|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-386 |
0e+00 |
|
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: 723.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 2 RIVDIREKTVSIASPIANAYIDFSKMTCSVVAVITDVIRDGKPVIGYGFNSNGRYGQGALMRDRFLARITEADPDTLVDH 81
Cdd:cd03326 1 RIVAIREKAIPLSSPIANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLLAAAPDSLLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 82 ENNNLDPFAIWKTLMTNEKPGGHGERSVAVGTIDMAVWDAVAKIEGKPLYRLLADRYREGVADDKVWVYAAGGYYYPGKD 161
Cdd:cd03326 81 AGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAAGGYYYPGDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 162 QTKLKAEMQSYLDRGYDVVKMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVG 241
Cdd:cd03326 161 LGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 242 DPLDYALQAELANHYELPMATGENLFSHQDARNLLRHGGMRPDRDYLQFDCALSYGLVEYMRTLKVMEEMGWSSRRVVPH 321
Cdd:cd03326 241 DPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFPH 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489526369 322 GGHQMSLNIAAGLHLGGNESYPDVFQPFGGFADGIKVENGYVGLPDIPGVGFEAKSALYAVMREL 386
Cdd:cd03326 321 GGHLMSLHIAAGLGLGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL 385
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-374 |
2.58e-78 |
|
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: 245.21 E-value: 2.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 2 RIVDIRekTVSIASPIANAYIDFSKMTCSVVAVITDvirDGkpVIGYGFNSNGRYGQG--ALMRDRFLARITEADPdtlv 79
Cdd:cd03316 1 KITDVE--TFVLRVPLPEPGGAVTWRNLVLVRVTTD---DG--ITGWGEAYPGGRPSAvaAAIEDLLAPLLIGRDP---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 80 dhennnLDPFAIWKTLMTNEKPGG-HGERSVAVGTIDMAVWDAVAKIEGKPLYRLLADRYRegvadDKVWVYAAGGYYYP 158
Cdd:cd03316 70 ------LDIERLWEKLYRRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVR-----DRVRVYASGGGYDD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 159 GKDQtkLKAEMQSYLDRGYDVVKMKIGAVP-----LDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYN 233
Cdd:cd03316 139 SPEE--LAEEAKRAVAEGFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 234 LFWYEEVGDPLDYALQAELANHYELPMATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMGw 313
Cdd:cd03316 217 LFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAV----DIIQPDVTKVGGITEAKKIAALAEAHG- 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489526369 314 ssRRVVPHG-----GHQMSLNIAAGL-HLGGNESYPDVFQPFGGFA-DGIKVENGYVGLPDIPGVGFE 374
Cdd:cd03316 292 --VRVAPHGaggpiGLAASLHLAAALpNFGILEYHLDDLPLREDLFkNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-374 |
1.40e-60 |
|
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: 199.66 E-value: 1.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 1 MRIVDIREKTVSI--ASPIANAYIDFSKMTCSVVAVITDvirDGkpVIGYG---FNSNGRYGQGALMRDRFLARITEADP 75
Cdd:COG4948 1 MKITDIEVYPVRLplKRPFTISRGTRTERDVVLVRVETD---DG--ITGWGeavPGGTGAEAVAAALEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 76 dtlvdhennnLDPFAIWKTLMTNEKPGGHgersvAVGTIDMAVWDAVAKIEGKPLYRLLADRYRegvadDKVWVYAAGGY 155
Cdd:COG4948 76 ----------LDIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLLGGKVR-----DRVPVYATLGI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 156 YYPgkdqTKLKAEMQSYLDRGYDVVKMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLF 235
Cdd:COG4948 136 DTP----EEMAEEAREAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 236 WYEEVGDPLDYALQAELANHYELPMATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMGwss 315
Cdd:COG4948 212 WIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAV----DIVNIKLSKVGGLTEALRIAALAEAHG--- 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489526369 316 RRVVPHGGHQMSLNIAAGLHLGGNESYPDVFQPFGG-------FADGIKVENGYVGLPDIPGVGFE 374
Cdd:COG4948 285 VPVMPHCMLESGIGLAAALHLAAALPNFDIVELDGPllladdlVEDPLRIEDGYLTVPDGPGLGVE 350
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
164-374 |
3.29e-45 |
|
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: 155.03 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 164 KLKAEMQSYLDR-GYDVVKMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGD 242
