|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-361 |
9.80e-144 |
|
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: 411.52 E-value: 9.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 1 MKITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVAddhvTGESWESTFHTLKHTLAPALIGKNPM 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVP----GGTGAEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 81 NIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKGYQSF 160
Cdd:COG4948 77 DIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 161 KMKVGT-NVKEDVKRIEAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLP 239
Cdd:COG4948 157 KLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAW-TLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 240 LMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSV 319
Cdd:COG4948 236 IAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627130 320 ELTGPLKFTKDI--GNLHYDVPFIRLNEKPGLGIEINEDTLQEL 361
Cdd:COG4948 316 ELDGPLLLADDLveDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
5-327 |
7.92e-130 |
|
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: 374.60 E-value: 7.92e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 5 AIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDeGIIGYGEGVADDHVTGESWESTFHTLKHtLAPALIGKNPMnIEK 84
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKS-VRPALIGGDPR-LEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 85 IHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKGYQSFKMKV 164
Cdd:cd03319 78 LLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 165 GTNVKEDVKRIEAVRERVGnDIAIRVDVNQGWKNsANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDE 244
Cdd:cd03319 158 GGDLEDDIERIRAIREAAP-DARLRVDANQGWTP-EEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 245 GLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKkiITSVELTGP 324
Cdd:cd03319 236 SCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAK--ADFVDLDGP 313
|
...
gi 446627130 325 LKF 327
Cdd:cd03319 314 LLL 316
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-358 |
1.08e-83 |
|
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: 258.79 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGV--ADDHVTGESWESTFHTLKHTLAPALIGKNP 79
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATtpGGPAWGGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 80 MNIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKG-YQ 158
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 159 SFKMKVGTN-VKEDVKRIEAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKID 237
Cdd:cd03318 161 RFKLKMGARpPADDLAHVEAIAKALGDRASVRVDVNQAW-DESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 238 LPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIIT 317
Cdd:cd03318 240 VPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627130 318 -SVELTGPLKFTKDIGN--LHYDVPFIRLNEKPGLGIEINEDTL 358
Cdd:cd03318 320 fGCELFGPLLLAEDLLEepLAYRDGELHVPTGPGLGVRLDEDKV 363
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-352 |
5.30e-79 |
|
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: 246.37 E-value: 5.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLRNPFvisyGSYSDMPSIIVKMETDEGIIGYGEGVaddhvTGESWESTFHTLKHTLAPALIGKNPMN 81
Cdd:cd03316 1 KITDVETFVLRVPLPEPG----GAVTWRNLVLVRVTTDDGITGWGEAY-----PGGRPSAVAAAIEDLLAPLLIGRDPLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 82 IEKI-HDMMDNTIYG-----VPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHV--THVLSIADPEDMAEEAASMI 153
Cdd:cd03316 72 IERLwEKLYRRLFWRgrggvAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVyaSGGGYDDSPEELAEEAKRAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 154 QKGYQSFKMKVG------TNVKEDVKRIEAVRERVGNDIAIRVDVNQGW-KNSAntLTALRSLGHLNIDWIEQPVIADDI 226
Cdd:cd03316 152 AEGFTAVKLKVGgpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWdLAEA--IRLARALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 227 DAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMvESSVASSAG 306
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGA-GGPIGLAAS 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446627130 307 FHVAFSKKIITSVELTGPLKFTKDIGNLHYDVP---FIRLNEKPGLGIE 352
