|
Name |
Accession |
Description |
Interval |
E-value |
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
22-386 |
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: 526.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 22 QIEAIETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGESITPCGPWWSGDSVEAIQATINHYLAPLVVGEPA 101
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 102 LDASRIMAKLHGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGKAG 181
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGRHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 182 AFKLKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARS 261
Cdd:cd03318 161 RFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 262 MLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPY 341
Cdd:cd03318 241 PIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLPF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1756170442 342 GGEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRR 386
Cdd:cd03318 321 GCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
23-389 |
6.11e-122 |
|
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: 357.57 E-value: 6.11e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGESITPCGPWWSGDSVEAIQATINHYLAPLVVGEPAL 102
Cdd:TIGR02534 1 IQSVETILVDVPTIRPHKLATTTMTEQTLVLVRIRTEDGVIGYGEGTTIGGLWWGGESPETIKANIDTYLAPVLVGRDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 103 DASRIMAKLHGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGKAGA 182
Cdd:TIGR02534 81 EIAAIMADLEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEKRHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 183 FKLKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSM 262
Cdd:TIGR02534 161 FKLKIGARDPADDVAHVVAIAKALGDRASVRVDVNAAWDERTALHYLPQLADAGVELIEQPTPAENREALARLTRRFNVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 263 LLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPYG 342
Cdd:TIGR02534 241 IMADESVTGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATFPALSFG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1756170442 343 GEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRRFAR 389
Cdd:TIGR02534 321 TELFGPLLLKDEILTEPLQYEDFQLHLPQGPGLGVEVDEDKVNFYRR 367
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
23-387 |
5.92e-101 |
|
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: 303.67 E-value: 5.92e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGEsitpCGPWWSGdsVEAIQATINHYLAPLVVGEPAL 102
Cdd:COG4948 3 ITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGE----AVPGGTG--AEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 103 DASRIMAKLHGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGkAGA 182
Cdd:COG4948 77 DIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARG-FRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 183 FKLKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSM 262
Cdd:COG4948 156 LKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 263 LLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPYg 342
Cdd:COG4948 236 IAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDI- 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1756170442 343 GEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRRF 387
Cdd:COG4948 315 VELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 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 ... |
25-335 |
1.54e-57 |
|
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: 190.48 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 25 AIETVIVDLPLRRIQQFARlGAK-HQSSVLIRLHTkGGIVGIGESiTPcGPWWSGDSVEAIQATINHYLAPLVVGEPALD 103
Cdd:cd03319 1 KISLRPERLPLKRPFTIAR-GSRtEAENVIVEIEL-DGITGYGEA-AP-TPRVTGETVESVLAALKSVRPALIGGDPRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 104 asRIMAKLHGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGkAGAF 183
Cdd:cd03319 77 --KLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRG-FPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 184 KLKMGaLPLAQDLRRALAIAKELeGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSML 263
Cdd:cd03319 154 KIKLG-GDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1756170442 264 LIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAAS 335
Cdd:cd03319 232 MADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAA 303
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
26-344 |
3.04e-56 |
|
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: 185.62 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 26 IETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGESitpcgpwwsgdsveaiqatinhylaplvvgepaldas 105
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEA------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 106 rimaklhgrvagnafAKAGIEMALLDAVGKIVDAPIhVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGkAGAFKL 185
Cdd:cd03315 44 ---------------TKAAVDMALWDLWGKRLGVPV-YLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAG-FRTFKL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 186 KMGAlPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLI 265