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 243 PLDYALQAELANHYELPMATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMGWssrRVVPHG 322
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAV----DIVQPDVTRVGGITEALKIAALAEAFGV---PVAPHS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 323 GHqMSLNIAAGLHLG---GNESYPDVFQPFGGFADGI-----KVENGYVGLPDIPGVGFE 374
Cdd:pfam13378 154 GG-GPIGLAASLHLAaavPNLLIQEYFLDPLLLEDDLlteplEVEDGRVAVPDGPGLGVE 212
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
103-337 |
2.82e-35 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 129.37 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 103 GHGErsvAVGTIDMAVWDAVAKIEGKPLYRLLADRYREGVAddkvwVYAAggyyypgkdqtklkaemqsyldrgydvvkm 182
Cdd:cd00308 39 GWGE---VISGIDMALWDLAAKALGVPLAELLGGGSRDRVP-----AYGS------------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 183 kigavpldedIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMAT 262
Cdd:cd00308 81 ----------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489526369 263 GENLFSHQDARNLLRHGGmrpdRDYLQFDCALSYGLVEYMRTLKVMEEMGWssrRVVPHGGHQMSLNIAAGLHLG 337
Cdd:cd00308 151 DESVTTVDDALEALELGA----VDILQIKPTRVGGLTESRRAADLAEAFGI---RVMVHGTLESSIGTAAALHLA 218
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
102-374 |
7.72e-32 |
|
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: 123.21 E-value: 7.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 102 GGHGERSVAVGTIDMAVWDAVAKIEGKPLYRLLADRYRegvadDKVWVYAAGGYYYPGKdqtKLKAEMQSYLDRGYDVVK 181
Cdd:cd03327 69 GRKGIAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTR-----DKIPAYASGLYPTDLD---ELPDEAKEYLKEGYRGMK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 182 MKIGAVP------LDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANH 255
Cdd:cd03327 141 MRFGYGPsdghagLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 256 YELPMATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEyMRTLKVMEEMgwSSRRVVPHGGhqmslNIAAgLH 335
Cdd:cd03327 221 TGIPISTGEHEYTVYGFKRLLEGRAV----DILQPDVNWVGGITE-LKKIAALAEA--YGVPVVPHAS-----QIYN-YH 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489526369 336 LGGNES----------YPD-----VFQPFggFADGIKVENGYVGLPDIPGVGFE 374
Cdd:cd03327 288 FIMSEPnspfaeylpnSPDevgnpLFYYI--FLNEPVPVNGYFDLSDKPGFGLE 339
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
110-374 |
4.69e-25 |
|
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: 104.72 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLAdryreGVADDKVWVYAAGGyyypGKDQTKLKAEMQSYLDRGYDVVKM----KIG 185
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLG-----GQVRDRVRVYSWIG----GDRPSDVAEAARARREAGFTAVKMnateELQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 186 AVP----LDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMA 261
Cdd:cd03325 152 WIDtskkVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 262 TGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEyMRTLKVMEEMgwSSRRVVPHGGhQMSLNIAAGLHLGGNeS 341
Cdd:cd03325 232 TGERLFSRWDFKELLEDGAV----DIIQPDISHAGGITE-LKKIAAMAEA--YDVALAPHCP-LGPIALAASLHVDAS-T 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489526369 342 YPDVFQPFGGFAD---------------GIKVENGYVGLPDIPGVGFE 374
Cdd:cd03325 303 PNFLIQEQSLGIHynegddlldylvdpeVFDMENGYVKLPTGPGLGIE 350
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
110-323 |
5.21e-22 |
|
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: 96.64 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLAD------------RY--------------REGVADDKVWVYAAGGYYYP----- 158
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLVDmtpeelvscidfRYitdaltpeealeilRRGQPGKAAREADLLAEGYPaytts 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 159 ----GKDQTKLKAEMQSYLDRGYDVVKMKIGAVPLDeDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNL 234
Cdd:cd03324 190 agwlGYSDEKLRRLCKEALAQGFTHFKLKVGADLED-DIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 235 FWYEEVGDPLDYALQAELAN---HYELPMATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEM 311
Cdd:cd03324 269 WWIEEPTSPDDILGHAAIRKalaPLPIGVATGEHCQNRVVFKQLLQAGAI----DVVQIDSCRLGGVNENLAVLLMAAKF 344
|
250
....*....|..
