMLKEIESYQKEGYQRIKIKI 165
Cdd:cd03317 81 EVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDdVEQLLKQIERYLEEGYKRIKLKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 166 QPGQDVELVKAIRSRFPTIPLMADANSSYELKDISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSV 245
Cdd:cd03317 161 KPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 246 DDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALASLPQFTIPGDISSSSRYWD 325
Cdd:cd03317 241 EDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALASLPNFTYPGDISASSRYFE 320
|
330 340 350
....*....|....*....|....*....|....
gi 490533565 326 EDIVTPDIRIDNGFISVSKQPGLGVEVNQDIMRK 359
Cdd:cd03317 321 EDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
10-334 |
0e+00 |
|
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: 562.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 10 YHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSPWYTEETIGTCLHMLKDFFIPNVVGrEFNHPSEVP 89
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINK-EFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 90 DSLARYKGNRMAKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKIKIQPGQ 169
Cdd:TIGR01928 80 ELVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKITPQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 170 DVELVKAIRSRFPTIPLMADANSSYELKDISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSVDDAR 249
Cdd:TIGR01928 160 MHQLVKLRRLRFPQIPLVIDANESYDLQDFPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 250 RAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALASLPQFTIPGDISSSSRYWDEDIV 329
Cdd:TIGR01928 240 NLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASLGGNDYPGDVSPSGYYFDQDIV 319
|
....*
gi 490533565 330 TPDIR 334
Cdd:TIGR01928 320 APSIR 324
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
4-360 |
3.68e-132 |
|
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: 382.25 E-value: 3.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 4 IEKITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSPwyteetIGTCLHMLKDFFIPNVVGREFN 83
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTG------AEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 84 HPSEVPDSLARY-KGNRMAKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRI 161
Cdd:COG4948 77 DIEALWQRLYRAlPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGkVRDRVPVYATLGIDTPEEMAEEAREAVARGFRAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 162 KIKI---QPGQDVELVKAIRSRF-PTIPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAI 236
Cdd:COG4948 157 KLKVggpDPEEDVERVRAVREAVgPDARLRVDANGAWTLEEaIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 237 CLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALAS-LPQFTIpG 315
Cdd:COG4948 237 AADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAaLPNFDI-V 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490533565 316 DIsSSSRYWDEDIVTPDIRIDNGFISVSKQPGLGVEVNQDIMRKY 360
Cdd:COG4948 316 EL-DGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 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 ... |
6-308 |
9.03e-72 |
|
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: 226.30 E-value: 9.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 6 KITLYHLSMNLKKPFKNSIETLQERKFLIVEaIDTSGVTGWGEVSAFssPWYTEETIGTCLHMLKDFFiPNVVGREFNHP 85
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVE-IELDGITGYGEAAPT--PRVTGETVESVLAALKSVR-PALIGGDPRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 86 SEVPDSLARYKGNRMAKAGLESAVWDIYAKKKGVSLAE-ALGGTRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKIK 164
Cdd:cd03319 77 KLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQlWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 165 I--QPGQDVELVKAIRSRFPTIPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDES 241
Cdd:cd03319 157 LggDLEDDIERIRAIREAAPDARLRVDANQGWTPEEaVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADES 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490533565 242 ICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALASL 308
Cdd:cd03319 237 CFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAA 303
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
4-351 |
7.49e-69 |
|
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: 220.18 E-value: 7.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 4 IEKITLYHLSMNLKKPFKnsieTLQERKFLIVEAIDTSGVTGWGEVSafssPWYTEETIgtcLHMLKDFFIPNVVGREFN 83
Cdd:cd03316 2 ITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGEAY----PGGRPSAV---AAAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 84 HPSEVPDSLARYKGNRM-------AKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVP--AGVVVGLAPLDDMLKEIESY 153
Cdd:cd03316 71 DIERLWEKLYRRLFWRGrggvamaAISAVDIALWDIKGKAAGVPVYKLLGGkVRDRVRvyASGGGYDDSPEELAEEAKRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 154 QKEGYQRIKIKI--------QPGQDVELVKAIRSRF-PTIPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIV 223
Cdd:cd03316 151 VAEGFTAVKLKVggpdsggeDLREDLARVRAVREAVgPDVDLMVDANGRWDLAEaIRLARALEEYDLFWFEEPVPPDDLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 224 DHRHLQKHLKTAICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVwCGGMLETGISRAQNV 303
Cdd:cd03316 231 GLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRV-APHGAGGPIGLAASL 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490533565 304 -ALASLPQFTI---PGDisssSRYWDEDIVTPDIRIDNGFISVSKQPGLGVE 351
Cdd:cd03316 310 hLAAALPNFGIleyHLD----DLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
13-317 |
8.24e-67 |
|
