|
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 ... |
4-411 |
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: 827.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 4 GRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKD 83
Cdd:cd03324 1 IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDA-AGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 84 IVGDFRGFYRQLTSDGQLRWIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEED 163
Cdd:cd03324 80 IVADMGKFWRRLTSDSQLRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 164 AL-------------EKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGP 230
Cdd:cd03324 160 ALeilrrgqpgkaarEADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 231 EKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQ 310
Cdd:cd03324 240 DNKL-----MIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 311 AKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYP 390
Cdd:cd03324 315 AGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYP 394
|
410 420
....*....|....*....|.
gi 1370473601 391 VMIQRASYMPPKDPGYSTEMK 411
Cdd:cd03324 395 VVIQNGAYMPPTDPGYSIEMK 415
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
5-418 |
4.62e-78 |
|
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: 246.27 E-value: 4.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 5 RISRLSVRDVRFPTSLGGHGAdaMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVN-ALAHHVLNKDLKD 83
Cdd:COG4948 2 KITDIEVYPVRLPLKRPFTIS--RGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAALEeALAPLLIGRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 84 IVGDFRGFYRQLtsdgqlrwigpekGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteed 163
Cdd:COG4948 78 IEALWQRLYRAL-------------PGNPAAKAAVDMALWDLLGKALGVPVYQLL------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 164 aleKQMLAQGYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMM 241
Cdd:COG4948 120 ---GGKVRDRVPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARL-----RV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 242 DANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDS 321
Cdd:COG4948 188 DANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 322 CRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQ 394
Cdd:COG4948 265 SKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIE 335
|
410 420
....*....|....*....|....
gi 1370473601 395 RASYMPPKDPGYSTEMKEESVKKH 418
Cdd:COG4948 336 DGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
5-409 |
1.89e-64 |
|
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: 210.93 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 5 RISRLSVRDVRFPTSLGGHgadamhTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDI 84
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG------AVTWRNLVLVRVTTD--DGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 85 VGDFRGFYRQLTSDGQlrwigpeKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMdprmlvscidFRyitdvlteeda 164
Cdd:cd03316 73 ERLWEKLYRRLFWRGR-------GGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGK----------VR----------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 165 lekqmlaQGYPAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKTLslfl 238
Cdd:cd03316 125 -------DRVRVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVDL---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 239 qMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQ 318
Cdd:cd03316 193 -MVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQA---TSVPIAAGENLYTRWEFRDLLEAGAVDIIQ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 319 IDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVM 392
Cdd:cd03316 269 PDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPE 340
|
410
....*....|....*..
gi 1370473601 393 IQRASYMPPKDPGYSTE 409
Cdd:cd03316 341 IEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
189-414 |
5.78e-58 |
|
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: 189.31 E-value: 5.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 189 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWI 267
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDL-----MVDANGAWSVAEAIRLARALEELGLLWI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 268 EEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH 347
Cdd:pfam13378 76 EEPVPPDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473601 348 AGGVGLcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 414
Cdd:pfam13378 153 SGGGPI-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
39-411 |
2.67e-37 |
|
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: 139.01 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 39 VVIETDAEDGIKGCGITFtlgkGTEVVVCAV-NALAHHVLNKDLKDIVGDFRGFYRQLTSDGQlrwigpeKGVVHLATAA 117
Cdd:cd03327 12 LFVEIETDDGTVGYANTT----GGPVACWIVdQHLARFLIGKDPSDIEKLWDQMYRATLAYGR-------KGIAMAAISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 118 VLNAVWDLWAKQEGKPVWKLL---VDMDPRMLVSCIdfrYITDvLTEEDALEKQMLAQGYPAYTTScawLGYSDDtlkql 194
Cdd:cd03327 81 VDLALWDLLGKIRGEPVYKLLggrTRDKIPAYASGL---YPTD-LDELPDEAKEYLKEGYRGMKMR---FGYGPS----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 195 caqalkDGwtrfkvkvGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPD 274
Cdd:cd03327 149 ------DG--------HAGLRKNVELVRAIREAVGYDVDL-----MLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 275 DILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVglc 354
Cdd:cd03327 210 DIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQI--- 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473601 355 eLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 411
Cdd:cd03327 284 -YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
5-347 |
1.29e-27 |
|
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: 112.51 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 5 RISRLSVRDVRFPTslgghgaDAMHTDPDY---SAAYVVIETDAeDGIKGCGITFTlgkGTEVVVCAVNALAHHVLNKDL 81
Cdd:cd03328 1 AVERVEARAYTVPT-------DAPEADGTLawdATTLVLVEVRA-GGRTGLGYTYA---DAAAAALVDGLLAPVVEGRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 82 KDIVGDFRGFYRQLtsdgqlRWIGPEkGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMlvscidfryitdvlte 161
Cdd:cd03328 70 LDPPAAWEAMQRAV------RNAGRP-GVAAMAISAVDIALWDLKARLLGLPLARLLGRAHDSV---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 162 edalekqmlaqgyPAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMM 241
Cdd:cd03328 127 -------------PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAEL-----FV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 242 DANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDS 321
Cdd:cd03328 188 DANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADV 266
|
330 340
....*....|....*....|....*.