Cdd:cd03315 107 KVGR-DPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMA 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756170442 266 DEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPYGGE 344
Cdd:cd03315 186 DESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGE 264
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
166-381 |
9.53e-46 |
|
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: 156.57 E-value: 9.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 166 QEVDEAFRMLEAGKAGAFKLKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVA 245
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 246 RWNLDAMARIHRQARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFlETSIG 325
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPIG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1756170442 326 TAANMQLAASIESLPYGGEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDE 381
Cdd:pfam13378 160 LAASLHLAAAVPNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
23-377 |
5.32e-44 |
|
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: 156.23 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIETVIVDLPLRRIQQfarlGAKHQSSVLIRLHTKGGIVGIGESitpcgpwWSGDSVEAIQATINHYLAPLVVGEPAL 102
Cdd:cd03316 2 ITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGEA-------YPGGRPSAVAAAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 103 DASRIMAKL------HGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVawpLATG-----DVNQEVDEA 171
Cdd:cd03316 71 DIERLWEKLyrrlfwRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRV---YASGggyddSPEELAEEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 172 FRMLEAGkAGAFKLKMGALP-----LAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVAR 246
Cdd:cd03316 148 KRAVAEG-FTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 247 WNLDAMARIHRQARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGM----HVYMGtflet 322
Cdd:cd03316 227 DDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVrvapHGAGG----- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1756170442 323 SIGTAANMQLAASIESLPYGGEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGI 377
Cdd:cd03316 302 PIGLAASLHLAAALPNFGILEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGV 356
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
26-386 |
1.02e-39 |
|
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: 144.68 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 26 IETVIVDLPLRRIQQ--FARLGAKHqsSVLIRLHTKGGIVGIGESITPCGPWWSGDSVEAIQATINHYLAPLVVGEPALD 103
Cdd:cd03317 1 IELFHVRMPLKFPFEtsFGTLNERE--FLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 104 ASRIMAKLhGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLGGRfRDRLSVAwpLATG---DVNQEVDEAFRMLEAGkA 180
Cdd:cd03317 79 PEEVSERL-APIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVG--VSIGiqdDVEQLLKQIERYLEEG-Y 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 181 GAFKLKM----GALPLAQdLRRALaiakeleGKASLRVDPNEAWdEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIH 256
Cdd:cd03317 154 KRIKLKIkpgwDVEPLKA-VRERF-------PDIPLMADANSAY-TLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 257 RQARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAasi 336
Cdd:cd03317 225 KLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALA--- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1756170442 337 eSLP---YGGEVIGP-LLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRR 386
Cdd:cd03317 302 -SLPnftYPGDISASsRYFEEDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
26-335 |
1.21e-29 |
|
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: 114.35 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 26 IETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGEsitpcgpwwsgdsveaiqatinhylaplvvgepaldas 105
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 106 rimaklhgrvagnafAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLsvawplatgdvnqevdeafrmleagkagafkl 185
Cdd:cd00308 43 ---------------VISGIDMALWDLAAKALGVPLAELLGGGSRDRV-------------------------------- 75
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 186 kmgalPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLI 265
Cdd:cd00308 76 -----PAYGSIERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 266 DEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAAS 335
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAA 220
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
121-341 |
5.19e-26 |
|
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: 105.42 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 121 AKAGIEMALLDAVGKIVDAPihvllggRFRDRLSVAWPLATGDVnQEVDEAfRMLEAGKAGAFKLKMGALPLAQDLRRAL 200
Cdd:cd03320 48 LAFGIESALANLEALLVGFT-------RPRNRIPVNALLPAGDA-AALGEA-KAAYGGGYRTVKLKVGATSFEEDLARLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 201 AIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLliDEGVQSLHDASEVVK 280
Cdd:cd03320 119 ALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGVPIAL--DESLRRLDDPLALAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756170442 281 RAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPY 341