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: 212.20 E-value: 8.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 13 SMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSafsspwyteetigtclhmlkdffipnvvgrefnhpsevpdsl 92
Cdd:cd03315 7 RLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEAT------------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 93 arykgnrmaKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKIKI--QPGQD 170
Cdd:cd03315 45 ---------KAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVgrDPARD 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 171 VELVKAIRSRFPT-IPLMADANSSY-ELKDISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSVDDA 248
Cdd:cd03315 116 VAVVAALREAVGDdAELRVDANRGWtPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDA 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 249 RRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVAL-ASLPQFTIPGDI 317
Cdd:cd03315 196 FRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLaAALRAVTLPGEL 265
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
145-356 |
9.89e-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: 202.41 E-value: 9.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 145 DMLKEIESYQKE-GYQRIKIKI---QPGQDVELVKAIRSRF-PTIPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQ 218
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVggpDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEaIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 219 ADDIVDHRHLQKHLKTAICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMlETGIS 298
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPIG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490533565 299 RAQNVALASLPQFTIPGDISSSSRYWDEDIVTPDIRIDNGFISVSKQPGLGVEVNQDI 356
Cdd:pfam13378 160 LAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
4-359 |
7.07e-52 |
|
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: 176.35 E-value: 7.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 4 IEKITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSPWYTEETIGTCLHMLKDFFIPNVVGREFN 83
Cdd:cd03318 2 IEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 84 HPSEVPDSLAR-YKGNRMAKAGLESAVWDIYAKKKGVSLAEALGGT-RDKVPAGVVVGLAPLDDMLKEIESYQKEG-YQR 160
Cdd:cd03318 82 NIGAAMALLDRaVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRvRDSLPVAWTLASGDTERDIAEAEEMLEAGrHRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 161 IKIKI---QPGQDVELVKAIRSRFPT-IPLMADANSSYELKDISR-LKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTA 235
Cdd:cd03318 162 FKLKMgarPPADDLAHVEAIAKALGDrASVRVDVNQAWDESTAIRaLPRLEAAGVELIEQPVPRENLDGLARLRSRNRVP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 236 ICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVAL-ASLPQFTIP 314
Cdd:cd03318 242 IMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLfATLPSLPFG 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490533565 315 GDIsSSSRYWDEDIVTPDIRIDNGFISVSKQPGLGVEVNQDIMRK 359
Cdd:cd03318 322 CEL-FGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
7-314 |
5.48e-47 |
|
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: 159.42 E-value: 5.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 7 ITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVsafsspwyteetigtclhmlkdffipnvvgrefnhps 86
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 87 evpdslarykgnrmaKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVglaplddmlkeiesyqkegyqrikiki 165
Cdd:cd00308 44 ---------------ISGIDMALWDLAAKALGVPLAELLGGgSRDRVPAYGSI--------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 166 qpgqdvELVKAIRSRFPT-IPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESIC 243
Cdd:cd00308 82 ------ERVRAVREAFGPdARLAVDANGAWTPKEaIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVT 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490533565 244 SVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVAL-ASLPQFTIP 314
Cdd:cd00308 156 TVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLaAALPNDRAI 227
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
4-360 |
1.90e-40 |
|
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: 146.48 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 4 IEKITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSPWYTEETIGTCLHMLKDFFIPNVVGREFN 83
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 84 HPSEVPDSLAR-YKGNRMAKAGLESAVWDIYAKKKGVSLAEALGGT-RDKVPAGVVVGLAPLDDMLKEIES-YQKEGYQR 160
Cdd:TIGR02534 81 EIAAIMADLEKvVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRvRDSVDVTWTLASGDTDRDIAEAEErIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 161 IKIKI---QPGQDVELVKAIRSRF-PTIPLMADANSSY-ELKDISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTA 235
Cdd:TIGR02534 161 FKLKIgarDPADDVAHVVAIAKALgDRASVRVDVNAAWdERTALHYLPQLADAGVELIEQPTPAENREALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 236 ICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAqnvalASLPQFTIPG 315
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTI-----ASAHFFATFP 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490533565 316 DISSSSRYW-----DEDIVTPDIRIDNGFISVSKQPGLGVEVNQDIMRKY 360
Cdd:TIGR02534 316 ALSFGTELFgplllKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFY 365
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
7-315 |
6.47e-33 |
|
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: 123.52 E-value: 6.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 7 ITLYHLSMNLKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSspwyteetigtclhmlkdffipnvvgrefnhps 86
