|
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 ... |
4-453 |
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: 801.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 4 GRISRLSVRDVRFPTSLGGHGADAMvsadamvsadamvsadamvsadamvsadamvsadamvsadamvsadamHTDPDYS 83
Cdd:cd03324 1 IKITALEVRDVRFPTSLELDGSDAM------------------------------------------------NPDPDYS 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 84 AAYVVIETDAeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQLRWIGPEKGVVHLAT 163
Cdd:cd03324 33 AAYVVLRTDA-AGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIVADMGKFWRRLTSDSQLRWIGPEKGVIHLAT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 164 AAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREKQMLAQGYPAYTTSCA 243
Cdd:cd03324 112 AAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREADLLAEGYPAYTTSAG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 244 WLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWI 323
Cdd:cd03324 192 WLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 324 EEPTSPDDILGHATISK--------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH 389
Cdd:cd03324 272 EEPTSPDDILGHAAIRKalaplpigvatgehCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPH 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1227523124 390 AGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 453
Cdd:cd03324 352 AGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
75-460 |
2.03e-68 |
|
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: 222.78 E-value: 2.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 75 AMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVN-ALAHHVLNKDLKDIVGDFRGFYRQLtsdgqlrwig 153
Cdd:COG4948 22 SRGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAALEeALAPLLIGRDPLDIEALWQRLYRAL---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 154 pekGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlaq 233
Cdd:COG4948 90 ---PGNPAAKAAVDMALWDLLGKALGVPVYQLL-----------------------------------GGKVRDR----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 234 gYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEW 311
Cdd:COG4948 127 -VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 312 MSKLAKFKPLWIEEPTSPDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAK 380
Cdd:COG4948 202 LRALEDLGLEWIEQPLPAEDLEGLAELRRatpvpiaadesLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 381 KFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASYMPPKDPGYSTEMK 453
Cdd:COG4948 282 AHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLGVELD 352
|
....*..
gi 1227523124 454 EESVKKH 460
Cdd:COG4948 353 EDALARY 359
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
77-451 |
9.29e-58 |
|
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: 194.75 E-value: 9.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 77 HTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQlrwigpeK 156
Cdd:cd03316 19 GAVTWRNLVLVRVTTD--DGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLYRRLFWRGR-------G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 157 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlaqgYP 236
Cdd:cd03316 90 GVAMAAISAVDIALWDIKGKAAGVPVYKLL-----------------------------------GGKVRDR------VR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 237 AYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVE 310
Cdd:cd03316 129 VYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 311 WMSKLAKFKPLWIEEPTSPDDILGHATISKC-----------HNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMA 379
Cdd:cd03316 208 LARALEEYDLFWFEEPVPPDDLEGLARLRQAtsvpiaagenlYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALA 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227523124 380 KKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVMIQRASYMPPKDPGYSTE 451
Cdd:cd03316 288 EAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
250-456 |
1.84e-51 |
|
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: 173.52 E-value: 1.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 250 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 328
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 329 PDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLcE 397
Cdd:pfam13378 81 PDDLEGLARLRRatpvpiatgesLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI-G 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 398 LVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 456
Cdd:pfam13378 160 LAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
87-453 |
1.57e-33 |
|
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: 129.38 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 87 VVIETDAEDGIKGCGITFtlgkGTEVVVCAV-NALAHHVLNKDLKDIVGDFRGFYRQLTSDGQlrwigpeKGVVHLATAA 165
Cdd:cd03327 12 LFVEIETDDGTVGYANTT----GGPVACWIVdQHLARFLIGKDPSDIEKLWDQMYRATLAYGR-------KGIAMAAISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 166 VLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlaqgYPAYTTScawL 245
Cdd:cd03327 81 VDLALWDLLGKIRGEPVYKLL-----------------------------------GGRTRDK------IPAYASG---L 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 246 GYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 317
Cdd:cd03327 117 YPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 318 FKPLWIEEPTSPDDILGHATISKC-----------HNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV 386
Cdd:cd03327 197 YELRWIEEPLIPDDIEGYAELKKAtgipistgeheYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPV 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227523124 387 CPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 453
Cdd:cd03327 277 VPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
249-340 |
4.82e-26 |
|
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: 101.59 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 249 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 328
Cdd:smart00922 2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81
|
90
....*....|..
gi 1227523124 329 PDDILGHATISK 340
Cdd:smart00922 82 PDDLEGLAELRR 93
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
255-402 |
3.63e-21 |
|
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: 92.01 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 255 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 327
Cdd:cd00308 54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 328 SPDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVG-- 394
Cdd:cd00308 130 APDDLEGYAALRRrtgipiaadesVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESsi 209
|
....*...