Cdd:cd03320 197 AGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPA 257
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
52-389 |
2.92e-22 |
|
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: 97.39 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLHTKGGIVGIGESitPCGpwwsGDSVEAIQATINHYLAPLVVGE--PALDASRIMAKLHG-----------RVAGN 118
Cdd:cd03323 31 NIVELTDDNGNTGVGES--PGG----AEALEALLEAARSLVGGDVFGAylAVLESVRVAFADRDaggrglqtfdlRTTVH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 119 AFAkaGIEMALLDAVGKIVDAPIHVLLGGRFRDRL------------------SVAWPLATG---DVNQEVDEAFRMLEA 177
Cdd:cd03323 105 VVT--AFEVALLDLLGQALGVPVADLLGGGQRDSVpflaylfykgdrhktdlpYPWFRDRWGealTPEGVVRLARAAIDR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 178 GKAGAFKLKMGALPLAQDLRRALAIAKELEGkASLRVDPNEAWDEPTTMRALAPLEAAgVEIIEQPVArwNLDAMARIHR 257
Cdd:cd03323 183 YGFKSFKLKGGVLPGEEEIEAVKALAEAFPG-ARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDPCG--GREGMAEFRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 258 QARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIE 337
Cdd:cd03323 259 ATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAAP 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1756170442 338 SLPYGGEVIGPLLIEEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRRFAR 389
Cdd:cd03323 339 GLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHE 390
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
23-387 |
5.89e-22 |
|
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: 96.01 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIETVIVDLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGigESITPCGPWWSGDSVEAIQATinhyLAPLVVGEPAL 102
Cdd:cd03321 3 ITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTG--HSYLFTYTPAALKSLKQLLDD----MAALLVGEPLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 103 DASrIMAKLHGR--VAGNA----FAKAGIEMALLDAVGKIVDAPIHVLLGGRFRdrlsvawPLAT------GDVNQEVDE 170
Cdd:cd03321 77 PAE-LERALAKRfrLLGYTglvrMAAAGIDMAAWDALAKVHGLPLAKLLGGNPR-------PVQAydshglDGAKLATER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 171 AFRMLEAGKAGAfKLKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLD 250
Cdd:cd03321 149 AVTAAEEGFHAV-KTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 251 AMARIHRQARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANM 330
Cdd:cd03321 228 GHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVT 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1756170442 331 QLAASIESLPYGGEVIGPLLIEEDLCEVPavykehalwlPEGPGLGIRLDENQVRRF 387
Cdd:cd03321 308 PTAHWLEYVDWAGAILEPPLKFEDGNAVI----------PDEPGNGIIWREKAVRKY 354
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
52-380 |
4.45e-18 |
|
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: 84.68 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLHTKGGIVGIGESITPcgpwWSGDSVEAIQATINHYLaplvVGEPALDASRIMAKL--HGRVAGNAF---AKAGIE 126
Cdd:cd03325 15 LFVKIETDEGVVGWGEPTVE----GKARTVEAAVQELEDYL----IGKDPMNIEHHWQVMyrGGFYRGGPVlmsAISGID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 127 MALLDAVGKIVDAPIHVLLGGRFRDRLSV-AWplATGDVNQEVDEAFRMLEAgkAGAFKLKMGALPLAQDLRRALAIAKE 205
Cdd:cd03325 87 QALWDIKGKVLGVPVHQLLGGQVRDRVRVySW--IGGDRPSDVAEAARARRE--AGFTAVKMNATEELQWIDTSKKVDAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 206 LEGKASLR----------VDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLIDEGVQSLHDA 275
Cdd:cd03325 163 VERVAALReavgpdidigVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 276 SEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGM----HVYMGtfletSIGTAANMQLAASI-------ESL----P 340
Cdd:cd03325 243 KELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDValapHCPLG-----PIALAASLHVDASTpnfliqeQSLgihyN 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1756170442 341 YGGEVIGPLLIEEDLCEVPAVYKehalwLPEGPGLGIRLD 380
Cdd:cd03325 318 EGDDLLDYLVDPEVFDMENGYVK-----LPTGPGLGIEID 352
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
49-380 |
5.03e-18 |
|
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: 84.31 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 49 QSSVLIRLHTKGGIVGIGESITPCGPWWSgdsveaiqatINHYLAPLVVGEPALDASRIMAKLH------GRVAGNAFAK 122
Cdd:cd03327 9 VGWLFVEIETDDGTVGYANTTGGPVACWI----------VDQHLARFLIGKDPSDIEKLWDQMYratlayGRKGIAMAAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 123 AGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSV-AWPLATGDVNQEVDEAFRMLEAGKAGaFKLKMGALPL--AQDLRRA 199
Cdd:cd03327 79 SAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAyASGLYPTDLDELPDEAKEYLKEGYRG-MKMRFGYGPSdgHAGLRKN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 200 LAIAKELEGKAS----LRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLIDEGVQSLHDA 275
Cdd:cd03327 158 VELVRAIREAVGydvdLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 276 SEVVKRAAAGLVSLKIMKTGGMRPAR---AMAD------IANAGGMHVYMgtfletSIGTAANMQLAasiESLP-----Y 341
Cdd:cd03327 238 KRLLEGRAVDILQPDVNWVGGITELKkiaALAEaygvpvVPHASQIYNYH------FIMSEPNSPFA---EYLPnspdeV 308
|
330 340 350
....*....|....*....|....*....|....*....
