|
Name |
Accession |
Description |
Interval |
E-value |
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
4-419 |
0e+00 |
|
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: 862.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 4 GRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKD 83
Cdd:cd03324 1 IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDA-AGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 84 IVGDFRGFYRQLTSDGQLRWIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEED 163
Cdd:cd03324 80 IVADMGKFWRRLTSDSQLRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 164 ALEILQKGQIGKKEREKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGP 243
Cdd:cd03324 160 ALEILRRGQPGKAAREADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 244 EKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQ 323
Cdd:cd03324 240 DNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAID 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 324 FLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQR 403
Cdd:cd03324 320 VVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQN 399
|
410
....*....|....*.
gi 42544119 404 ASYMPPKDPGYSTEMK 419
Cdd:cd03324 400 GAYMPPTDPGYSIEMK 415
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
5-426 |
2.96e-80 |
|
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: 252.05 E-value: 2.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 5 RISRLSVRDVRFPTSLGGHGAdaMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVN-ALAHHVLNKDLKD 83
Cdd:COG4948 2 KITDIEVYPVRLPLKRPFTIS--RGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAALEeALAPLLIGRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 84 IVGDFRGFYRQLtsdgqlrwigpekGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteed 163
Cdd:COG4948 78 IEALWQRLYRAL-------------PGNPAAKAAVDMALWDLLGKALGVPVYQLL------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 164 aleilqkgqiGKKEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMI 241
Cdd:COG4948 120 ----------GGKVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 242 GPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKA 321
Cdd:COG4948 180 GPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 322 LQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEH 394
Cdd:COG4948 257 VDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDL 327
|
410 420 430
....*....|....*....|....*....|..
gi 42544119 395 FKYPVMIQRASYMPPKDPGYSTEMKEESVKKH 426
Cdd:COG4948 328 VEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
5-417 |
2.93e-68 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 220.95 E-value: 2.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 5 RISRLSVRDVRFPTSLGGHgadamhTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDI 84
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG------AVTWRNLVLVRVTTD--DGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 85 VGDFRGFYRQLTSDGQlrwigpeKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteeda 164
Cdd:cd03316 73 ERLWEKLYRRLFWRGR-------GGVAMAAISAVDIALWDIKGKAAGVPVYKLL-------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 165 leilqkgqiGKKEREKqmlaqgYPAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIR 238
Cdd:cd03316 120 ---------GGKVRDR------VRVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 239 DMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQ 318
Cdd:cd03316 184 EAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQA---TSVPIAAGENLYTRWEFRDLLE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 319 AKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH-- 394
Cdd:cd03316 261 AGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLre 332
|
410 420
....*....|....*....|....*
gi 42544119 395 --FKYPVMIQRASYMPPKDPGYSTE 417
Cdd:cd03316 333 dlFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
202-422 |
2.78e-60 |
|
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: 195.86 E-value: 2.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 202 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 280
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 281 PDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVG 360
Cdd:pfam13378 81 PDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42544119 361 LcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 422
Cdd:pfam13378 158 I-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
39-419 |
9.13e-39 |
|
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: 142.86 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 39 VVIETDAEDGIKGCGITFtlgkGTEVVVCAV-NALAHHVLNKDLKDIVGDFRGFYRQLTSDGQlrwigpeKGVVHLATAA 117
Cdd:cd03327 12 LFVEIETDDGTVGYANTT----GGPVACWIVdQHLARFLIGKDPSDIEKLWDQMYRATLAYGR-------KGIAMAAISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 118 VLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlaqgYPAYTTScawL 197
Cdd:cd03327 81 VDLALWDLLGKIRGEPVYKLL-----------------------------------GGRTRDK------IPAYASG---L 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 198 GYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 269
Cdd:cd03327 117 YPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 270 FKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFE 349
Cdd:cd03327 197 YELRWIEEPLIPDDIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYG 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42544119 350 IPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 419
Cdd:cd03327 274 VPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
5-355 |
3.96e-28 |
|
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: 114.05 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 5 RISRLSVRDVRFPTslgghgaDAMHTDPDY---SAAYVVIETDAeDGIKGCGITFTlgkGTEVVVCAVNALAHHVLNKDL 81
Cdd:cd03328 1 AVERVEARAYTVPT-------DAPEADGTLawdATTLVLVEVRA-GGRTGLGYTYA---DAAAAALVDGLLAPVVEGRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 82 KDIVGDFRGFYRQLtsdgqlRWIGPEkGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMlvscidfryitdvlte 161
Cdd:cd03328 70 LDPPAAWEAMQRAV------RNAGRP-GVAAMAISAVDIALWDLKARLLGLPLARLLGRAHDSV---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 162 edaleilqkgqigkkerekqmlaqgyPAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMI 241
Cdd:cd03328 127 --------------------------PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 242 GPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKA 321
Cdd:cd03328 180 GPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHA 258
|
330 340 350
....*....|....*....|....*....|....