gi 1370473601 322 CRLGSVNENLSVLLMAKKFEIPVCPH 347
Cdd:cd03328 267 TRCGGVTGFLQAAALAAAHHVDLSAH 292
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
188-286 |
2.25e-25 |
|
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: 99.28 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 188 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLW 266
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADL-----MVDANGAWTAEEAIRALEALDELGLEW 75
|
90 100
....*....|....*....|
gi 1370473601 267 IEEPTSPDDILGHATISKAL 286
Cdd:smart00922 76 IEEPVPPDDLEGLAELRRAT 95
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
194-360 |
1.35e-23 |
|
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: 98.55 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 194 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMSKLAKFKPLW 266
Cdd:cd00308 54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAV-----DANGAWTPKEAIRLIRALEKYGLAW 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 267 IEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 346
Cdd:cd00308 125 IEEPCAPDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMV 201
|
170
....*....|....*.
gi 1370473601 347 HAGGVG--LCELVQHL 360
Cdd:cd00308 202 HGTLESsiGTAAALHL 217
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
38-353 |
1.17e-18 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 86.61 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 38 YVVIETDAedGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLtsdgqlRWIGpekGVVHL-ATA 116
Cdd:cd03325 16 FVKIETDE--GVVGWGEPTVEGK-ARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGG------FYRG---GPVLMsAIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 117 AVLNAVWDLWAKQEGKPVWKLLVDMDPRMLvscidfryitdvlteedalekqmlaQGYpayttscAWLG-YSDDTLKQLC 195
Cdd:cd03325 84 GIDQALWDIKGKVLGVPVHQLLGGQVRDRV-------------------------RVY-------SWIGgDRPSDVAEAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 196 AQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEktlslFLQMMDANQRWDVPEAVEWMSKLAKFKPLW 266
Cdd:cd03325 132 RARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPD-----IDIGVDFHGRVSKPMAKDLAKELEPYRLLF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 267 IEEPTSPDDILGHATISKALvplGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 346
Cdd:cd03325 207 IEEPVLPENVEALAEIAART---TIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAP 283
|
....*....
gi 1370473601 347 HA--GGVGL 353
Cdd:cd03325 284 HCplGPIAL 292
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
5-419 |
4.33e-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: 85.23 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 5 RISRLSVRDVRFPTSLGGHGADAMHTdpdySAAYVVIETDAEDGIKGCGITFTLgkgTEVVVCAVNALAHHvLNKDLKDI 84
Cdd:cd03321 2 LITGLRARAVNVPMQYPVHTSVGTVA----TAPLVLIDLATDEGVTGHSYLFTY---TPAALKSLKQLLDD-MAALLVGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 85 VGDFRGFYRQLtsDGQLRWIGpEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvDMDPRMLvscidfryitdvlteeda 164
Cdd:cd03321 74 PLAPAELERAL--AKRFRLLG-YTGLVRMAAAGIDMAAWDALAKVHGLPLAKLL-GGNPRPV------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 165 lekqmlaqgyPAYTTScawlGYSddtLKQLCA----QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLslflq 239
Cdd:cd03321 132 ----------QAYDSH----GLD---GAKLATeravTAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGL----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 240 MMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIgiatGEQCHNRVIFKQLLQAKALQFLQ 318
Cdd:cd03321 190 MVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALrTPVQM----GENWLGPEEMFKALSAGACDLVM 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 319 IDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqhliIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQR 395
Cdd:cd03321 266 PDLMKIGGVTGWLRASALAEQAGIPMSSH--------------LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFED 331
|
410 420
....*....|....*....|....