gi 1756170442 342 GGEVIGPLLIEEdlcevPAVYKEHaLWLPEGPGLGIRLD 380
Cdd:cd03327 309 GNPLFYYIFLNE-----PVPVNGY-FDLSDKPGFGLELN 341
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
25-146 |
8.88e-18 |
|
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: 78.67 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 25 AIETVIV-DLPLRRIQQFARLGAKHQSSVLIRLHTKGGIVGIGEsitpCGPWwsGDSVEAIQATINHYLAPLVVGEPALD 103
Cdd:pfam02746 1 AIEVFVVdVGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGE----ATSY--GGRAETIKAILDDHLAPLLIGRDAAN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1756170442 104 ASRIMAKLHGRVAGNAFAKAGIEMALLDAVGKIVDAPIHVLLG 146
Cdd:pfam02746 75 ISDLWQLMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
23-387 |
3.25e-17 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 82.10 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIEtVIVDLPLRRIqqfarlgakhqssVLIRLHTKGGIVGIGESITPCGPwwsgdsvEAIQATINHYLAPLVVGEpal 102
Cdd:cd03322 2 ITAIE-VIVTCPGRNF-------------VTLKITTDQGVTGLGDATLNGRE-------LAVKAYLREHLKPLLIGR--- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 103 DASRIMAKLH----------GRVAGNAFAkaGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAF 172
Cdd:cd03322 58 DANRIEDIWQylyrgaywrrGPVTMNAIA--AVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 173 RMLEAGkagaFK-LKMGALPLAQDLRRALAIAKELEGKASLRVDPNEAwdepttMRALAPLEAAGVEIIEQPVARWNLDA 251
Cdd:cd03322 136 RHLAQG----YRaIRVQLPKLFEAVREKFGFEFHLLHDVHHRLTPNQA------ARFGKDVEPYRLFWMEDPTPAENQEA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 252 MARIHRQARSMLLIDEGVQSLHDASEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVYM-GTFLETSIGTAANM 330
Cdd:cd03322 206 FRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWhGPTDLSPVGMAAAL 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756170442 331 QL------AASIESLPYGGEVigpllieEDLCEVPAVYKEHALWLPEGPGLGIRLDENQVRRF 387
Cdd:cd03322 286 HLdlwvpnFGIQEYMRHAEET-------LEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKF 341
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
168-260 |
2.27e-16 |
|
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: 73.85 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 168 VDEAFRMLEAGKAGAFKLKMGAlPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARW 247
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPD 83
|
90
....*....|...
gi 1756170442 248 NLDAMARIHRQAR 260
Cdd:smart00922 84 DLEGLAELRRATP 96
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
191-361 |
5.32e-16 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 78.09 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 191 PLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAG-VEIIEQPVArwNLDAMARIHRQARSMLLIDEGV 269
Cdd:PRK02901 116 TLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGpLEYVEQPCA--TVEELAELRRRVGVPIAADESI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 270 QSLHDASEVVKRAAAGLVSLKIMKTGGMrpaRAMADIANAGGMHVYMGTFLETSIGTAANMQLAASIESLPYG------- 342
Cdd:PRK02901 194 RRAEDPLRVARAGAADVAVLKVAPLGGV---RAALDIAEQIGLPVVVSSALDTSVGIAAGLALAAALPELDHAcglatgg 270
|
170 180
....*....|....*....|..