gi 489526369 312 GwssRRVVPHGG 323
Cdd:cd03324 345 G---VPVCPHAG 353
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
164-258 |
1.77e-21 |
|
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: 88.11 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 164 KLKAEMQSYL-DRGYDVVKMKIGAvPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGD 242
Cdd:smart00922 3 ELAEAARRAVaEAGFRAVKVKVGG-GPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81
|
90
....*....|....*.
gi 489526369 243 PLDYALQAELANHYEL 258
Cdd:smart00922 82 PDDLEGLAELRRATPI 97
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
86-291 |
6.91e-20 |
|
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: 89.78 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 86 LDPFAIWKTL---MTNEKPGGHGerSVAVGTIDMAVWDAVAKIEGKPLYRLLadryreGVADDKVWVYAAGGY--Yypgk 160
Cdd:cd03328 70 LDPPAAWEAMqraVRNAGRPGVA--AMAISAVDIALWDLKARLLGLPLARLL------GRAHDSVPVYGSGGFtsY---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 161 DQTKLKAEMQSYLDRGYDVVKMKIGAVPlDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEV 240
Cdd:cd03328 138 DDDRLREQLSGWVAQGIPRVKMKIGRDP-RRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEP 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489526369 241 GDPLDYALQAELANHYELPM--ATGENLFSHQDARNLLRHGGMrpdrDYLQFD 291
Cdd:cd03328 217 VSSDDLAGLRLVRERGPAGMdiAAGEYAYTLAYFRRLLEAHAV----DVLQAD 265
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
112-312 |
4.13e-19 |
|
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: 86.24 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 112 GTIDMAVWDAVAKIEGKPLYRLLAdRYREGVADDkvWVYAAGgyyypgkDQTKLKAEMQSYLDRGYDVVKMKIGAvPLDE 191
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLG-GYRDRVRVA--HMLGLG-------EPAEVAEEARRALEAGFRTFKLKVGR-DPAR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 192 DIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMATGENLFSHQD 271
Cdd:cd03315 115 DVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHD 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489526369 272 ARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMG 312
Cdd:cd03315 195 AFRELALGAA----DAVNIKTAKTGGLTKAQRVLAVAEALG 231
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
110-374 |
4.40e-19 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 87.64 E-value: 4.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLADRYRegvadDKVWVYAAGGyyypGKDQTKLKAEMQSYLDRGYDVVKMKiGAVPL 189
Cdd:PRK14017 82 AIAGIDQALWDIKGKALGVPVHELLGGLVR-----DRIRVYSWIG----GDRPADVAEAARARVERGFTAVKMN-GTEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 190 ---------DEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPM 260
Cdd:PRK14017 152 qyidsprkvDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 261 ATGENLFSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEyMRTLKVMEEMGWSSrrVVPH---GghqmSLNIAAGLHLG 337
Cdd:PRK14017 232 ATGERLFSRWDFKRVLEAGGV----DIIQPDLSHAGGITE-CRKIAAMAEAYDVA--LAPHcplG----PIALAACLQVD 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489526369 338 -------------------GNE--SY---PDVFQPfggfadgikvENGYVGLPDIPGVGFE 374
Cdd:PRK14017 301 avspnafiqeqslgihynqGADllDYvknKEVFAY----------EDGFVAIPTGPGLGIE 351
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
102-284 |
1.42e-18 |
|
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: 86.00 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 102 GGHGERSVAVGTIDMAVWDAVAKIEGKPLYRLLadryreGVADDKVWVYAAGGYyypgkDQTKLKA-EMQSYLDRGYDVV 180
Cdd:cd03321 92 GYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLL------GGNPRPVQAYDSHGL-----DGAKLATeRAVTAAEEGFHAV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 181 KMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPM 260
Cdd:cd03321 161 KTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPV 240
|
170 180
....*....|....*....|....*..