gi 1227523124 395 LCELVQHL 402
Cdd:cd00308 210 GTAAALHL 217
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
87-389 |
5.10e-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: 91.32 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 87 VVIETDAeDGIKGCGITFTlgkGTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLtsdgqlRWIGPEkGVVHLATAAV 166
Cdd:cd03328 31 VLVEVRA-GGRTGLGYTYA---DAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAV------RNAGRP-GVAAMAISAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 167 LNAVWDLWAKQEGKPVWKLLVDMDPRMlvscidfryitdvlteedaleilqkgqigkkerekqmlaqgyPAYTtSCAWLG 246
Cdd:cd03328 100 DIALWDLKARLLGLPLARLLGRAHDSV------------------------------------------PVYG-SGGFTS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 247 YSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP 326
Cdd:cd03328 137 YDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEP 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227523124 327 TSPDDILGHATISK-------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH 389
Cdd:cd03328 217 VSSDDLAGLRLVRErgpagmdiaageyAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH 292
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
86-390 |
2.23e-15 |
|
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: 77.37 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 86 YVVIETDAedGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFRGFYRQLtsdgqlRWIGpekGVVHL-ATA 164
Cdd:cd03325 16 FVKIETDE--GVVGWGEPTVEGK-ARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGG------FYRG---GPVLMsAIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 165 AVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlAQGYpayttscAW 244
Cdd:cd03325 84 GIDQALWDIKGKVLGVPVHQLL-----------------------------------GGQVRDR---VRVY-------SW 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 245 LG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSK 314
Cdd:cd03325 119 IGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 315 LAKFKPLWIEEPTSPDDILGHATISKCHNRVI-----------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFE 383
Cdd:cd03325 199 LEPYRLLFIEEPVLPENVEALAEIAARTTIPIatgerlfsrwdFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYD 278
|
....*..
gi 1227523124 384 IPVCPHA 390
Cdd:cd03325 279 VALAPHC 285
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
240-335 |
2.32e-14 |
|
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: 73.06 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 240 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 318
Cdd:cd03320 74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153
|
90
....*....|....*..
gi 1227523124 319 KPLWIEEPTSPDDILGH 335
Cdd:cd03320 154 RIEYIEQPLPPDDLAEL 170
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
84-461 |
2.70e-14 |
|
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: 74.06 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 84 AAYVVIETDAEDGIKGCGITFTLgkgTEVVVCAVNALAHHvLNKDLKDIVGDFRGFYRQLtsDGQLRWIGpEKGVVHLAT 163
Cdd:cd03321 29 APLVLIDLATDEGVTGHSYLFTY---TPAALKSLKQLLDD-MAALLVGEPLAPAELERAL--AKRFRLLG-YTGLVRMAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 164 AAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREkqmlaqgYPAYTTSca 243
Cdd:cd03321 102 AGIDMAAWDALAKVHGLPLAKLL-----------------------------------GGNPRP-------VQAYDSH-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 244 wlGYSddtLKQLCA----QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 318
Cdd:cd03321 138 --GLD---GAKLATeravTAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 319 KPLWIEEPTSPDDILGHATISKCHNRVI-----------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVC 387
Cdd:cd03321 213 GLTWIEEPTLQHDYEGHARIASALRTPVqmgenwlgpeeMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMS 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227523124 388 PHaggvglcelvqhliIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 461
Cdd:cd03321 293 SH--------------LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
157-402 |
5.15e-14 |
|
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: 71.99 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 157 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfrYITDVLTEEDALEilqkgqigkkerekqmlaqgyp 236
Cdd:cd03315 39 GWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVA-----HMLGLGEPAEVAE---------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 237 ayttscawlgysddtlkqLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLA 316
Cdd:cd03315 92 ------------------EARRALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 317 KFKPLWIEEPTSPDDILGHAtisKCHNRVI--------------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKF 382
Cdd:cd03315 154 DLGLDYVEQPLPADDLEGRA---ALARATDtpimadesaftphdAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEAL 230
|
250 260
....*....|....*....|...
gi 1227523124 383 EIPV---CPHAGGVGLCELVqHL 402
Cdd:cd03315 231 GLPVmvgSMIESGLGTLANA-HL 252
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
162-342 |
2.93e-13 |
|
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: 71.27 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 162 ATAAVLNAVWDLWAKQEGKPVWKLLVDmdprmlvscidfRYitdvlteedaleilqkGQIGKKEREKQMLAQGYPaytts 241
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLAR------------RY----------------GRGQADPRVPVYAAGGYY----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 242 cawlgYSDDTLKQLCAQA---LKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 317
Cdd:cd03326 156 -----YPGDDLGRLRDEMrryLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAP 230
|
170 180
....*....|....*....|....*
gi 1227523124 318 FKPLWIEEPTSPDDILGHATISKCH 342
Cdd:cd03326 231 YGLRWYEEPGDPLDYALQAELADHY 255
|
|
| 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 ... |
162-332 |
2.72e-12 |
|
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: 67.60 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 162 ATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIdfryiTDVLTEEDALeilqkgqigkKEREKQMLAQGYPAytts 241
Cdd:cd03319 92 ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDY-----TISIDTPEAM----------AAAAKKAAKRGFPL---- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 242 cawlgysddtlkqlcaqalkdgwtrFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL 321
Cdd:cd03319 153 -------------------------LKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVE 206
|
170
....*....|.