gi 1756170442 343 ---GEVIGPLLIEEDLCEVPAV 361
Cdd:PRK02901 271 lfeEDVADPLLPVDGFLPVRRV 292
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
23-380 |
1.02e-13 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 72.04 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 23 IEAIETVIVDLPLRRIQQFAR---LGAKHQSSV-LIRLHTKGGIVGigESITPcGPWWSGDSVEAiqatinhYLAPLVVG 98
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGhhhPGPAGTRKLaLLTIETDEGAKG--HAFGG-RPVTDPALVDR-------FLKKVLIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 99 EPALDASRIMAKLHGRVAGNAFAKAG-IEMALLDAVGKIVDAPIHVLLGGrFRDRLSVAWPLATGD-------VNQEVDE 170
Cdd:cd03329 72 QDPLDRERLWQDLWRLQRGLTDRGLGlVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDdleglesPEAYADF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 171 AFRMLEAGKAgAFKLKMGALP-LAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNL 249
Cdd:cd03329 151 AEECKALGYR-AIKLHPWGPGvVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 250 DAMARIHRQARSMLLIDEGVQSLHDA-SEVVKRAAAGLVSLKIMKTGGMRPARAMADIANAGGMHVymgtflETSIGTAA 328
Cdd:cd03329 230 SSYRWLAEKLDIPILGTEHSRGALESrADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDV------ELHGNGAA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756170442 329 NMQLAASI------------ESLPYGGEVIGPLLIEEDlcevpaVYKEHALWLPEGPGLGIRLD 380
Cdd:cd03329 304 NLHVIAAIrntryyergllhPSQKYDVYAGYLSVLDDP------VDSDGFVHVPKGPGLGVEID 361
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
52-389 |
1.22e-11 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 65.69 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLHTKGGIVGIGESItpcgpwwSGDSVEAIQATInHYLAPLVVGEPALDASRIMAKLH-------GRVAGNAFAkaG 124
Cdd:PRK14017 16 LFLKIETDEGIVGWGEPV-------VEGRARTVEAAV-HELADYLIGKDPRRIEDHWQVMYrggfyrgGPILMSAIA--G 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 125 IEMALLDAVGKIVDAPIHVLLGGRFRDRLSV-AWplATGDVNQEVDEAFRmlEAGKAGAFKLKMGALPLAQDLRRALAIA 203
Cdd:PRK14017 86 IDQALWDIKGKALGVPVHELLGGLVRDRIRVySW--IGGDRPADVAEAAR--ARVERGFTAVKMNGTEELQYIDSPRKVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 204 KELEGKASLR----------VDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLIDEGVQSLH 273
Cdd:PRK14017 162 AAVARVAAVReavgpeigigVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 274 DASEVVKRAAAGLVSLKIMKTGGMRPAR---AMA---DIANAggMHVYMGtfletSIGTAANMQLAASI-------ESLP 340
Cdd:PRK14017 242 DFKRVLEAGGVDIIQPDLSHAGGITECRkiaAMAeayDVALA--PHCPLG-----PIALAACLQVDAVSpnafiqeQSLG 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1756170442 341 YGGEVIGPLLieeDLCEVPAV--YKEHALWLPEGPGLGIRLDENQVRRFAR 389
Cdd:PRK14017 315 IHYNQGADLL---DYVKNKEVfaYEDGFVAIPTGPGLGIEIDEAKVRERAK 362
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
119-303 |
4.76e-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: 60.87 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 119 AFAKAGIEMALLDAVGKIVDAPIHVLLGGRFRD-----RLSV----AWPLATGDVNQEVDEAFRMLEAGKAgAFKLKMGA 189
Cdd:cd03326 107 AVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRgqadpRVPVyaagGYYYPGDDLGRLRDEMRRYLDRGYT-VVKIKIGG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 190 LPLAQDLRRALAIAKELEGKASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLIDEGV 269
Cdd:cd03326 186 APLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPIATGENL 265
|
170 180 190
....*....|....*....|....*....|....