Cdd:cd03316 309 LHLAAALPNFGILEYHLDDLPLREDLFKNPPEIedgYVTVPDRPGLGVE 357
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
6-317 |
9.55e-70 |
|
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: 219.52 E-value: 9.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 6 IHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGvaddhvtgeswestfhtlkhtlapaligknpmnieki 85
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEA------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 86 hdmmdntiygvptAKAAIDIACFDIMGKKLNQPVYQLiGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKGYQSFKMKVG 165
Cdd:cd03315 44 -------------TKAAVDMALWDLWGKRLGVPVYLL-LGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 166 TNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSAnTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDEG 245
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQ-AIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADES 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446627130 246 LKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIIT 317
Cdd:cd03315 189 AFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVT 260
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
144-356 |
1.17e-61 |
|
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: 197.02 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 144 DMAEEAASMI-QKGYQSFKMKVGTN-VKEDVKRIEAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQPV 221
Cdd:pfam13378 1 ELAAEARRAVeARGFRAFKLKVGGPdPEEDVERVRAVREAVGPGVDLMVDANGAW-SVAEAIRLARALEELGLLWIEEPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 222 IADDIDAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMvESSV 301
Cdd:pfam13378 80 PPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446627130 302 ASSAGFHVAFSKKIITSVELT-GPLKFTKDI--GNLHYDVPFIRLNEKPGLGIEINED 356
Cdd:pfam13378 159 GLAASLHLAAAVPNLLIQEYFlDPLLLEDDLltEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-358 |
1.35e-55 |
|
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: 185.90 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 6 IHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDH--VTGESWESTFHTLKHTLAPALIGKNPMNIE 83
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGpfYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 84 KIHDMMdNTIYGVPTAKAAIDIACFDIMGKKLNQPVYQLIGGRyHEEFHVTHVLSIA-DPEDMAEEAASMIQKGYQSFKM 162
Cdd:cd03317 81 EVSERL-APIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVGVSIGIQdDVEQLLKQIERYLEEGYKRIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 163 KVGTNVkeDVKRIEAVRERVGnDIAIRVDVNqgwknSANTLT---ALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLP 239
Cdd:cd03317 159 KIKPGW--DVEPLKAVRERFP-DIPLMADAN-----SAYTLAdipLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 240 LMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVasSAGFHVAFS--KKIIT 317
Cdd:cd03317 231 ICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGI--GRAHNVALAslPNFTY 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627130 318 SVELTGPLK-FTKDIGNLHYDVP--FIRLNEKPGLGIEINEDTL 358
Cdd:cd03317 309 PGDISASSRyFEEDIITPPFELEngIISVPTGPGIGVTVDREAL 352
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
31-354 |
1.78e-51 |
|
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: 174.83 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 31 SIIVKMETDEGIIGYGEGVADDHVTgeswestFHTLKHtLAPALIGKNPMNIEKIHDMMDN-TIY----GVP-TAKAAID 104
Cdd:cd03327 11 WLFVEIETDDGTVGYANTTGGPVAC-------WIVDQH-LARFLIGKDPSDIEKLWDQMYRaTLAygrkGIAmAAISAVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 105 IACFDIMGKKLNQPVYQLIGGRYHEE--FHVTHvLSIADPEDMAEEAASMIQKGYQSFKMKVG-------TNVKEDVKRI 175
Cdd:cd03327 83 LALWDLLGKIRGEPVYKLLGGRTRDKipAYASG-LYPTDLDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 176 EAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDEGLKSSREMRQI 255
Cdd:cd03327 162 RAIREAVGYDVDLMLDCYMSW-NLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 256 IKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIecqvgsMVESSVASSAGFHVA-------FSKKIITSVELTGPLKFt 328
Cdd:cd03327 241 LEGRAVDILQPDVNWVGGITELKKIAALAEAYGV------PVVPHASQIYNYHFImsepnspFAEYLPNSPDEVGNPLF- 313
|
330 340 350
....*....|....*....|....*....|.