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGEIAPLP--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 87 evpdslarykgnrmAKAGLESAVWDiyakkkgvsLAEALGGTRDKVPAGVVVGLAPLDD--MLKEIESYQKEGYQRIKIK 164
Cdd:cd03320 48 --------------LAFGIESALAN---------LEALLVGFTRPRNRIPVNALLPAGDaaALGEAKAAYGGGYRTVKLK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 165 I---QPGQDVELVKAIRSRFPT-IPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIvdHRHLQKHLKTAICLD 239
Cdd:cd03320 105 VgatSFEEDLARLRALREALPAdAKLRLDANGGWSLEEaLAFLEALAAGRIEYIEQPLPPDDL--AELRRLAAGVPIALD 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490533565 240 ESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALASL--PQFTIPG 315
Cdd:cd03320 183 ESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAAlpPLPAACG 260
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
16-360 |
1.75e-29 |
|
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: 116.43 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 16 LKKPFKNSIETLQERKFLIVEAIDTSGVTGWGEVsaFSspwYTEETIGTCLHMLKDFfIPNVVGREFNhPSEVPDSLA-R 94
Cdd:cd03321 15 MQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYL--FT---YTPAALKSLKQLLDDM-AALLVGEPLA-PAELERALAkR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 95 YK--GN----RMAKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKIKI-QP 167
Cdd:cd03321 88 FRllGYtglvRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIgYP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 168 --GQDVELVKAIRSRFPT-IPLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESIC 243
Cdd:cd03321 168 taDEDLAVVRSIRQAVGDgVGLMVDYNQSLTVPEaIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 244 SVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHhmqvwcggmletGISRAQNValasLPQFTIPGDISSSSRY 323
Cdd:cd03321 248 GPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQA------------GIPMSSHL----FQEISAHLLAVTPTAH 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490533565 324 WDE------DIVTPDIRIDNGFISVSKQPGLGVEVNQDIMRKY 360
Cdd:cd03321 312 WLEyvdwagAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
100-353 |
2.37e-29 |
|
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: 115.89 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 100 MAKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVPA-GVVVGLAPLDDMLKEIESYQKEGYQRIKIKIQPG--------- 168
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLGGrTRDKIPAyASGLYPTDLDELPDEAKEYLKEGYRGMKMRFGYGpsdghaglr 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 169 QDVELVKAIRSRF-PTIPLMADANSSYELK-DISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSVD 246
Cdd:cd03327 156 KNVELVRAIREAVgYDVDLMLDCYMSWNLNyAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 247 DARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVwcggmletgISRAQNValASLpQFTIPGDISSSSRY--- 323
Cdd:cd03327 236 GFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPV---------VPHASQI--YNY-HFIMSEPNSPFAEYlpn 303
|
250 260 270
....*....|....*....|....*....|....*...
gi 490533565 324 ---WD-----EDIVTPDIRIDNGFISVSKQPGLGVEVN 353
Cdd:cd03327 304 spdEVgnplfYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
32-353 |
4.70e-26 |
|
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: 107.03 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 32 FLIVEaiDTSGVTGWGEVSAFSSpwytEETIGTCLHMLKDFFIpnvvGREfnhPSEVPD------SLARYKGNRM---AK 102
Cdd:cd03325 16 FVKIE--TDEGVVGWGEPTVEGK----ARTVEAAVQELEDYLI----GKD---PMNIEHhwqvmyRGGFYRGGPVlmsAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 103 AGLESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKI-------------KIQPG 168
Cdd:cd03325 83 SGIDQALWDIKGKVLGVPVHQLLGGqVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMnateelqwidtskKVDAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 169 qdVELVKAIRSRF-PTIPLMADAN---SSYELKDIsrLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICS 244
Cdd:cd03325 163 --VERVAALREAVgPDIDIGVDFHgrvSKPMAKDL--AKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 245 VDDARRAIELGSCKIINIKPSRVGGLTEALKIhdlckehhmqvwcGGMLET-GISRAQN-----VALA-------SLPQF 311
Cdd:cd03325 239 RWDFKELLEDGAVDIIQPDISHAGGITELKKI-------------AAMAEAyDVALAPHcplgpIALAaslhvdaSTPNF 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490533565 312 TIPgDISSSSRYWDED------IVTPDIRIDNGFISVSKQPGLGVEVN 353
Cdd:cd03325 306 LIQ-EQSLGIHYNEGDdlldylVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
24-360 |
1.04e-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: 106.37 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 24 IETLQERKFLIVEAIDTSGVTGWGEVSAFSSPWYTEEtigtclhMLKDFFIPNVVGREFNHPSEVPDSLarYKG------ 97
Cdd:cd03322 8 IVTCPGRNFVTLKITTDQGVTGLGDATLNGRELAVKA-------YLREHLKPLLIGRDANRIEDIWQYL--YRGaywrrg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 98 ---NRmAKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKIkiqpgQDVEL 173
Cdd:cd03322 79 pvtMN-AIAAVDMALWDIKGKAAGMPLYQLLGGkSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRV-----QLPKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 174 VKAIRSRF-PTIPLMADANSSYELKDISRL-KELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSVDDARRA 251
Cdd:cd03322 153 FEAVREKFgFEFHLLHDVHHRLTPNQAARFgKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 252 IELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLE-TGISRAQNVAL-ASLPQFTIpgdiSSSSRYWDE--D 327
Cdd:cd03322 233 IQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDlSPVGMAAALHLdLWVPNFGI----QEYMRHAEEtlE 308
|
330 340 350
....*....|....*....|....*....|...