gi 1370473601 396 ASYMPPKDPGYSTEMKEESVKKHQ 419
Cdd:cd03321 332 GNAVIPDEPGNGIIWREKAVRKYL 355
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
109-360 |
2.84e-17 |
|
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: 81.23 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 109 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfrYITDVLTEEDALEKQMlaqgypayttscawlgysd 188
Cdd:cd03315 39 GWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVA-----HMLGLGEPAEVAEEAR------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 189 dtlkqlcaQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEktLSLFLqmmDANQRWDVPEAVEWMSKLAKFKPLWIE 268
Cdd:cd03315 95 --------RALEAGFRTFKLKVGRDPARDVAVVAALREAVGDD--AELRV---DANRGWTPKQAIRALRALEDLGLDYVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 269 EPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV---C 345
Cdd:cd03315 162 QPLPADDLEGRAALARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVmvgS 238
|
250
....*....|....*
gi 1370473601 346 PHAGGVGLCELVqHL 360
Cdd:cd03315 239 MIESGLGTLANA-HL 252
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
114-297 |
5.23e-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: 73.20 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 114 ATAAVLNAVWDLWAKQEGKPVWKLLVD------MDPRMLVSCidfryitdvlteedalekqmlAQGYPayttscawlgYS 187
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLARrygrgqADPRVPVYA---------------------AGGYY----------YP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 188 DDTLKQLCAQA---LKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMSKLAKFK 263
Cdd:cd03326 158 GDDLGRLRDEMrryLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAV-----DANGRFDLETAIAYAKALAPYG 232
|
170 180 190
....*....|....*....|....*....|....
gi 1370473601 264 PLWIEEPTSPDDILGHATISKALVPlgiGIATGE 297
Cdd:cd03326 233 LRWYEEPGDPLDYALQAELADHYDG---PIATGE 263
|
|
| 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 ... |
114-302 |
5.97e-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: 72.22 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 114 ATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfryitdvlteedalekqmlaqgypAYTTScawLGySDDTLKQ 193
Cdd:cd03319 92 ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLET---------------------------DYTIS---ID-TPEAMAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 194 LCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIgPEKTLSLflqmmDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSP 273
Cdd:cd03319 141 AAKKAAKRGFPLLKIKLGGDLEDDIERIRAIREAA-PDARLRV-----DANQGWTPEEAVELLRELAELGVELIEQPVPA 214
|
170 180
....*....|....*....|....*....
gi 1370473601 274 DDILGHATISKAlvpLGIGIATGEQCHNR 302
Cdd:cd03319 215 GDDDGLAYLRDK---SPLPIMADESCFSA 240
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
179-344 |
1.41e-13 |
|
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: 70.37 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 179 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMS 257
Cdd:cd03320 74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRL-----DANGGWSLEEALAFLE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 258 KLAKFKPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVN 328
Cdd:cd03320 149 ALAAGRIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPR 214
|
170
....*....|....*.
gi 1370473601 329 ENLSVLLMAKKFEIPV 344
Cdd:cd03320 215 ALLELAEEARARGIPA 230
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
22-351 |
1.86e-13 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 71.68 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 22 GHGADAMHTDPDYSAA----------YVVIETDAEDGIKGCGITfTLGKGTEVVVcaVNALAHHVLNKDLKDIVGDFRGF 91
Cdd:PRK15440 32 DHIATPMSKYPEYRQSrqsfginvlgTLVVEVEAENGQVGFAVS-TAGEMGAFIV--EKHLNRFIEGKCVSDIELIWDQM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 92 YRQLTSDGQlrwigpeKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMdprmlvscidfryITDVLTeedalekqmla 171
Cdd:PRK15440 109 LNATLYYGR-------KGLVMNTISCVDLALWDLLGKVRGLPVYKLLGGA-------------VRDELQ----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 172 qgypAYTTscawlGYSDDTLKQLcaqalkdGWTRFKVKV-------GADLQDDMRRCQIIRDMIGPEktlslFLQMMDAN 244
Cdd:PRK15440 158 ----FYAT-----GARPDLAKEM-------GFIGGKMPLhhgpadgDAGLRKNAAMVADMREKVGDD-----FWLMLDCW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 245 QRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRL 324
Cdd:PRK15440 217 MSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEHEATLQGFRTLLEMGCIDIIQPDVGWC 295
|
330 340
....*....|....*....|....*..