gi 489526369 261 ATGENLFSHQDARNLLRHGG---MRPD 284
Cdd:cd03321 241 QMGENWLGPEEMFKALSAGAcdlVMPD 267
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
108-372 |
6.77e-17 |
|
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: 81.21 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 108 SVAVGTIDMAVWDAVAKIEGKPLYRLLADRYREGVadDKVWVYAAGgyyypgkDQTKLKAEMQSYLDRG-YDVVKMKIGA 186
Cdd:cd03318 98 LFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSL--PVAWTLASG-------DTERDIAEAEEMLEAGrHRRFKLKMGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 187 VPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMATGENL 266
Cdd:cd03318 169 RPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 267 FSHQDARNLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMGwssrrVVPHGGHQM--SLNIAAGLHLGGneSYPD 344
Cdd:cd03318 249 SGPADAFELARRGAA----DVFSLKIAKSGGLRRAQKVAAIAEAAG-----IALYGGTMLesSIGTAASAHLFA--TLPS 317
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489526369 345 VfqPFGG-------FADGI-----KVENGYVGLPDIPGVG 372
Cdd:cd03318 318 L--PFGCelfgpllLAEDLleeplAYRDGELHVPTGPGLG 355
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
110-374 |
5.22e-16 |
|
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: 78.64 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLADRYREGVAddkVWVYAAggyyypGKDQTKLKAEMQSYLDRGYDVVKMKIGAVpl 189
Cdd:cd03322 84 AIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIM---VYSHAS------GRDIPELLEAVERHLAQGYRAIRVQLPKL-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 190 dedirrIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMATGENLFSH 269
Cdd:cd03322 153 ------FEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 270 QDARNLLRHGGMrpdrDYLQfdCALSY-GLVEYMRTLKVMEEM-----GWssrrvvpHGGHQMS-LNIAAGLHLggNESY 342
Cdd:cd03322 227 WDWQNLIQERLI----DYIR--TTVSHaGGITPARKIADLASLygvrtGW-------HGPTDLSpVGMAAALHL--DLWV 291
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489526369 343 PDV-FQPFGGFAD--------GIKVENGYVGLPDIPGVGFE 374
Cdd:cd03322 292 PNFgIQEYMRHAEetlevfphSVRFEDGYLHPGEEPGLGVE 332
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
161-280 |
2.16e-15 |
|
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: 75.37 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 161 DQTKLKAEMQSYLDRGYDVVKMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEV 240
Cdd:cd03320 82 GDAAALGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQP 161
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489526369 241 GDPLDYALQAELAnhYELPMATGENLFSHQDARNLLRHGG 280
Cdd:cd03320 162 LPPDDLAELRRLA--AGVPIALDESLRRLDDPLALAAAGA 199
|
|
| 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 ... |
114-279 |
1.26e-14 |
|
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: 73.76 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 114 IDMAVWDAVAKIEGKPLYRLLADRYREGVADDkvwvyaaggYYYPGKDQTKLKAEMQSYLDRGYDVVKMKIGAvPLDEDI 193
Cdd:cd03319 96 VDIALWDLEAKLLGLPLYQLWGGGAPRPLETD---------YTISIDTPEAMAAAAKKAAKRGFPLLKIKLGG-DLEDDI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 194 RRIEAVLEVVGDGrRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEvgdPL---DYALQAELANHYELPMATGENLFSHQ 270
Cdd:cd03319 166 ERIRAIREAAPDA-RLRVDANQGWTPEEAVELLRELAELGVELIEQ---PVpagDDDGLAYLRDKSPLPIMADESCFSAA 241
|
....*....