gi 446627130 329 kdiGNLHYDVP-----FIRLNEKPGLGIEIN 354
Cdd:cd03327 314 ---YYIFLNEPvpvngYFDLSDKPGFGLELN 341
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-321 |
4.43e-51 |
|
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: 170.20 E-value: 4.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 6 IHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEgvaddhvtgeswestfhtlkhtlapaligknpmnieki 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 86 hdmmdntiygvptAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVthvlsiadpedmaeeaasmiqkgYQSfkmkvg 165
Cdd:cd00308 43 -------------VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPA-----------------------YGS------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 166 tnvkedVKRIEAVRERVGNDIAIRVDVNQGWknsaNTLTAL---RSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMI 242
Cdd:cd00308 81 ------IERVRAVREAFGPDARLAVDANGAW----TPKEAIrliRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446627130 243 DEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVAFSKKIITSVEL 321
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-360 |
3.68e-41 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 148.51 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 1 MKITAIHLYaiRLPLRNPFVisygsysdmpsiivKMETDEGIIGYGEGVAddhvtgESWESTFHTLKHTLAPALIGKNPM 80
Cdd:PRK14017 1 MKITKLETF--RVPPRWLFL--------------KIETDEGIVGWGEPVV------EGRARTVEAAVHELADYLIGKDPR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 81 NIEKIHdmmdNTIY------GVP---TAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAAS 151
Cdd:PRK14017 59 RIEDHW----QVMYrggfyrGGPilmSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 152 MIQKGYQSFKMKvGTN----------VKEDVKRIEAVRERVGNDIAIRVDVNqGWKNSANTLTALRSLGHLNIDWIEQPV 221
Cdd:PRK14017 135 RVERGFTAVKMN-GTEelqyidsprkVDAAVARVAAVREAVGPEIGIGVDFH-GRVHKPMAKVLAKELEPYRPMFIEEPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 222 IADDIDAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGI----ECQVGsmv 297
Cdd:PRK14017 213 LPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDValapHCPLG--- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446627130 298 esSVASSAGFHVAFSKK--IITSVEL-------TGPLKFTKDIGNLHYDVPFIRLNEKPGLGIEINEDTLQE 360
Cdd:PRK14017 290 --PIALAACLQVDAVSPnaFIQEQSLgihynqgADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRE 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-354 |
4.25e-41 |
|
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: 147.86 E-value: 4.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLrnpfvisygsysdmpsIIVKMETDEGIIGYGEGVAddhvtgESWESTFHTLKHTLAPALIGKNPMN 81
Cdd:cd03325 1 KITKIETFVVPPRW----------------LFVKIETDEGVVGWGEPTV------EGKARTVEAAVQELEDYLIGKDPMN 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 82 IEKIHDMMDNTIY--GVP---TAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKG 156
Cdd:cd03325 59 IEHHWQVMYRGGFyrGGPvlmSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 157 YQSFKMK-------VGTN--VKEDVKRIEAVRERVGNDIAIRVDVN-QGWKNSANTLtaLRSLGHLNIDWIEQPVIADDI 226
Cdd:cd03325 139 FTAVKMNateelqwIDTSkkVDAAVERVAALREAVGPDIDIGVDFHgRVSKPMAKDL--AKELEPYRLLFIEEPVLPENV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 227 DAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIecqvgSMV----ESSVA 302
Cdd:cd03325 217 EALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV-----ALAphcpLGPIA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446627130 303 SSAGFHVAFSKK---------IITSVELTGPLKFTKDIGNLHYDVPFIRLNEKPGLGIEIN 354
Cdd:cd03325 292 LAASLHVDASTPnfliqeqslGIHYNEGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
6-310 |
7.18e-38 |
|
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: 136.62 E-value: 7.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 6 IHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEgvaddhvtgeswestfhtlkhtLAPALIGKnpmnieki 85