gi 490533565 328 IVTPDIRIDNGFISVSKQPGLGVEVNQDIMRKY 360
Cdd:cd03322 309 VFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
143-234 |
5.22e-24 |
|
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: 94.66 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 143 LDDMLKEIESYQKE-GYQRIKIKI--QPGQDVELVKAIRSRF-PTIPLMADANSSYELKD-ISRLKELDDYHLMMIEQPL 217
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEaIRALEALDELGLEWIEEPV 80
|
90
....*....|....*..
gi 490533565 218 QADDIVDHRHLQKHLKT 234
Cdd:smart00922 81 PPDDLEGLAELRRATPI 97
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
99-355 |
2.36e-23 |
|
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: 99.78 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 99 RMAKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPA-------GVVVGLAPLDDMLKEIESYQKEGYQRIKIKI-QPG-- 168
Cdd:cd03329 93 DRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAyastmvgDDLEGLESPEAYADFAEECKALGYRAIKLHPwGPGvv 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 169 -QDVELVKAIRSRF-PTIPLMADANSSYELKDISRL-KELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSV 245
Cdd:cd03329 173 rRDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLgRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 246 DDARRA-IELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGmleTGISRAQNVALASLPQFTIPGDISSSSRYW 324
Cdd:cd03329 253 LESRADwVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHG---NGAANLHVIAAIRNTRYYERGLLHPSQKYD 329
|
250 260 270
....*....|....*....|....*....|....
gi 490533565 325 DED--IVTPDIRIDN-GFISVSKQPGLGVEVNQD 355
Cdd:cd03329 330 VYAgyLSVLDDPVDSdGFVHVPKGPGLGVEIDFD 363
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
34-360 |
2.87e-20 |
|
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: 91.23 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 34 IVEAIDTSGVTGWGEVSAFSSPwyteetigtcLHMLKDFFIPNVVGREF-NHPSEV---------PDSLARYKGNRMAK- 102
Cdd:cd03323 32 IVELTDDNGNTGVGESPGGAEA----------LEALLEAARSLVGGDVFgAYLAVLesvrvafadRDAGGRGLQTFDLRt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 103 -----AGLESAVWDIYAKKKGVSLAEALGGT-RDKVPAgvvvgLAPL--------------------------DDMLKEI 150
Cdd:cd03323 102 tvhvvTAFEVALLDLLGQALGVPVADLLGGGqRDSVPF-----LAYLfykgdrhktdlpypwfrdrwgealtpEGVVRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 151 ES-YQKEGYQRIKIK---IQPGQDVELVKAIRSRFPTIPLMADANSSYELKD-ISRLKELDDYhLMMIEQPLQADDIVDh 225
Cdd:cd03323 177 RAaIDRYGFKSFKLKggvLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETaIRLAKELEGV-LAYLEDPCGGREGMA- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 226 rhlQKHLKTAICLDESICSVD--DARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRAQNV 303
Cdd:cd03323 255 ---EFRRATGLPLATNMIVTDfrQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMT 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490533565 304 ALASlpqfTIPGDISSSSRYW---DEDIVTPD-IRIDNGFISVSKQPGLGVEVNQDIMRKY 360
Cdd:cd03323 332 HVAA----AAPGLITACDTHWiwqDGQVITGEpLRIKDGKVAVPDKPGLGVELDRDKLAKA 388
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
101-310 |
4.46e-20 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 89.81 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 101 AKAGLESAVWDIYAKKKGVSLAEALGGTRDK--VPAGVVVGLAPlDDMLKEIESYQKEGYQRIKIKIQPGQDVELVKAIR 178
Cdd:PRK15129 87 ARNAVDCALWDLAARQQQQSLAQLIGITLPEtvTTAQTVVIGTP-EQMANSASALWQAGAKLLKVKLDNHLISERMVAIR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 179 SRFPTIPLMADANSSYELKDI-SRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLktAICLDESiCSVDDARRAIElGSC 257