gi 1756170442 270 QSLHDASEVVkraaaglvslkimKTGGMRPARAM 303
Cdd:cd03326 266 FSLQDARNLL-------------RYGGMRPDRDV 286
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
52-259 |
2.74e-09 |
|
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: 58.19 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLHTkGGIVGIGesitpcgpWWSGDSveAIQATINHYLAPLVVGEPALDA----SRIMAKLH--GRVAGNAFAKAGI 125
Cdd:cd03328 31 VLVEVRA-GGRTGLG--------YTYADA--AAAALVDGLLAPVVEGRDALDPpaawEAMQRAVRnaGRPGVAAMAISAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 126 EMALLDAVGKIVDAPIHVLLgGRFRDRLSVawpLATGDVNQEVDEAFRMLEAGKAG----AFKLKMGALPlAQDLRRaLA 201
Cdd:cd03328 100 DIALWDLKARLLGLPLARLL-GRAHDSVPV---YGSGGFTSYDDDRLREQLSGWVAqgipRVKMKIGRDP-RRDPDR-VA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1756170442 202 IAKELEGK-ASLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQA 259
Cdd:cd03328 174 AARRAIGPdAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERG 232
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
52-334 |
3.45e-09 |
|
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: 57.51 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLhTKGGIVGIGEsITPCgPWWSGDSVEaiQATinHYLAPLVVGEPALDASRIMAKLhgrvAGNAFakaGIEMALLd 131
Cdd:TIGR01927 24 LIVRL-TDEGRTGWGE-IAPL-PGFGTETLA--EAL--DFCRALIEEITRGDIEAIDDQL----PSVAF---GFESALI- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 132 AVGKIVDAPIhvllggrfrDRLSVAWPLATGDVNqevDEAFRMLEAGKAGAFKLKMGALPLAQDLRRALAIAKELEGKAS 211
Cdd:TIGR01927 89 ELESGDELPP---------ASNYYVALLPAGDPA---LLLLRSAKAEGFRTFKWKVGVGELAREGMLVNLLLEALPDKAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 212 LRVDPNEAWDEPTT---MRALAPLEAAGVEIIEQPVArwNLDAMARIHRQARSMLLIDEGVQSLHDASEVVKRAAAGLVS 288
Cdd:TIGR01927 157 LRLDANGGLSPDEAqqfLKALDPNLRGRIAFLEEPLP--DADEMSAFSEATGTAIALDESLWELPQLADEYGPGWRGALV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1756170442 289 LKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAA 334
Cdd:TIGR01927 235 IKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAA 280
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
50-335 |
2.14e-06 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 49.24 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 50 SSVLIRLHTKGGIVGIGEsITPCgPWWSGDSVEAIQAtINHYLAPLVVGEpaldasrIMAKLHGRVAGNAFakaGIEMAL 129
Cdd:PRK02714 29 EGIILRLTDETGKIGWGE-IAPL-PWFGSETLEEALA-FCQQLPGEITPE-------QIFSIPDALPACQF---GFESAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 130 LDAVG-----KIVDAPIHVLLGgrfrdrlsvawplaTGdvnQEVDEAFRMLEAGKAGAFKLKMGALPLAQDLRRALAIAK 204
Cdd:PRK02714 96 ENESGsrsnvTLNPLSYSALLP--------------AG---EAALQQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 205 ELEGKASLRVDPNEAWDEPTTMRALAPLEAAG---VEIIEQPVARWNLDAMARIHRQARSMLLIDEGVQSLHDASEVVKR 281
Cdd:PRK02714 159 RLPAGAKLRLDANGGLSLEEAKRWLQLCDRRLsgkIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVANLAQLQQCYQQ 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1756170442 282 AAAGLVslkIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLAAS 335
Cdd:PRK02714 239 GWRGIF---VIKPAIAGSPSRLRQFCQQHPLDAVFSSVFETAIGRKAALALAAE 289
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
45-333 |
3.22e-04 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 42.43 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 45 GAKHQSSVLIRLHTKGGIVGIGEsitpCGPWWS-GDSVEAIQATInhylAPLVvgePALDASRIMAKLHGRVAGNAfAKA 123
Cdd:PRK15129 22 GSRSEARVVVVELEEEGIKGTGE----CTPYPRyGESDASVMAQI----MSVV---PQLEKGLTREALQKLLPAGA-ARN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 124 GIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWPLATGDVNQEVDEAFRMLEAGkAGAFKLKMGALPLAQdlrRALAIA 203