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGE----------------------IAPLPLAF-------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 86 hdmmdntiyGVPTAKAAIDIACFDIMGKKLNQPVYQLIGgryheefhvthvlsiADPEDMAEEAASMIQKGYQSFKMKVG 165
Cdd:cd03320 51 ---------GIESALANLEALLVGFTRPRNRIPVNALLP---------------AGDAAALGEAKAAYGGGYRTVKLKVG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 166 -TNVKEDVKRIEAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQPVIADDIDAMAhiRSKIDLPLMIDE 244
Cdd:cd03320 107 aTSFEEDLARLRALREALPADAKLRLDANGGW-SLEEALAFLEALAAGRIEYIEQPLPPDDLAELR--RLAAGVPIALDE 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446627130 245 GLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSAGFHVA 310
Cdd:cd03320 184 SLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLA 249
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-293 |
6.22e-35 |
|
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: 131.75 E-value: 6.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLRNPfviSYGSYSDMP--SIIVKM-----ETDEGIIGYgegvaddHVTGESWESTfHTLKHTLAPAL 74
Cdd:cd03329 1 KITDVEVTVFEYPTQPV---SFDGGHHHPgpAGTRKLalltiETDEGAKGH-------AFGGRPVTDP-ALVDRFLKKVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 75 IGKNPMNIEKIHDMMDNTIYGVP-TAKAAIDIACFDIMGKKLNQPVYQLIGG------RYHEEFHVTHVLSIADPEDMAE 147
Cdd:cd03329 70 IGQDPLDRERLWQDLWRLQRGLTdRGLGLVDIALWDLAGKYLGLPVHRLLGGyrekipAYASTMVGDDLEGLESPEAYAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 148 EAASMIQKGYQSFKMK--VGTNVKEDVKRIEAVRERVGNDIAIRVDvNQGWKNSANTLTALRSLGHLNIDWIEQPVIADD 225
Cdd:cd03329 150 FAEECKALGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHD-GAHWYSRADALRLGRALEELGFFWYEDPLREAS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446627130 226 IDAMAHIRSKIDLPLMIDEGLKSSREMR-QIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQV 293
Cdd:cd03329 229 ISSYRWLAEKLDIPILGTEHSRGALESRaDWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVEL 297
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-356 |
9.29e-34 |
|
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: 127.98 E-value: 9.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 1 MKITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDHVTGESWEStfhtLKHTLAPALIGKN-- 78
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYLFTYTPAALKSLKQ----LLDDMAALLVGEPla 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 79 PMNIEKihdMMDN--TIYG----VPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHE-EFHVTHVLSIAdpEDMAEEAAS 151
Cdd:cd03321 77 PAELER---ALAKrfRLLGytglVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPvQAYDSHGLDGA--KLATERAVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 152 MIQKGYQSFKMKVG-TNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSAnTLTALRSLGHLNIDWIEQPVIADDIDAMA 230
Cdd:cd03321 152 AAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPE-AIERGQALDQEGLTWIEEPTLQHDYEGHA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 231 HIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSV---ASSAGF 307
Cdd:cd03321 231 RIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAhllAVTPTA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446627130 308 H----VAFSKKIITSveltgPLKFTKdiGNLHYDvpfirlnEKPGLGIEINED 356
Cdd:cd03321 311 HwleyVDWAGAILEP-----PLKFED--GNAVIP-------DEPGNGIIWREK 349
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
142-238 |
6.40e-32 |
|
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: 115.84 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 142 PEDMAEEAASMI-QKGYQSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWkNSANTLTALRSLGHLNIDWIEQP 220
Cdd:smart00922 1 PEELAEAARRAVaEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAW-TAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 446627130 221 VIADDIDAMAHIRSKIDL 238