gi 1227523124 322 WIEEPTSPDDI 332
Cdd:cd03319 207 LIEQPVPAGDD 217
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
89-459 |
5.27e-11 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 64.15 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 89 IETDaeDGIKGCGITFTLGKgTEVVVCAVNALAHHVLNKDLKDIVGDFR-----GFYRQltsdgqlrwiGPekgvVHL-A 162
Cdd:PRK14017 20 IETD--EGIVGWGEPVVEGR-ARTVEAAVHELADYLIGKDPRRIEDHWQvmyrgGFYRG----------GP----ILMsA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 163 TAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKQMlaqgypAYttsc 242
Cdd:PRK14017 83 IAGIDQALWDIKGKALGVPVHELL-----------------------------------GGLVRDRIR------VY---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 243 AWLGYSDDTLKQLCAQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEWM 312
Cdd:PRK14017 118 SWIGGDRPADVAEAARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVLA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 313 SKLAKFKPLWIEEPTSPD------DILGHATIS-----KCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKK 381
Cdd:PRK14017 198 KELEPYRPMFIEEPVLPEnaealpEIAAQTSIPiatgeRLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 382 FEIPVCPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASYM-PPKDPGY 448
Cdd:PRK14017 278 YDVALAPHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGFVaIPTGPGL 348
|
410
....*....|.
gi 1227523124 449 STEMKEESVKK 459
Cdd:PRK14017 349 GIEIDEAKVRE 359
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
86-339 |
4.79e-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: 61.18 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 86 YVVIETDAEDGIKGCGITFTLGK---GTEVVVCAVNA----LAHHVLNKDLKDIVGDFRGFYRQLTSDgqlrwigpekgv 158
Cdd:cd03318 30 LVLVRLTTSDGVVGIGEATTPGGpawGGESPETIKAIidryLAPLLIGRDATNIGAAMALLDRAVAGN------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 159 vHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdPRMLVSCIDFRY-ITDVLTEEDALEILQkgqigkkerekqMLAQGYpa 237
Cdd:cd03318 98 -LFAKAAIEMALLDAQGRRLGLPVSELL----GGRVRDSLPVAWtLASGDTERDIAEAEE------------MLEAGR-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 238 yttscawlgysddtlkqlcaqalkdgWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLA 316
Cdd:cd03318 159 --------------------------HRRFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLE 212
|
250 260
....*....|....*....|...
gi 1227523124 317 KFKPLWIEEPTSPDDILGHATIS 339
Cdd:cd03318 213 AAGVELIEQPVPRENLDGLARLR 235
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
87-393 |
1.82e-08 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 56.28 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 87 VVIETDAEDGIKGCGITfTLGKGTEVVVcaVNALAHHVLNKDLKDIVGDFRGFYRQLTSDGQlrwigpeKGVVHLATAAV 166
Cdd:PRK15440 59 LVVEVEAENGQVGFAVS-TAGEMGAFIV--EKHLNRFIEGKCVSDIELIWDQMLNATLYYGR-------KGLVMNTISCV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 167 LNAVWDLWAKQEGKPVWKLL---VDMDprmlvscIDFrYIT----DVLTEedaleilqKGQIGKKerekqMLAQGYPAyt 239
Cdd:PRK15440 129 DLALWDLLGKVRGLPVYKLLggaVRDE-------LQF-YATgarpDLAKE--------MGFIGGK-----MPLHHGPA-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 240 tscawlgysddtlkqlcaqalkDGwtrfkvkvGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFK 319
Cdd:PRK15440 186 ----------------------DG--------DAGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 320 PLWIEEPTSPDDILGHATISKC-------------HNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV 386
Cdd:PRK15440 236 LKWIEECLPPDDYWGYRELKRNapagmmvtsgeheATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLV 315
|
....*..