Cdd:PRK15129 166 SAVPDATLIVDANESWRAEGLaARCQLLADLGVAMLEQPLPAQDDAALENFIHPL--PICADES-CHTRSSLKALK-GRY 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490533565 258 KIINIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETgiSRAQNVALASLPQ 310
Cdd:PRK15129 242 EMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCT--SRAISAALPLVPQ 292
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
10-306 |
2.17e-19 |
|
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: 87.55 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 10 YHLSMNLKKPFKNSIETLQERKFLIVEAIDTsGVTGWGEVSAFssPWYTEETIGTCLHMLKDFfIPNVVGREFNHPSEVP 89
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDE-GRTGWGEIAPL--PGFGTETLAEALDFCRAL-IEEITRGDIEAIDDQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 90 DSLArykgnrmakAGLESAVWDIYAkkkGVSLAEALGGTRDKVPAGvvvglAPLDDMLKeieSYQKEGYQRIKIKI---Q 166
Cdd:TIGR01927 77 PSVA---------FGFESALIELES---GDELPPASNYYVALLPAG-----DPALLLLR---SAKAEGFRTFKWKVgvgE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 167 PGQDVELVKAIRSRFP-TIPLMADANSSYE-LKDISRLKELDDYH---LMMIEQPLQADDivDHRHLQKHLKTAICLDES 241
Cdd:TIGR01927 137 LAREGMLVNLLLEALPdKAELRLDANGGLSpDEAQQFLKALDPNLrgrIAFLEEPLPDAD--EMSAFSEATGTAIALDES 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490533565 242 ICSVDDARRAIELGSCKIINIKPSRVGGLTealKIHDLCKEHH---MQVWCGGMLETGISRAQNVALA 306
Cdd:TIGR01927 215 LWELPQLADEYGPGWRGALVIKPAIIGSPA---KLRDLAQKAHrlgLQAVFSSVFESSIALGQLARLA 279
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
32-359 |
3.66e-17 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 81.87 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 32 FLIVEAIDtsGVTGWGEVSAfsspwytE---ETIGTCLHMLKDFFIpnvvGREfnhPSEVPD---SLAR---YKG---NR 99
Cdd:PRK14017 17 FLKIETDE--GIVGWGEPVV-------EgraRTVEAAVHELADYLI----GKD---PRRIEDhwqVMYRggfYRGgpiLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 100 MAKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVGLAPLDDMLKEIESYQKEGYQRIKI-------------KI 165
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGlVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMngteelqyidsprKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 166 QpgQDVELVKAIRSRF-PTI-----------PLMAdanssyelKDIsrLKELDDYHLMMIEQPLQADDIVDHRHLQKHLK 233
Cdd:PRK14017 161 D--AAVARVAAVREAVgPEIgigvdfhgrvhKPMA--------KVL--AKELEPYRPMFIEEPVLPENAEALPEIAAQTS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 234 TAICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIhdlckehhmqvwcGGMLET-GISRAQN-----VALAS 307
Cdd:PRK14017 229 IPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKI-------------AAMAEAyDVALAPHcplgpIALAA 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490533565 308 LPQ--FTIPGDI---SSSSRYWDED------IVTPDI-RIDNGFISVSKQPGLGVEVNQDIMRK 359
Cdd:PRK14017 296 CLQvdAVSPNAFiqeQSLGIHYNQGadlldyVKNKEVfAYEDGFVAIPTGPGLGIEIDEAKVRE 359
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
100-287 |
7.62e-15 |
|
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: 74.76 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 100 MAKAGLESAVWDIYAKKKGVSLAEALGGTRDKVPAGVVVGLA--PLDDMLKEIESYQKEGYQRIKIKI--QPGQDVELVK 175
Cdd:cd03328 94 MAISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTsyDDDRLREQLSGWVAQGIPRVKMKIgrDPRRDPDRVA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 176 AIRSRF-PTIPLMADANSSYELKDISRLKE-LDDYHLMMIEQPLQADDIVDHRHLQKHL--KTAICLDESICSVDDARRA 251
Cdd:cd03328 174 AARRAIgPDAELFVDANGAYSRKQALALARaFADEGVTWFEEPVSSDDLAGLRLVRERGpaGMDIAAGEYAYTLAYFRRL 253
|
170 180 190
....*....|....*....|....*....|....*.