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
14-305 |
2.58e-25 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 104.44 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 14 PLRNPFVISYGSYSDMPSIIVKMEtDEGIIGYGEGVADDHVtGESWESTFHTLKhTLAPALigKNPMNIEKIHDMMdnti 93
Cdd:PRK15129 12 PLHTPFVIARGSRSEARVVVVELE-EEGIKGTGECTPYPRY-GESDASVMAQIM-SVVPQL--EKGLTREALQKLL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 94 ygvPT--AKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKGYQSFKMKVGTNVKED 171
Cdd:PRK15129 83 ---PAgaARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLISE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 172 vkRIEAVRERVgNDIAIRVDVNQGWKnsANTLTA-LRSLGHLNIDWIEQPVIADDIDAMAHIRSKidLPLMIDE------ 244
Cdd:PRK15129 160 --RMVAIRSAV-PDATLIVDANESWR--AEGLAArCQLLADLGVAMLEQPLPAQDDAALENFIHP--LPICADEschtrs 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446627130 245 ---GLKSSREMrqiikleaadkVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVASSA 305
Cdd:PRK15129 233 slkALKGRYEM-----------VNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISA 285
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-356 |
1.79e-24 |
|
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: 102.52 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRlPLRNpFVIsygsysdmpsiiVKMETDEGIIGYGegvaDDHVTGESwESTFHTLKHTLAPALIGKNPMN 81
Cdd:cd03322 1 KITAIEVIVTC-PGRN-FVT------------LKITTDQGVTGLG----DATLNGRE-LAVKAYLREHLKPLLIGRDANR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 82 IEKI-HDMMDNTIYG----VPTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIADPEDMAEEAASMIQKG 156
Cdd:cd03322 62 IEDIwQYLYRGAYWRrgpvTMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 157 YQSFKMKVgtnvkedVKRIEAVRERVGNDIAIRVDVNQGWK-NSANTLTalRSLGHLNIDWIEQPVIADDIDAMAHIRSK 235
Cdd:cd03322 142 YRAIRVQL-------PKLFEAVREKFGFEFHLLHDVHHRLTpNQAARFG--KDVEPYRLFWMEDPTPAENQEAFRLIRQH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 236 IDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQV-GSMVESSVASSAGFHVAFSKK 314
Cdd:cd03322 213 TATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWhGPTDLSPVGMAAALHLDLWVP 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627130 315 IITSVELTGPLKFTKDI--GNLHYDVPFIRLNEKPGLGIEINED 356
Cdd:cd03322 293 NFGIQEYMRHAEETLEVfpHSVRFEDGYLHPGEEPGLGVEIDEK 336
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
141-310 |
3.25e-22 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 95.81 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 141 DPEDMAEEAASMiqKGYQSFKMKV---GTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWknsaNTLTALRSLGHLN---- 213
Cdd:PRK02901 89 DAAQVPEVLARF--PGCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGW----SVDEAVAAARALDadgp 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 214 IDWIEQPVIAddIDAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLahqAEMAGIECQV 293
Cdd:PRK02901 163 LEYVEQPCAT--VEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDI---AEQIGLPVVV 237
|
170
....*....|....*..
gi 446627130 294 GSMVESSVASSAGFHVA 310
Cdd:PRK02901 238 SSALDTSVGIAAGLALA 254
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
13-124 |
1.68e-21 |
|
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold similarity with enolase N-terminal domain.
Pssm-ID: 397046 [Multi-domain] Cd Length: 117 Bit Score: 88.68 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 13 LPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVAddhvTGESWESTFHTLKHTLAPALIGKNPMNIEKIHDMMDNT 92
Cdd:pfam02746 10 GWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATS----YGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRA 85
|
90 100 110
....*....|....*....|....*....|..