Cdd:PRK15129 90 AVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAG-AKLLKVKLDNHLISE---RMVAIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 204 KELEgKASLRVDPNEAWdEPTTMRALAPLEA-AGVEIIEQPVARWNLDAMAR-IHRQArsmLLIDEGVQSLHDASEVVKR 281
Cdd:PRK15129 166 SAVP-DATLIVDANESW-RAEGLAARCQLLAdLGVAMLEQPLPAQDDAALENfIHPLP---ICADESCHTRSSLKALKGR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1756170442 282 AAagLVSLKIMKTGGMRPARAMADIANAGGMHVYMGTFLETSIGTAANMQLA 333
Cdd:PRK15129 241 YE--MVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLV 290
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
52-178 |
3.28e-04 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 42.59 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 52 VLIRLHTKGGIVGIGEsitpcgpwwsgdsveaiqATIN-----------HYLAPLVVGEpalDASRI------------- 107
Cdd:PRK15072 18 VTLKITTDDGVTGLGD------------------ATLNgrelavasylqDHVCPLLIGR---DAHRIediwqylyrgayw 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1756170442 108 ------MAklhgrvagnafAKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVaWPLATG-DVNQEVDEAFRMLEAG 178
Cdd:PRK15072 77 rrgpvtMS-----------AIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMV-YGHANGrDIDELLDDVARHLELG 142
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
122-337 |
4.68e-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: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 122 KAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVAWP-----LATGDVN---QEVDEAFRMLEAGKAGAFKLKMG----- 188
Cdd:PLN02980 1040 RCGLEMAILNAIAVRHGSSLLNILDPYQKDENGSEQShsvqiCALLDSNgspLEVAYVARKLVEEGFSAIKLKVGrrvsp 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 189 ---ALPLaQDLRRALAIAKElegkasLRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVArwNLDAMARIHRQARSMLLI 265
Cdd:PLN02980 1120 iqdAAVI-QEVRKAVGYQIE------LRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQ--DEDDLIKFCEETGLPVAL 1190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756170442 266 DEGVQSLHDA--SEVVKRAAAGLVSLKIMKT--GGMRPARAMADIANA-GGMHVYMGTFlETSIGTAANMQLAASIE 337
Cdd:PLN02980 1191 DETIDKFEECplRMLTKYTHPGIVAVVIKPSvvGGFENAALIARWAQQhGKMAVISAAY-ESGLGLSAYIQFASYLE 1266
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
169-243 |
1.18e-03 |
|
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: 40.79 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 169 DEAFRML--EAGKAG--AFKLKMGAlPLAQDLRRaLAIAKELEGKA-SLRVDPNEAWDEP---TTMRALAPLEAAgveII 240
Cdd:cd03324 197 DEKLRRLckEALAQGftHFKLKVGA-DLEDDIRR-CRLAREVIGPDnKLMIDANQRWDVPeaiEWVKQLAEFKPW---WI 271
|
...
gi 1756170442 241 EQP 243
Cdd:cd03324 272 EEP 274
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
121-386 |
7.11e-03 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 38.17 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 121 AKAGIEMALLDAVGKIVDAPIHVLLGGRFRDRLSVawpLATGdvnQEVDEAFRMLEAGkaGAFKLKMGALPLAQDLRRAL 200
Cdd:PRK15440 124 TISCVDLALWDLLGKVRGLPVYKLLGGAVRDELQF---YATG---ARPDLAKEMGFIG--GKMPLHHGPADGDAGLRKNA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 201 AIAKELEGKAS----LRVDPNEAWDEPTTMRALAPLEAAGVEIIEQPVARWNLDAMARIHRQARSMLLIDEGVqslHDAS 276
Cdd:PRK15440 196 AMVADMREKVGddfwLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGE---HEAT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756170442 277 EVVKRAAAGLVSLKIMK-----TGGMRPARAMADIANAGGM----H---VYMGTFletsIGTAANMQLAASIESLPYGGE 344
Cdd:PRK15440 273 LQGFRTLLEMGCIDIIQpdvgwCGGLTELVKIAALAKARGQlvvpHgssVYSHHF----VITRTNSPFSEFLMMSPDADT 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1756170442 345 VI---GPLLIEEdlcEVPAVYKEHALWLpEGPGLGIRLD-ENQVRR 386
Cdd:PRK15440 349 VVpqfDPILLDE---PVPVNGRIHKSVL-DKPGFGVELNrDCNLKR 390
|
|
| |
