|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-362 |
4.61e-91 |
|
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: 277.47 E-value: 4.61e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 1 MKITELHLYAHPLPVRDgPYRMASTEVWSLDTTLVKLVTDSGLIGWGETCPVGPVyqpqHAAGARAALAEMAPGLIGADP 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKR-PFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTG----AEAVAAALEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 81 LQPLRLQRRMDGLLNGHRYAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYASGVGEPDEIARIAAERADEGYPR 160
Cdd:COG4948 76 LDIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 161 MQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPC--NSIEEIAAIRGQLHHA 237
Cdd:COG4948 156 LKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLgLEWIEQPLpaEDLEGLAELRRATPVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 238 VYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMPHTCDDAWGGDIIAAACTHIGATV-QPRLM 316
Cdd:COG4948 236 IAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALpNFDIV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 499650543 317 EGV---WLAQPYIEGhfdpenGLRIEGGHIRLPEGPGLGIVPDESLFGA 362
Cdd:COG4948 316 ELDgplLLADDLVED------PLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-317 |
6.80e-57 |
|
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: 185.22 E-value: 6.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 6 LHLYAHPLPVRDGPYrMASTEVWSLDTTLVKLVTDSGLIGWGETcpvgpvyqpqhaagaraalaemapgligadplqplr 85
Cdd:cd00308 1 VEVYAVRLPTSRPFY-LAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 86 lqrrmdgllnghryaKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYAsgvgepdeiariaaeradegyprmqvki 165
Cdd:cd00308 44 ---------------ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS---------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 166 ggrpveidIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPE-IPFILEQPCNS--IEEIAAIRGQLHHAVYLDE 242
Cdd:cd00308 81 --------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKyGLAWIEEPCAPddLEGYAALRRRTGIPIAADE 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499650543 243 TAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMPHTCDDAWGGDIIAAACTHIGATVQ-PRLME 317
Cdd:cd00308 153 SVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPnDRAIE 228
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-354 |
1.04e-54 |
|
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: 183.58 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 2 KIT--ELHLYAHPLPVRDGPyrmasteVWSLDTTLVKLVTDSGLIGWGETCPVGPVYQPQHAAGAraalaEMAPGLIGAD 79
Cdd:cd03316 1 KITdvETFVLRVPLPEPGGA-------VTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIED-----LLAPLLIGRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 80 PLQPLRLQRRM-DGLLNGHRY-----AKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPsYYASGVG---EPDEIARIA 150
Cdd:cd03316 69 PLDIERLWEKLyRRLFWRGRGgvamaAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVR-VYASGGGyddSPEELAEEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 151 AERADEGYPRMQVKIGGRP-----VEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPC--N 222
Cdd:cd03316 148 KRAVAEGFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYdLFWFEEPVppD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 223 SIEEIAAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICE---VRSMPHtcddAWGGDI 299
Cdd:cd03316 228 DLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEahgVRVAPH----GAGGPI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499650543 300 IAAACTHIGATVQ-PRLMEGVWLAQPYIEGHFDpeNGLRIEGGHIRLPEGPGLGIV 354
Cdd:cd03316 304 GLAASLHLAAALPnFGILEYHLDDLPLREDLFK--NPPEIEDGYVTVPDRPGLGVE 357
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-357 |
7.43e-47 |
|
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: 163.26 E-value: 7.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 2 KITELHLYAHPLPVRDgPYRMASTEVWSLDTTLVKLVTDSGLIGWGETCPV-GPVYQPQHAAGARAALAE-MAPGLIGAD 79
Cdd:cd03318 1 KIEAIETTIVDLPTRR-PHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPgGPAWGGESPETIKAIIDRyLAPLLIGRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 80 PLQPLRLQRRMDGLLNGHRYAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYASGVGEPDEIARIAAERADEG-Y 158
Cdd:cd03318 80 ATNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 159 PRMQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPC--NSIEEIAAIRGQLH 235
Cdd:cd03318 160 RRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVprENLDGLARLRSRNR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 236 HAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMPHTCDDAWGGDIIAAACTHIGATVqPRL 315