gi 446627130 93 IYGVPTAKAAIDIACFDIMGKKLNQPVYQLIG 124
Cdd:pfam02746 86 ALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-356 |
5.32e-20 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 90.35 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 1 MKITAIHLYaIRLPLRNpFVIsygsysdmpsiiVKMETDEGIIGYGEG--------VA---DDHVtgeswestfhtlkht 69
Cdd:PRK15072 1 MKIVDAEVI-VTCPGRN-FVT------------LKITTDDGVTGLGDAtlngrelaVAsylQDHV--------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 70 lAPALIGKNPMNIEKIHDMMDNTIY---GvP---TAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHV-THVlSIADP 142
Cdd:PRK15072 52 -CPLLIGRDAHRIEDIWQYLYRGAYwrrG-PvtmSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVyGHA-NGRDI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 143 EDMAEEAASMIQKGYQSFKMKVG------------------------TNVKEDV-----------KRIEAVRERVGNDIA 187
Cdd:PRK15072 129 DELLDDVARHLELGYKAIRVQCGvpglkttygvskgkglayepatkgLLPEEELwstekylrfvpKLFEAVRNKFGFDLH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 188 IRVDVNqgwknsaNTLTAL------RSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDEGLKSSREMRQIIKLEAA 261
Cdd:PRK15072 209 LLHDVH-------HRLTPIeaarlgKSLEPYRLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 262 DKVNIKLMKCGGIYPAVKLAHQAEMAGIECQV-GSMVESSVASSAGFHVAFS------KKIITSVELTG---PLKFTKDI 331
Cdd:PRK15072 282 DYIRTTVTHAGGITHLRRIADFAALYQVRTGShGPTDLSPVCMAAALHFDLWvpnfgiQEYMGHSEETLevfPHSYTFED 361
|
410 420
....*....|....*....|....*
gi 446627130 332 GNLHYDvpfirlnEKPGLGIEINED 356
Cdd:PRK15072 362 GYLHPG-------DAPGLGVDFDEK 379
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
31-288 |
7.24e-19 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 87.09 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 31 SIIVKMETDEGIIGYGegvaddhVTGESWESTFHTLKHtLAPALIGKNPMNIEKIHDMMDNTI--YG----VPTAKAAID 104
Cdd:PRK15440 58 TLVVEVEAENGQVGFA-------VSTAGEMGAFIVEKH-LNRFIEGKCVSDIELIWDQMLNATlyYGrkglVMNTISCVD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 105 IACFDIMGKKLNQPVYQLIGGRYHEE--FHVTHvlsiADPeDMAEEAasmiqkGYQSFKMKV-------GTNVKEDVKRI 175
Cdd:PRK15440 130 LALWDLLGKVRGLPVYKLLGGAVRDElqFYATG----ARP-DLAKEM------GFIGGKMPLhhgpadgDAGLRKNAAMV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 176 EAVRERVGNDIAIRVDVnqgWKN-SANTLTALRSLGH-LNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDEGLKSSRE-- 251
Cdd:PRK15440 199 ADMREKVGDDFWLMLDC---WMSlDVNYATKLAHACApYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGEHEATLqg 275
|
250 260 270
....*....|....*....|....*....|....*..
gi 446627130 252 MRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAG 288
Cdd:PRK15440 276 FRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARG 312
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
2-361 |
8.11e-19 |
|
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: 86.99 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADdhvtGESWESTFhtlkhTLAPALIGKNPMN 81
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGG----AEALEALL-----EAARSLVGGDVFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 82 IEK--IHDMM------DNTIYGVPT--------AKAAIDIACFDIMGKKLNQPVYQLIGGRYHEE-------F-----HV 133
Cdd:cd03323 72 AYLavLESVRvafadrDAGGRGLQTfdlrttvhVVTAFEVALLDLLGQALGVPVADLLGGGQRDSvpflaylFykgdrHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 134 THVLSIA---------DPEDMAEEAASMIQK-GYQSFKMKVGTNVKED-VKRIEAVRERVGNDiAIRVDVNQGWknSANT 202
Cdd:cd03323 152 TDLPYPWfrdrwgealTPEGVVRLARAAIDRyGFKSFKLKGGVLPGEEeIEAVKALAEAFPGA-RLRLDPNGAW--SLET 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 203 LTAL-RSLGHLNiDWIEQPVIAddIDAMAHIRSKIDLPL---MIDEGLkssREMRQIIKLEAadkVNIKLMKC---GGIY 275
Cdd:cd03323 229 AIRLaKELEGVL-AYLEDPCGG--REGMAEFRRATGLPLatnMIVTDF---RQLGHAIQLNA---VDIPLADHhfwGGMR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 276 PAVKLA------------HQAEMAGIecQVGSMVEssVASSA-GFHVAFSKKII---TSVELTGPLKFTKdiGNLHydVP 339
Cdd:cd03323 300 GSVRVAqvcetwglgwgmHSNNHLGI--SLAMMTH--VAAAApGLITACDTHWIwqdGQVITGEPLRIKD--GKVA--VP 371
|
410 420
....*....|....*....|..