gi 1370473601 325 GSVNENLSVLLMAKKFEIPVCPHAGGV 351
Cdd:PRK15440 296 GGLTELVKIAALAKARGQLVVPHGSSV 322
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
41-417 |
3.38e-13 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 70.70 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 41 IETDaeDGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFR-----GFYRqltsdGqlrwiGPekgvVHL-A 114
Cdd:PRK14017 20 IETD--EGIVGWGEPVVEGR-ARTVEAAVHELADYLIGKDPRRIEDHWQvmyrgGFYR-----G-----GP----ILMsA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 115 TAAVLNAVWDLWAKQEGKPVWKLL----VDmdpRMLVscidfryitdvlteedalekqmlaqgypaYttscAWLGYSDDT 190
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELLgglvRD---RIRV-----------------------------Y----SWIGGDRPA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 191 LKQLCAQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMSKLA 260
Cdd:PRK14017 127 DVAEAARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGV-----DFHGRVHKPMAKVLAKELE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 261 KFKPLWIEEPTSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVL 334
Cdd:PRK14017 202 PYRPMFIEEPVLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 335 LMAKKFEIPVCPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASYM-PP 401
Cdd:PRK14017 273 AMAEAYDVALAPHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGFVaIP 343
|
410
....*....|....*.
gi 1370473601 402 KDPGYSTEMKEESVKK 417
Cdd:PRK14017 344 TGPGLGIEIDEAKVRE 359
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
38-289 |
1.67e-10 |
|
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: 62.33 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 38 YVVIETDAEDGIKGCGITFTLGK---GTEVVVCAVNA----LAHHVLNKDLKDIVGDFRGFYRQLTSDgqlrwigpekgv 110
Cdd:cd03318 30 LVLVRLTTSDGVVGIGEATTPGGpawGGESPETIKAIidryLAPLLIGRDATNIGAAMALLDRAVAGN------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 111 vHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdPRMLVSCIDFRY-ITDVLTEED-ALEKQMLAQGYpayttscawlgysd 188
Cdd:cd03318 98 -LFAKAAIEMALLDAQGRRLGLPVSELL----GGRVRDSLPVAWtLASGDTERDiAEAEEMLEAGR-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 189 dtlkqlcaqalkdgWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWI 267
Cdd:cd03318 159 --------------HRRFKLKMGArPPADDLAHVEAIAKALGDRASV-----RVDVNQAWDESTAIRALPRLEAAGVELI 219
|
250 260
....*....|....*....|...
gi 1370473601 268 EEPTSPDDILGHATI-SKALVPL 289
Cdd:cd03318 220 EQPVPRENLDGLARLrSRNRVPI 242
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
25-427 |
3.41e-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: 55.14 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 25 ADAMHTDPDYSAAYVVIETDaeDGIKGCG-ITFTlgkGTEVVVCAvnALAHHV----LNKDLKDIVGDFRGFYRqltsdG 99
Cdd:cd03322 5 IEVIVTCPGRNFVTLKITTD--QGVTGLGdATLN---GRELAVKA--YLREHLkpllIGRDANRIEDIWQYLYR-----G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 100 QLRWIGPekgVVHLATAAVLNAVWDLWAKQEGKPVWKLL--VDMDPRMLVSCIDFRYITDVLteeDALEKQMlAQGYpay 177
Cdd:cd03322 73 AYWRRGP---VTMNAIAAVDMALWDIKGKAAGMPLYQLLggKSRDGIMVYSHASGRDIPELL---EAVERHL-AQGY--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 178 ttscawlgysddtlKQLCAQALKdgwtRFKVkvgadlqddmrrcqiIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMS 257
Cdd:cd03322 143 --------------RAIRVQLPK----LFEA---------------VREKFGFEFHL-----LHDVHHRLTPNQAARFGK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 258 KLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLM 336
Cdd:cd03322 185 DVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 337 AKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsaslenrvceYVDHLHEHFKYPVMIQRASYMPPKDPG 405
Cdd:cd03322 261 ASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR-----------HAEETLEVFPHSVRFEDGYLHPGEEPG 328
|
410 420 430
....*....|....*....|....*....|..