gi 490533565 252 IELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQV 287
Cdd:cd03328 254 LEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDL 289
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
17-306 |
1.28e-13 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 70.81 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 17 KKPFKNSIET----LQERKFLIVEAIDTSGVTGWGEVSAFssPWYTEETIGTCLHMLKDFfiPNVVGREfnHPSEVPDSL 92
Cdd:PRK02714 11 QRPFRQPLQTahglWRIREGIILRLTDETGKIGWGEIAPL--PWFGSETLEEALAFCQQL--PGEITPE--QIFSIPDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 93 ArykgnrMAKAGLESAvwdiYAKKKGVSLAEALGGTRDKV--PAGvvvgLAPLDDmlkeIESYQKEGYQRIKIKI---QP 167
Cdd:PRK02714 85 P------ACQFGFESA----LENESGSRSNVTLNPLSYSAllPAG----EAALQQ----WQTLWQQGYRTFKWKIgvdPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 168 GQDVELVKAIRSRFPT-IPLMADANSSYELKDISRLKELDDYHLM----MIEQPLQADDIVDHRHLQKHLKTAICLDESI 242
Cdd:PRK02714 147 EQELKIFEQLLERLPAgAKLRLDANGGLSLEEAKRWLQLCDRRLSgkieFIEQPLPPDQFDEMLQLSQDYQTPIALDESV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490533565 243 CSVDDARRAIELGSCKIINIKPSRVGgltEALKIHDLCKEHHMQVWCGGMLETGISRAQNVALA 306
Cdd:PRK02714 227 ANLAQLQQCYQQGWRGIFVIKPAIAG---SPSRLRQFCQQHPLDAVFSSVFETAIGRKAALALA 287
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
30-360 |
5.12e-13 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 69.55 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 30 RKFLIVEAIDTSGVTGWG-------EVSAFSspwYteetigtclhmLKDFFIPNVVGREfnhPSEVPD---SLarYKG-- 97
Cdd:PRK15072 15 RNFVTLKITTDDGVTGLGdatlngrELAVAS---Y-----------LQDHVCPLLIGRD---AHRIEDiwqYL--YRGay 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 98 ------NRMAKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVpagVVVGLA---PLDDMLKEIESYQKEGYQriKIKIQ- 166
Cdd:PRK15072 76 wrrgpvTMSAIAAVDMALWDIKAKAAGMPLYQLLGGaSREGV---MVYGHAngrDIDELLDDVARHLELGYK--AIRVQc 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 167 --PGQDV------------------------------------ELVKAIRSRF-PTIPLMADANSSYELKDISRL-KELD 206
Cdd:PRK15072 151 gvPGLKTtygvskgkglayepatkgllpeeelwstekylrfvpKLFEAVRNKFgFDLHLLHDVHHRLTPIEAARLgKSLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 207 DYHLMMIEQPLQADDIVDHRHLQKHLKTAICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQ 286
Cdd:PRK15072 231 PYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 287 VWCGGmlETGISraqNVALA-------SLPQFtipgDISSSSRYWDE-DIVTP-DIRIDNGFISVSKQPGLGVEVNQDIM 357
Cdd:PRK15072 311 TGSHG--PTDLS---PVCMAaalhfdlWVPNF----GIQEYMGHSEEtLEVFPhSYTFEDGYLHPGDAPGLGVDFDEKLA 381
|
...
gi 490533565 358 RKY 360
Cdd:PRK15072 382 AKY 384
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
19-126 |
2.08e-11 |
|
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: 60.56 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 19 PFKNSIETLQERKFLIVEAIDTSGVTGWGEVSAFSSpwyTEETIGTCLHmlkDFFIPNVVGREFNHPSEVPDSLARY-KG 97
Cdd:pfam02746 15 PIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGG---RAETIKAILD---DHLAPLLIGRDAANISDLWQLMYRAaLG 88
|
90 100
....*....|....*....|....*....