gi 446627130 340 firlnEKPGLGIEINEDTLQEL 361
Cdd:cd03323 372 -----DKPGLGVELDRDKLAKA 388
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
67-274 |
2.74e-17 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 82.07 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 67 KHTLAPALIGKNPMNIEKIHDMMDNTI--YGVP----TAKAAIDIACFDIMGKKLNQPVYQLIGgRYHEEFHV--THVLS 138
Cdd:cd03328 57 DGLLAPVVEGRDALDPPAAWEAMQRAVrnAGRPgvaaMAISAVDIALWDLKARLLGLPLARLLG-RAHDSVPVygSGGFT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 139 IADPEDMAEEAASMIQKGYQSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWKNSAnTLTALRSLGHLNIDWIE 218
Cdd:cd03328 136 SYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQ-ALALARAFADEGVTWFE 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446627130 219 QPVIADDIDAMAHIRSKIDLPLMIDEG--LKSSREMRQIIKLEAADKVNIKLMKCGGI 274
Cdd:cd03328 215 EPVSSDDLAGLRLVRERGPAGMDIAAGeyAYTLAYFRRLLEAHAVDVLQADVTRCGGV 272
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
99-274 |
7.37e-16 |
|
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: 78.15 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 99 AKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEF-------HVTHVLSIADPEDM--------AEEAASMIQKGY------ 157
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELvscidfrYITDALTPEEALEIlrrgqpgkAAREADLLAEGYpaytts 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 158 -----------------------QSFKMKVGTNVKEDVKRIEAVRERVGNDIAIRVDVNQGWK-NSAntLTALRSLGHLN 213
Cdd:cd03324 190 agwlgysdeklrrlckealaqgfTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDvPEA--IEWVKQLAEFK 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446627130 214 IDWIEQPVIADDIDAMAHIRSKI-DLPLMIDEG-LKSSREM-RQIIKLEAADKVNIKLMKCGGI 274
Cdd:cd03324 268 PWWIEEPTSPDDILGHAAIRKALaPLPIGVATGeHCQNRVVfKQLLQAGAIDVVQIDSCRLGGV 331
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-302 |
3.61e-13 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 69.45 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 9 YAIRLPLRNPFVISYGSYSDMPSIIVKMeTDEGIIGYGEGVADDHVTGESWESTFHTLKhtlapALIGK-NPMNIEKIHD 87
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRL-TDEGRTGWGEIAPLPGFGTETLAEALDFCR-----ALIEEiTRGDIEAIDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 88 MMDNTIYGVPTAKAAIDIAcfDIMGKKLNQPVYQLIGGryheefhvthvlsiaDPEDMAEEAASMiqKGYQSFKMKVGT- 166
Cdd:TIGR01927 75 QLPSVAFGFESALIELESG--DELPPASNYYVALLPAG---------------DPALLLLRSAKA--EGFRTFKWKVGVg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 167 NVKEDVKRIEAVRERVGNDIAIRVDVNQGWK--NSANTLTALRSLGHLNIDWIEQPV-IADDIDAMAhirskIDLPLMI- 242
Cdd:TIGR01927 136 ELAREGMLVNLLLEALPDKAELRLDANGGLSpdEAQQFLKALDPNLRGRIAFLEEPLpDADEMSAFS-----EATGTAIa 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446627130 243 -DEGLKSSREMRQIIKLEAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESSVA 302
Cdd:TIGR01927 211 lDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIA 271
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-257 |
2.27e-12 |
|