gi 489526369 271 DARNLLRHG 279
Cdd:cd03319 242 DAARLAGGG 250
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
110-374 |
1.62e-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: 71.27 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLADrYRegvadDKVWVYA--AGGYYYPGKDQTKLKAEM-QSYLDRGYDVVKMKI-G 185
Cdd:cd03329 95 GLGLVDIALWDLAGKYLGLPVHRLLGG-YR-----EKIPAYAstMVGDDLEGLESPEAYADFaEECKALGYRAIKLHPwG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 186 AVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELANHYELPMATGEN 265
Cdd:cd03329 169 PGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEH 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 266 LFSHQDAR-NLLRHGGMrpdrDYLQFDCALSYGLVEYMRTLKVMEEMGWssrRVVPHGGHqmslniAAGLHLGG---NES 341
Cdd:cd03329 249 SRGALESRaDWVLAGAT----DFLRADVNLVGGITGAMKTAHLAEAFGL---DVELHGNG------AANLHVIAairNTR 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489526369 342 Y-----PDVFQPFGGFADGIKV------ENGYVGLPDIPGVGFE 374
Cdd:cd03329 316 YyerglLHPSQKYDVYAGYLSVlddpvdSDGFVHVPKGPGLGVE 359
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
110-279 |
8.65e-11 |
|
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: 62.64 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLadryreGVADDKVWVYAAGGYyypGKDQTKLKAEMQSYLDRGYDVVKMKIGAvpl 189
Cdd:cd03317 95 AKAGLEMAVWDLYAKAQGQSLAQYL------GGTRDSIPVGVSIGI---QDDVEQLLKQIERYLEEGYKRIKLKIKP--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 190 DEDIRRIEAVLEVVGDgRRLAVDANGRFDLQTgIAYAEAIKKYNLFWYEE---VGDPLDYalqAELANHYELPMATGENL 266
Cdd:cd03317 163 GWDVEPLKAVRERFPD-IPLMADANSAYTLAD-IPLLKRLDEYGLLMIEQplaADDLIDH---AELQKLLKTPICLDESI 237
|
170
....*....|...
gi 489526369 267 FSHQDARNLLRHG 279
Cdd:cd03317 238 QSAEDARKAIELG 250
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
104-322 |
4.49e-10 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 60.90 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 104 HGERSVAVGTI---DMAVWDAVAKIEGKPLYRLLADRYRegvadDKVWVYAAGGyyypgkdQTKLKAEMqsyldrGYDVV 180
Cdd:PRK15440 115 YGRKGLVMNTIscvDLALWDLLGKVRGLPVYKLLGGAVR-----DELQFYATGA-------RPDLAKEM------GFIGG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 181 KMKIGAVP------LDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLFWYEEVGDPLDYALQAELAN 254
Cdd:PRK15440 177 KMPLHHGPadgdagLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKR 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 255 HYELPM--ATGENLFSHQDARNLLRHGgmrpDRDYLQFDCALSYGLVEYMRTLKVMEEMGwssRRVVPHG 322
Cdd:PRK15440 257 NAPAGMmvTSGEHEATLQGFRTLLEMG----CIDIIQPDVGWCGGLTELVKIAALAKARG---QLVVPHG 319
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
110-278 |
1.52e-09 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 59.15 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 110 AVGTIDMAVWDAVAKIEGKPLYRLLADRYREGVAddkvwVYAAGGyyypGKDQTKLKAEMQSYLDRGYDVVKMKIG---- 185
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLGGASREGVM-----VYGHAN----GRDIDELLDDVARHLELGYKAIRVQCGvpgl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 186 --------------------AVPLDED------IRRI----EAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIKKYNLF 235
Cdd:PRK15072 156 kttygvskgkglayepatkgLLPEEELwstekyLRFVpklfEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489526369 236 WYEevgDPLDYALQAELA---NHYELPMATGENLFSHQDARNLLRH 278
Cdd:PRK15072 236 WLE---DPTPAENQEAFRlirQHTTTPLAVGEVFNSIWDCKQLIEE 278
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
180-253 |
1.36e-05 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 46.50 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 180 VKMKIG--AVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTGIAYAEAIkkynlfwyeEVGDPLDYALQ-----AEL 252
Cdd:PRK02901 106 AKVKVAepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARAL---------DADGPLEYVEQpcatvEEL 176
|
.
gi 489526369 253 A 253
Cdd:PRK02901 177 A 177
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
170-264 |
2.79e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 42.31 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489526369 170 QSYLDRGYDVVKMKIGAVPLDEDIRRIEAVLEVVGDGRRLAVDANGRFDLQTG---IAYAEAIKKYNLFWYEEVGDPLDY 246
Cdd:PRK02714 127 QTLWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQF 206
|
90
....*....|....*...
gi 489526369 247 ALQAELANHYELPMATGE 264
Cdd:PRK02714 207 DEMLQLSQDYQTPIALDE 224
|
|
| |