gi 1370473601 406 YSTEMKEESVKKHQY----------PDGEVWK 427
Cdd:cd03322 329 LGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
113-417 |
6.84e-08 |
|
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: 54.16 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 113 LATAAVLNAVWDLWAKQEGKPVWKLL------------VDMDPRMlvscidfryitdvlteedalekqmlaqgypaytts 180
Cdd:cd03317 94 MAKAGLEMAVWDLYAKAQGQSLAQYLggtrdsipvgvsIGIQDDV----------------------------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 181 cawlgysDDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLslflqMMDAN---QRWDVPEavewMS 257
Cdd:cd03317 139 -------EQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPL-----MADANsayTLADIPL----LK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 258 KLAKFKPLWIEEPTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGSVNENLSVL 334
Cdd:cd03317 199 RLDEYGLLMIEQPLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGGLTEALKIH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 335 LMAKKFEIPVCpHAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKDPGY 406
Cdd:cd03317 273 DLCQEHGIPVW-CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTGPGI 343
|
330
....*....|.
gi 1370473601 407 STEMKEESVKK 417
Cdd:cd03317 344 GVTVDREALKK 354
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
6-351 |
9.31e-08 |
|
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: 53.94 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 6 ISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAEDGIKGCGITftlgkGTEVVVCAV--NALAHHVLNKDlkd 83
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFG-----GRPVTDPALvdRFLKKVLIGQD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 84 ivgdfrGFYRQLTSDGQLRWigpEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDmdprmlvscidFRyitdvlteeD 163
Cdd:cd03329 74 ------PLDRERLWQDLWRL---QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGG-----------YR---------E 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 164 ALekqmlaqgyPAY-TTSCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLslf 237
Cdd:cd03329 125 KI---------PAYaSTMVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRL--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 238 lqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIGIATGEQCHNRVIFkqlLQAKALQF 316
Cdd:cd03329 193 --MHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLdIPILGTEHSRGALESRADW---VLAGATDF 267
|
330 340 350
....*....|....*....|....*....|....*
gi 1370473601 317 LQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 351
Cdd:cd03329 268 LRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGA 302
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
36-138 |
9.92e-07 |
|
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: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 36 AAYVVIETDAEDGIKGCGITFTLGKGTEVVVCAVNA-LAHHVLNKDLKDIVGDFRGFYRQLTsdgqlrWIGpekgvvhLA 114
Cdd:pfam02746 26 QSLVIVRIETSEGVVGIGEATSYGGRAETIKAILDDhLAPLLIGRDAANISDLWQLMYRAAL------GNM-------SA 92
|
90 100
....*....|....*....|....
gi 1370473601 115 TAAVLNAVWDLWAKQEGKPVWKLL 138
Cdd:pfam02746 93 KAAIDMALWDLKAKVLNLPLADLL 116
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
202-270 |
9.15e-06 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 9.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473601 202 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLSlflqmMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 270
Cdd:PRK02901 102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVR-----VDANGGWSVDEAVAAARALDADGPLeYVEQP 169
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
194-277 |
2.54e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 43.69 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 194 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLSlflqmMDANQRWDVPEAVEWMSKLAKFKPLWIEEP- 270
Cdd:PLN02980 1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELR-----ADANRNWTYEEAIEFGSLVKSCNLKYIEEPv 1171
|
....*..
gi 1370473601 271 TSPDDIL 277
Cdd:PLN02980 1172 QDEDDLI 1178
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
162-274 |
2.85e-03 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 39.61 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473601 162 EDALEKQMLAQGYPAYT--TSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLSLfl 238
Cdd:PRK02714 92 ESALENESGSRSNVTLNplSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRL-- 168
|
90 100 110
....*....|....*....|....*....|....*....
gi 1370473601 239 qmmDANQRWDVPEAVEWMSKLAKFKPL---WIEEPTSPD 274
Cdd:PRK02714 169 ---DANGGLSLEEAKRWLQLCDRRLSGkieFIEQPLPPD 204
|
|
| |