gi 42544119 322 LQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH 355
Cdd:cd03328 259 VDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH 292
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
201-294 |
1.76e-27 |
|
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: 105.06 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 201 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 280
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81
|
90
....*....|....
gi 42544119 281 PDDILGHATISKAL 294
Cdd:smart00922 82 PDDLEGLAELRRAT 95
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
207-368 |
3.02e-25 |
|
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: 103.18 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 207 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 279
Cdd:cd00308 54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 280 SPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 359
Cdd:cd00308 130 APDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE 206
|
170
....*....|.
gi 42544119 360 G--LCELVQHL 368
Cdd:cd00308 207 SsiGTAAALHL 217
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
38-356 |
8.61e-20 |
|
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: 90.08 E-value: 8.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 38 YVVIETDAedGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLtsdgqlRWIGpekGVVHL-ATA 116
Cdd:cd03325 16 FVKIETDE--GVVGWGEPTVEGK-ARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGG------FYRG---GPVLMsAIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 117 AVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlAQGYpayttscAW 196
Cdd:cd03325 84 GIDQALWDIKGKVLGVPVHQLL-----------------------------------GGQVRDR---VRVY-------SW 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 197 LG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSK 266
Cdd:cd03325 119 IGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 267 LAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAK 346
Cdd:cd03325 199 LEPYRLLFIEEPVLPENVEALAEIAAR---TTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAE 275
|
330
....*....|
gi 42544119 347 KFEIPVCPHA 356
Cdd:cd03325 276 AYDVALAPHC 285
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
5-427 |
1.00e-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: 87.15 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 5 RISRLSVRDVRFPTSLGGHGADAMHTdpdySAAYVVIETDAEDGIKGCGITFTLgkgTEVVVCAVNALAHHvLNKDLKDI 84
Cdd:cd03321 2 LITGLRARAVNVPMQYPVHTSVGTVA----TAPLVLIDLATDEGVTGHSYLFTY---TPAALKSLKQLLDD-MAALLVGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 85 VGDFRGFYRQLtsDGQLRWIGpEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteeda 164
Cdd:cd03321 74 PLAPAELERAL--AKRFRLLG-YTGLVRMAAAGIDMAAWDALAKVHGLPLAKLL-------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 165 leilqkgqiGKKEREkqmlaqgYPAYTTScawlGYSddtLKQLCA----QALKDGWTRFKVKVG-ADLQDDMRRCQIIRD 239
Cdd:cd03321 125 ---------GGNPRP-------VQAYDSH----GLD---GAKLATeravTAAEEGFHAVKTKIGyPTADEDLAVVRSIRQ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 240 MIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIgiatGEQCHNRVIFKQLLQ 318
Cdd:cd03321 182 AVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALrTPVQM----GENWLGPEEMFKALS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 319 AKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqhliIFDYISV---SASLENRVCEYVDHLHEHF 395
Cdd:cd03321 258 AGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH--------------LFQEISAhllAVTPTAHWLEYVDWAGAIL 323
|
410 420 430
....*....|....*....|....*....|..
gi 42544119 396 KYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 427
Cdd:cd03321 324 EPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
109-368 |
1.22e-16 |
|
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: 79.69 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 109 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfrYITDVLTEEDALEilqkgqigkkerekqmlaqgyp 188
Cdd:cd03315 39 GWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVA-----HMLGLGEPAEVAE---------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 189 ayttscawlgysddtlkqLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLA 268
Cdd:cd03315 92 ------------------EARRALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 269 KFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKF 348
Cdd:cd03315 154 DLGLDYVEQPLPADDLEGRAALARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEAL 230
|
250 260
....*....|....*....|...
gi 42544119 349 EIPV---CPHAGGVGLCELVqHL 368
Cdd:cd03315 231 GLPVmvgSMIESGLGTLANA-HL 252
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
192-352 |
5.13e-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: 74.60 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 192 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 270
Cdd:cd03320 74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 271 KPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVNENLSV 341
Cdd:cd03320 154 RIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPRALLEL 219
|
170
....*....|.