gi 490533565 98 NRMAKAGLESAVWDIYAKKKGVSLAEALG 126
Cdd:pfam02746 89 NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
97-283 |
2.83e-10 |
|
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: 61.26 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 97 GNRMAKAG-LESAVWDIYAKKKGVSLAEALGG-TRDKVPAGVVVGLA------PLDDMLK---EIESYQKEGYQRIKIKI 165
Cdd:cd03326 104 GERAVAVGaLDMAVWDAVAKIAGLPLYRLLARrYGRGQADPRVPVYAaggyyyPGDDLGRlrdEMRRYLDRGYTVVKIKI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 166 QP---GQDVELVKAI------RSRfptipLMADANSSYELKD-ISRLKELDDYHLMMIEQPLQADDIVDHRHLQKHLKTA 235
Cdd:cd03326 184 GGaplDEDLRRIEAAldvlgdGAR-----LAVDANGRFDLETaIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGP 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490533565 236 ICLDESICSVDDARRAIELGSCK----IINIKPSRVGGLTEALKIHDLCKEH 283
Cdd:cd03326 259 IATGENLFSLQDARNLLRYGGMRpdrdVLQFDPGLSYGLPEYLRMLDVLEAH 310
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
100-351 |
2.92e-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: 58.12 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 100 MAKAGLESAVWDIYAKKKGVSL---------------------------AEALGGTRDK---------------VPAGVV 137
Cdd:cd03324 109 LATAAVVNAVWDLWAKAEGKPLwkllvdmtpeelvscidfryitdaltpEEALEILRRGqpgkaareadllaegYPAYTT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 138 -VG-LAPLDDMLKEI-ESYQKEGYQRIKIKI--QPGQDVELVKAIRSRF-PTIPLMADANSSYELKD-ISRLKELDDYHL 210
Cdd:cd03324 189 sAGwLGYSDEKLRRLcKEALAQGFTHFKLKVgaDLEDDIRRCRLAREVIgPDNKLMIDANQRWDVPEaIEWVKQLAEFKP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 211 MMIEQPLQADDIVDHRHLQKHLKTA---ICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEHHMQV 287
Cdd:cd03324 269 WWIEEPTSPDDILGHAAIRKALAPLpigVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPV 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490533565 288 W--CGGmletgisraqnVALASLPQFTIPGD---ISSSSR-----YWD---EDIVTPdIRIDNGFISVSKQPGLGVE 351
Cdd:cd03324 349 CphAGG-----------VGLCELVQHLSMIDyicVSGSKEgrvieYVDhlhEHFVYP-VVIQNGAYMPPTDPGYSIE 413
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
129-360 |
1.39e-06 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 129 RDKVPAGVVVGLAPLDDMLKEIESYQkeGYQRIKIKI-QPGQ----DVELVKAIRSRFPTIP-LMADANSSYELKD-ISR 201
Cdd:PRK02901 76 RDRVPVNATVPAVDAAQVPEVLARFP--GCRTAKVKVaEPGQtladDVARVNAVRDALGPDGrVRVDANGGWSVDEaVAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 202 LKELD-DYHLMMIEQPLQA-DDIVDHRHlQKHLKTAIclDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIHDL 279
Cdd:PRK02901 154 ARALDaDGPLEYVEQPCATvEELAELRR-RVGVPIAA--DESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDIAEQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 280 CKehhMQVWCGGMLETGISRAQNVALA-SLPQFTIPGDISSSSRYwDEDIVTPdIRIDNGFISVSKqpglgVEVNQDIMR 358
Cdd:PRK02901 231 IG---LPVVVSSALDTSVGIAAGLALAaALPELDHACGLATGGLF-EEDVADP-LLPVDGFLPVRR-----VTPDPARLA 300
|
..
gi 490533565 359 KY 360
Cdd:PRK02901 301 AL 302
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
101-283 |
6.09e-06 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 47.80 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 101 AKAGLESAVWDIYAKKKGVSLAEALGG-TRDKVpagVVVGLAPLDDMLKEIesyqkeGYQRIKIKIQPG---------QD 170
Cdd:PRK15440 124 TISCVDLALWDLLGKVRGLPVYKLLGGaVRDEL---QFYATGARPDLAKEM------GFIGGKMPLHHGpadgdaglrKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 171 VELVKAIRSRF-PTIPLMADANSSYELKDISRL-KELDDYHLMMIEQPLQADDIVDHRHLQKHLKTAICLD--ESICSVD 246
Cdd:PRK15440 195 AAMVADMREKVgDDFWLMLDCWMSLDVNYATKLaHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTsgEHEATLQ 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 490533565 247 DARRAIELGSCKIINIKPSRVGGLTEALKIHDLCKEH 283
Cdd:PRK15440 275 GFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKAR 311
|
|
| enolase |
cd03313 |
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of ... |
199-287 |
5.19e-05 |
|
Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.
Pssm-ID: 239429 [Multi-domain] Cd Length: 408 Bit Score: 44.78 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 199 ISRLKEL-DDYHLMMIEQPLQADDIVDHRHLQKHL--KTAICLDESICS-VDDARRAIELGSCKIINIKPSRVGGLTEAL 274
Cdd:cd03313 267 IDYYKELvKKYPIVSIEDPFDEDDWEGWAKLTAKLgdKIQIVGDDLFVTnPERLKKGIEKKAANALLIKVNQIGTLTETI 346
|
90
....*....|...