gi 1227523124 387 CPHAGGV 393
Cdd:PRK15440 316 VPHGSSV 322
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
161-459 |
2.53e-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: 55.70 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 161 LATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGQIGKKerekqmlaqgypaytt 240
Cdd:cd03317 94 MAKAGLEMAVWDLYAKAQGQSLAQYL--------------------------------GGTRDS---------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 241 scAWLGYS-------DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEave 310
Cdd:cd03317 126 --IPVGVSigiqddvEQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 311 wMSKLAKFKPLWIEEPTSPDDILGHATISK------CHNRVI--FKQLLQAKALQFLQ---IDSCRLGSVNENLSVLLMA 379
Cdd:cd03317 197 -LKRLDEYGLLMIEQPLAADDLIDHAELQKllktpiCLDESIqsAEDARKAIELGACKiinIKPGRVGGLTEALKIHDLC 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 380 KKFEIPVCpHAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKDPGYSTE 451
Cdd:cd03317 276 QEHGIPVW-CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTGPGIGVT 346
|
....*...
gi 1227523124 452 MKEESVKK 459
Cdd:cd03317 347 VDREALKK 354
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
263-326 |
3.60e-07 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 3.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227523124 263 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 326
Cdd:PRK02901 102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
84-186 |
2.61e-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: 46.31 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 84 AAYVVIETDAEDGIKGCGITFTLGKGTEVVVCAVNA-LAHHVLNKDLKDIVGDFRGFYRQLTsdgqlrWIGpekgvvhLA 162
Cdd:pfam02746 26 QSLVIVRIETSEGVVGIGEATSYGGRAETIKAILDDhLAPLLIGRDAANISDLWQLMYRAAL------GNM-------SA 92
|
90 100
....*....|....*....|....
gi 1227523124 163 TAAVLNAVWDLWAKQEGKPVWKLL 186
Cdd:pfam02746 93 KAAIDMALWDLKAKVLNLPLADLL 116
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
255-333 |
5.20e-06 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 49.08 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 255 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 331
Cdd:PLN02980 1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176
|
..
gi 1227523124 332 IL 333
Cdd:PLN02980 1177 LI 1178
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
71-340 |
8.84e-06 |
|
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: 47.78 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 71 VSADAMHTDPDYSA----AYVVIETDaeDGIKGCGITftlgkGTEVVVCAV--NALAHHVLNKDlkdivgdfrGFYRQLT 144
Cdd:cd03329 17 VSFDGGHHHPGPAGtrklALLTIETD--EGAKGHAFG-----GRPVTDPALvdRFLKKVLIGQD---------PLDRERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 145 SDGQLRWigpEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGqiGKK 224
Cdd:cd03329 81 WQDLWRL---QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLL--------------------------------G--GYR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 225 ERekqmlaqgYPAY-TTSCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLMMD 298
Cdd:cd03329 124 EK--------IPAYaSTMVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHD 195
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1227523124 299 ANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISK 340
Cdd:cd03329 196 GAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAE 237
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
72-469 |
1.13e-05 |
|
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: 47.43 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 72 SADAMHTDPDYSAAYVVIETDaeDGIKGCG-ITFTlgkGTEVVVCAvnALAHHV----LNKDLKDIVGDFRGFYRqltsd 146
Cdd:cd03322 4 AIEVIVTCPGRNFVTLKITTD--QGVTGLGdATLN---GRELAVKA--YLREHLkpllIGRDANRIEDIWQYLYR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 147 GQLRWIGPekgVVHLATAAVLNAVWDLWAKQEGKPVWKLL--VDMDPRMLVSCIDFRYITDVLteedaleilqkgqigkk 224
Cdd:cd03322 72 GAYWRRGP---VTMNAIAAVDMALWDIKGKAAGMPLYQLLggKSRDGIMVYSHASGRDIPELL----------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 225 EREKQMLAQGYpayttscawlgysddtlKQLCAQALKdgwtRFKVkvgadlqddmrrcqiIRDMIGPEKTLMMDANQRWD 304
Cdd:cd03322 132 EAVERHLAQGY-----------------RAIRVQLPK----LFEA---------------VREKFGFEFHLLHDVHHRLT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 305 VPEAVEWMSKLAKFKPLWIEEPTSPDD------ILGHAT----ISKCHNRVI-FKQLLQAKALQFLQIDSCRLGSVNENL 373
Cdd:cd03322 176 PNQAARFGKDVEPYRLFWMEDPTPAENqeafrlIRQHTAtplaVGEVFNSIWdWQNLIQERLIDYIRTTVSHAGGITPAR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 374 SVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsaslenrvceYVDHLHEHFKYPVMIQRASYMP 442
Cdd:cd03322 256 KIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR-----------HAEETLEVFPHSVRFEDGYLHP 323
|
410 420 430
....*....|....*....|....*....|....*..
gi 1227523124 443 PKDPGYSTEMKEESVKKHQY----------PDGEVWK 469
Cdd:cd03322 324 GEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
239-330 |
2.33e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 43.08 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523124 239 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 317
Cdd:PRK02714 110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188
|
90
....*....|....*.
gi 1227523124 318 FKPL---WIEEPTSPD 330
Cdd:PRK02714 189 RLSGkieFIEQPLPPD 204
|
|
| |