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: 67.42 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRL--PLRNPFVisygSYSDMPSIIVKMETD---EG--IIGYG---------EGVADDHVTGESWESTFHT 65
Cdd:cd03326 1 RIVAIREKAIPLssPIANAYV----DFSGLTTSLVAVVTDvvrDGrpVVGYGfdsigryaqGGLLRERFIPRLLAAAPDS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 66 LKH----TLAPALIGKNPMNIEKIHDMMDNTiygvpTAKAAIDIACFDIMGKKLNQPVYQLIGGRYHEEFHVTHVLSIA- 140
Cdd:cd03326 77 LLDdaggNLDPARAWAAMMRNEKPGGHGERA-----VAVGALDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 141 --------DPEDMAEEAASMIQKGYQSFKMKVG-TNVKEDVKRIEAVRERVGNDIAIRVDVNqGWKNSANTLTALRSLGH 211
Cdd:cd03326 152 ggyyypgdDLGRLRDEMRRYLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDAN-GRFDLETAIAYAKALAP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446627130 212 LNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDEGLKSSREMRQIIK 257
Cdd:cd03326 231 YGLRWYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDARNLLR 276
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
2-305 |
2.33e-10 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 62.18 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 2 KITAIHLYAIRLPLRNPFVISYGSYSDM--PSIIVKMETDEGIIGYGEgVA--DDHVTG-----ESWESTFHTLKHT--- 69
Cdd:PLN02980 932 KISGMEYSLYRIQLCAPPTSASVDFSQFhrEGFILSLSLEDGSVGFGE-VAplEIHEEDlldveEQLRFLLHVIKGAkis 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 70 -LAPALIGKNPMNIEKIHDMMDNTIYgvPTAKAAIDIACFDIMGKKLNQPVYQLIG--GRYHEEFHVTHVLSI------- 139
Cdd:PLN02980 1011 fMLPLLKGSFSSWIWSELGIPPSSIF--PSVRCGLEMAILNAIAVRHGSSLLNILDpyQKDENGSEQSHSVQIcalldsn 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 140 ADPEDMAEEAASMIQKGYQSFKMKVGTNVK--EDVKRIEAVRERVGNDIAIRVDVNQGWknsanTLTALRSLGHL----N 213
Cdd:PLN02980 1089 GSPLEVAYVARKLVEEGFSAIKLKVGRRVSpiQDAAVIQEVRKAVGYQIELRADANRNW-----TYEEAIEFGSLvkscN 1163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 214 IDWIEQPViaDDIDAMAHIRSKIDLPLMIDEGLKSSRE--MRQIIKLEAADKVN--IKLMKCGGIYPAVKLAHQAEMAGI 289
Cdd:PLN02980 1164 LKYIEEPV--QDEDDLIKFCEETGLPVALDETIDKFEEcpLRMLTKYTHPGIVAvvIKPSVVGGFENAALIARWAQQHGK 1241
|
330
....*....|....*.
gi 446627130 290 ECQVGSMVESSVASSA 305
Cdd:PLN02980 1242 MAVISAAYESGLGLSA 1257
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
14-254 |
8.88e-09 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 56.18 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 14 PLRNPFVISYGSYSDMPSIIVKMETDEGIIGYGEgVADDHVTG-ESWES--TF-HTLKHTLAPAligknpmNIEKIHDMM 89
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGE-IAPLPWFGsETLEEalAFcQQLPGEITPE-------QIFSIPDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 90 DNTIYGVPTAKAAIDIACFDIMgkkLNQPVY-QLIG-GRYheefhvthVLsiadpedmaEEAASMIQKGYQSFKMKVGTN 167
Cdd:PRK02714 85 PACQFGFESALENESGSRSNVT---LNPLSYsALLPaGEA--------AL---------QQWQTLWQQGYRTFKWKIGVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627130 168 -VKEDVKRIEAVRERVGNDIAIRVDVNQGWKN-SANT-LTALRSLGHLNIDWIEQPVIADDIDAMAHIRSKIDLPLMIDE 244
Cdd:PRK02714 145 pLEQELKIFEQLLERLPAGAKLRLDANGGLSLeEAKRwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDE 224
|
250
....*....|
gi 446627130 245 GLKSSREMRQ 254
Cdd:PRK02714 225 SVANLAQLQQ 234
|
|
| |