gi 42544119 342 LLMAKKFEIPV 352
Cdd:cd03320 220 AEEARARGIPA 230
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
41-425 |
7.16e-15 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 75.70 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 41 IETDaeDGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFR-----GFYRQltsdgqlrwiGPekgvVHL-A 114
Cdd:PRK14017 20 IETD--EGIVGWGEPVVEGR-ARTVEAAVHELADYLIGKDPRRIEDHWQvmyrgGFYRG----------GP----ILMsA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 115 TAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKQMlaqgypAYttsc 194
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELL-----------------------------------GGLVRDRIR------VY---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 195 AWLGYSDDTLKQLCAQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEWM 264
Cdd:PRK14017 118 SWIGGDRPADVAEAARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVLA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 265 SKLAKFKPLWIEEPTSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNEN 338
Cdd:PRK14017 198 KELEPYRPMFIEEPVLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITEC 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 339 LSVLLMAKKFEIPVCPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASY 406
Cdd:PRK14017 269 RKIAAMAEAYDVALAPHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGF 339
|
410 420
....*....|....*....|
gi 42544119 407 M-PPKDPGYSTEMKEESVKK 425
Cdd:PRK14017 340 VaIPTGPGLGIEIDEAKVRE 359
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
114-305 |
3.11e-14 |
|
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: 73.97 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 114 ATAAVLNAVWDLWAKQEGKPVWKLLVDmdprmlvscidfRYitdvlteedaleilqkGQIGKKEREKQMLAQGYPaytts 193
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLAR------------RY----------------GRGQADPRVPVYAAGGYY----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 194 cawlgYSDDTLKQLCAQA---LKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 269
Cdd:cd03326 156 -----YPGDDLGRLRDEMrryLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAP 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 42544119 270 FKPLWIEEPTSPDDILGHATISKALVPlgiGIATGE 305
Cdd:cd03326 231 YGLRWYEEPGDPLDYALQAELADHYDG---PIATGE 263
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
22-359 |
6.62e-14 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 72.84 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 22 GHGADAMHTDPDYSAA----------YVVIETDAEDGIKGCGITfTLGKGTEVVVcaVNALAHHVLNKDLKDIVGDFRGF 91
Cdd:PRK15440 32 DHIATPMSKYPEYRQSrqsfginvlgTLVVEVEAENGQVGFAVS-TAGEMGAFIV--EKHLNRFIEGKCVSDIELIWDQM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 92 YRQLTSDGQlrwigpeKGVVHLATAAVLNAVWDLWAKQEGKPVWKLL---VDMDprmlvscIDFrYIT----DVLTEeda 164
Cdd:PRK15440 109 LNATLYYGR-------KGLVMNTISCVDLALWDLLGKVRGLPVYKLLggaVRDE-------LQF-YATgarpDLAKE--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 165 leilqKGQIGKKerekqMLAQGYPAyttscawlgysddtlkqlcaqalkDGwtrfkvkvGADLQDDMRRCQIIRDMIGPE 244
Cdd:PRK15440 171 -----MGFIGGK-----MPLHHGPA------------------------DG--------DAGLRKNAAMVADMREKVGDD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 245 KTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQCHNRVIFKQLLQAKALQF 324
Cdd:PRK15440 209 FWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEHEATLQGFRTLLEMGCIDI 287
|
330 340 350
....*....|....*....|....*....|....*
gi 42544119 325 LQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 359
Cdd:PRK15440 288 IQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
|
|
| 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 ... |
114-310 |
8.04e-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: 71.84 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 114 ATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIdfryiTDVLTEEDALeilqkgqigkKEREKQMLAQGYPAytts 193
Cdd:cd03319 92 ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDY-----TISIDTPEAM----------AAAAKKAAKRGFPL---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 194 cawlgysddtlkqlcaqalkdgwtrFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL 273
Cdd:cd03319 153 -------------------------LKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVE 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 42544119 274 WIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNR 310
Cdd:cd03319 207 LIEQPVPAGDDDGLAYLRDK---SPLPIMADESCFSA 240
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
38-297 |
2.77e-11 |
|
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: 64.65 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 38 YVVIETDAEDGIKGCGITFTLGK---GTEVVVCAVNA----LAHHVLNKDLKDIVGDFRGFYRQLTSDgqlrwigpekgv 110
Cdd:cd03318 30 LVLVRLTTSDGVVGIGEATTPGGpawGGESPETIKAIidryLAPLLIGRDATNIGAAMALLDRAVAGN------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 111 vHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdPRMLVSCIDFRY-ITDVLTEEDALEILQkgqigkkerekqMLAQGYpa 189
Cdd:cd03318 98 -LFAKAAIEMALLDAQGRRLGLPVSELL----GGRVRDSLPVAWtLASGDTERDIAEAEE------------MLEAGR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 190 yttscawlgysddtlkqlcaqalkdgWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLA 268
Cdd:cd03318 159 --------------------------HRRFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLE 212
|
250 260 270
....*....|....*....|....*....|
gi 42544119 269 KFKPLWIEEPTSPDDILGHATI-SKALVPL 297
Cdd:cd03318 213 AAGVELIEQPVPRENLDGLARLrSRNRVPI 242
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
113-425 |
8.50e-09 |
|
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: 56.86 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 113 LATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGQIGKKerekqmlaqgypaytt 192
Cdd:cd03317 94 MAKAGLEMAVWDLYAKAQGQSLAQYL--------------------------------GGTRDS---------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 193 scAWLGYS-------DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEave 262
Cdd:cd03317 126 --IPVGVSigiqddvEQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 263 wMSKLAKFKPLWIEEPTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGSVNENL 339
Cdd:cd03317 197 -LKRLDEYGLLMIEQPLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGGLTEAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 340 SVLLMAKKFEIPVCpHAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKD 411
Cdd:cd03317 270 KIHDLCQEHGIPVW-CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTG 340
|
330
....*....|....