gi 490533565 275 KIHDLCKEHHMQV 287
Cdd:cd03313 347 EAIKLAKKNGYGV 359
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
102-368 |
3.77e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 42.54 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 102 KAGLESAVWDIYAKKKGVSLAEALGGTRDKVPA----GVVVGLAPLDDMLKEIE------SYQKEGYQRIKIKI----QP 167
Cdd:PLN02980 1040 RCGLEMAILNAIAVRHGSSLLNILDPYQKDENGseqsHSVQICALLDSNGSPLEvayvarKLVEEGFSAIKLKVgrrvSP 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 168 GQDVELVKAIRSRFP-TIPLMADANS--SYE--LKDISRLKELDdyhLMMIEQPLQADDIVDHRHLQKHLKTAicLDESI 242
Cdd:PLN02980 1120 IQDAAVIQEVRKAVGyQIELRADANRnwTYEeaIEFGSLVKSCN---LKYIEEPVQDEDDLIKFCEETGLPVA--LDETI 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 243 -----CSVDDARRAIELGSCKIInIKPSRVGGLTEALKIHDLCKEHHMQVWCGGMLETGISRA-----------QNVALA 306
Cdd:PLN02980 1195 dkfeeCPLRMLTKYTHPGIVAVV-IKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSayiqfasylemQNAKAS 1273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490533565 307 SLPQFTIPGDIS---SSSRYWDEDIVTPDIRI----DNGFISVSKQPGLG----VEVNQDIMRKYVTKMDVFT 368
Cdd:PLN02980 1274 REMNKGTCPSVAhglGTYRWLKEDVTMNPLGIfrspYSGFIEASVADASRnlqkFQINNDVIVRTFKEEQVRT 1346
|
|
| Enolase_C |
pfam00113 |
Enolase, C-terminal TIM barrel domain; |
114-282 |
3.90e-04 |
|
Enolase, C-terminal TIM barrel domain;
Pssm-ID: 395063 Cd Length: 296 Bit Score: 41.70 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 114 AKKKGVSLAEALGGTRdkvpagvvvGLAPLDDMLKE-----IESYQKEGYqriKIKIQPGQDV---ELVKAIRSRFP--- 182
Cdd:pfam00113 55 LKAKYGQSATNVGDEG---------GFAPNLQSNKEaldliVEAIEKAGY---KGKIKIAMDVassEFYNKKDGKYDldf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 183 --TIPLMADANSSYELKDIsrLKEL-DDYHLMMIEQPLQADDIVDHRHLQKHLKTAICL---DESICSVDDARRAIELGS 256
Cdd:pfam00113 123 kgEKSDKSKKLTSAQLADL--YEELvKKYPIVSIEDPFDEDDWEAWKYLTERLGDKVQIvgdDLTVTNPKRLKTAIEKKI 200
|
170 180
....*....|....*....|....*.
gi 490533565 257 CKIINIKPSRVGGLTEALKIHDLCKE 282
Cdd:pfam00113 201 ANALLLKVNQIGSLTESIAAVKMAKD 226
|
|
| MAL |
cd03314 |
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ... |
207-315 |
4.41e-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: 42.00 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 207 DYHLMmIEQPLQADD----IVDHRHLQKHLKTA-----ICLDESICSVDDARRAIELGSCKIINIKPSRVGGLTEALKIH 277
Cdd:cd03314 227 PFPLR-IEGPMDAGSreaqIERMAALRAELDRRgvgvrIVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGGIDNTIDAV 305
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90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490533565 278 DLCKEHHMQVWCGGML-ETGIS--RAQNVALASLPQFTI--PG 315
Cdd:cd03314 306 LYCKEHGVGAYLGGSCnETDISarVTVHVALATRADQMLakPG 348
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| eno |
PRK00077 |
enolase; Provisional |
141-285 |
1.18e-03 |
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enolase; Provisional
Pssm-ID: 234617 [Multi-domain] Cd Length: 425 Bit Score: 40.46 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 141 APLDDMLKEIEsyqKEGYQrikikiqPGQDVELvkAIrsrfptiplmaDANSS-------YELKD--------ISRLKEL 205
Cdd:PRK00077 217 EALDLILEAIE---KAGYK-------PGEDIAL--AL-----------DCAASefykdgkYVLEGegltseemIDYLAEL 273
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490533565 206 -DDYHLMMIEQPLQADDIVDHRHLQKHL--KTAICLDESICS-VDDARRAIELGSCKIINIKPSRVGGLTEALKIHDLCK 281
Cdd:PRK00077 274 vDKYPIVSIEDGLDENDWEGWKLLTEKLgdKVQLVGDDLFVTnTKRLKKGIEKGAANSILIKVNQIGTLTETLDAIELAK 353
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....
gi 490533565 282 EHHM 285
Cdd:PRK00077 354 RAGY 357
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