gi 42544119 412 PGYSTEMKEESVKK 425
Cdd:cd03317 341 PGIGVTVDREALKK 354
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
6-359 |
8.76e-09 |
|
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: 57.02 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 6 ISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAEDGIKGCGITftlgkGTEVVVCAV--NALAHHVLNKDlkd 83
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFG-----GRPVTDPALvdRFLKKVLIGQD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 84 ivgdfrGFYRQLTSDGQLRWigpEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteed 163
Cdd:cd03329 74 ------PLDRERLWQDLWRL---QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLL------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 164 aleilqkGqiGKKERekqmlaqgYPAY-TTSCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQII 237
Cdd:cd03329 120 -------G--GYREK--------IPAYaSTMVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 238 RDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIGIATGEQCHNRVIFkql 316
Cdd:cd03329 183 REAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLdIPILGTEHSRGALESRADW--- 259
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 42544119 317 LQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 359
Cdd:cd03329 260 VLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGA 302
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
25-435 |
1.51e-08 |
|
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: 56.29 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 25 ADAMHTDPDYSAAYVVIETDaeDGIKGCG-ITFTlgkGTEVVVCAvnALAHHV----LNKDLKDIVGDFRGFYRqltsdG 99
Cdd:cd03322 5 IEVIVTCPGRNFVTLKITTD--QGVTGLGdATLN---GRELAVKA--YLREHLkpllIGRDANRIEDIWQYLYR-----G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 100 QLRWIGPekgVVHLATAAVLNAVWDLWAKQEGKPVWKLL--VDMDPRMLVSCIDFRYITDVLteedaleilqkgqigkkE 177
Cdd:cd03322 73 AYWRRGP---VTMNAIAAVDMALWDIKGKAAGMPLYQLLggKSRDGIMVYSHASGRDIPELL-----------------E 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 178 REKQMLAQGYpayttscawlgysddtlKQLCAQALKdgwtRFKVkvgadlqddmrrcqiIRDMIGPEKTLMMDANQRWDV 257
Cdd:cd03322 133 AVERHLAQGY-----------------RAIRVQLPK----LFEA---------------VREKFGFEFHLLHDVHHRLTP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 258 PEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVN 336
Cdd:cd03322 177 NQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGIT 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 337 ENLSVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsaslenrvceYVDHLHEHFKYPVMIQRAS 405
Cdd:cd03322 253 PARKIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR-----------HAEETLEVFPHSVRFEDGY 320
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 42544119 406 YMPPKDPGYSTEMKEESVKKHQY----------PDGEVWK 435
Cdd:cd03322 321 LHPGEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
215-278 |
1.05e-07 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 1.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42544119 215 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 278
Cdd:PRK02901 102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
36-138 |
1.05e-06 |
|
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: 47.47 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 36 AAYVVIETDAEDGIKGCGITFTLGKGTEVVVCAVNA-LAHHVLNKDLKDIVGDFRGFYRQLTsdgqlrWIGpekgvvhLA 114
Cdd:pfam02746 26 QSLVIVRIETSEGVVGIGEATSYGGRAETIKAILDDhLAPLLIGRDAANISDLWQLMYRAAL------GNM-------SA 92
|
90 100
....*....|....*....|....
gi 42544119 115 TAAVLNAVWDLWAKQEGKPVWKLL 138
Cdd:pfam02746 93 KAAIDMALWDLKAKVLNLPLADLL 116
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
207-285 |
3.47e-06 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 49.47 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 207 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 283
Cdd:PLN02980 1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176
|
..
gi 42544119 284 IL 285
Cdd:PLN02980 1177 LI 1178
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
191-282 |
2.13e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 43.08 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42544119 191 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 269
Cdd:PRK02714 110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188
|
90
....*....|....*.
gi 42544119 270 FKPL---WIEEPTSPD 282
Cdd:PRK02714 189 RLSGkieFIEQPLPPD 204
|
|
| |