Cdd:cd03318 240 VPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATL-PSL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499650543 316 MEGVWLAQPYIEGHFDPENGLRIEGGHIRLPEGPGLGIVPDE 357
Cdd:cd03318 319 PFGCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDE 360
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
144-357 |
1.46e-41 |
|
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: 145.02 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 144 DEIARIAAERADEGYPRMQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPCN 222
Cdd:pfam13378 1 ELAAEARRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 223 S--IEEIAAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICE---VRSMPHtcddAWGG 297
Cdd:pfam13378 81 PddLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEafgVPVAPH----SGGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 298 DIIAAACTHIGATVqPRLMEGVWLAQPYIEGHFDPENGLRIEGGHIRLPEGPGLGIVPDE 357
Cdd:pfam13378 157 PIGLAASLHLAAAV-PNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
5-288 |
5.00e-36 |
|
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: 133.08 E-value: 5.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 5 ELHLYAHPLPVRdGPYRMASTEVWSLDTTLVKLVTDsGLIGWGETCPVGPVYQpQHAAGARAALAEMAPGLIGADPLQPL 84
Cdd:cd03319 1 KISLRPERLPLK-RPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTG-ETVESVLAALKSVRPALIGGDPRLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 85 RLQRrMDGLLNGHRYAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYASGVGEPDEIARIAAERADEGYPRMQVK 164
Cdd:cd03319 78 LLEA-LQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 165 IGGrPVEIDIETIRKVWERVGTrMRLAVDGNRGLTTRDALRLSRECPE--IPFIlEQPCNS--IEEIAAIRGQLHHAVYL 240
Cdd:cd03319 157 LGG-DLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELLRELAElgVELI-EQPVPAgdDDGLAYLRDKSPLPIMA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499650543 241 DETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMP 288
Cdd:cd03319 234 DESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLK 281
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
19-310 |
8.49e-32 |
|
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: 120.52 E-value: 8.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 19 PYRMASTEVWSLDTTLVKLVTDSGLIGWGETcpvgpvyqpqhaagaraalaemapgligadplqplrlqrrmdgllnghr 98
Cdd:cd03315 13 PLKWASGTLTTADHVLLRLHTDDGLVGWAEA------------------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 99 yAKAAIDIAAHDLMGKAWGVRVADLLGGaVTERVPSYYASGVGEPDEIARIAAERADEGYPRMQVKIGGRPvEIDIETIR 178
Cdd:cd03315 44 -TKAAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDP-ARDVAVVA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 179 KVWERVGTRMRLAVDGNRGLTTRDALRLSRECPE--IPFIlEQPC--NSIEEIAAIRGQLHHAVYLDETAEDVATVLRAV 254
Cdd:cd03315 121 ALREAVGDDAELRVDANRGWTPKQAIRALRALEDlgLDYV-EQPLpaDDLEGRAALARATDTPIMADESAFTPHDAFREL 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499650543 255 GQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMPHTCDDAWGGDIIAAACTHIGAT 310
Cdd:cd03315 200 ALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAA 255
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
34-353 |
2.04e-24 |
|
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: 102.40 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 34 LVKLVTDSGLIGWGEtcpvgPVYQpQHAAGARAALAEMAPGLIGADPLqplRLQRRMDGLLNGHRY--------AKAAID 105
Cdd:cd03325 16 FVKIETDEGVVGWGE-----PTVE-GKARTVEAAVQELEDYLIGKDPM---NIEHHWQVMYRGGFYrggpvlmsAISGID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 106 IAAHDLMGKAWGVRVADLLGGAVTERVPSYYASGVGEPDEIARIAAERADEGY--------PRMQVKIGGRPVEIDIETI 177
Cdd:cd03325 87 QALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFtavkmnatEELQWIDTSKKVDAAVERV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 178 RKVWERVGTRMRLAVDGNRGLTTRDALRLSREC-PEIPFILEQPC--NSIEEIAAIRGQLHHAVYLDE---TAEDVATVL 251
Cdd:cd03325 167 AALREAVGPDIDIGVDFHGRVSKPMAKDLAKELePYRLLFIEEPVlpENVEALAEIAARTTIPIATGErlfSRWDFKELL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 252 RavgQGVCDGFGMKVTRIGG---LRPMAVFRDICEVRSMPHTCDdawgGDIIAAACTHIGAT-----VQPRLMEGV-WLA 322
Cdd:cd03325 247 E---DGAVDIIQPDISHAGGiteLKKIAAMAEAYDVALAPHCPL----GPIALAASLHVDAStpnflIQEQSLGIHyNEG 319
|
330 340 350
....*....|....*....|....*....|.
gi 499650543 323 QPYIEGHFDPEnGLRIEGGHIRLPEGPGLGI 353
Cdd:cd03325 320 DDLLDYLVDPE-VFDMENGYVKLPTGPGLGI 349
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
31-357 |
2.93e-23 |
|
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: 99.23 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 31 DTTLVKLVTDSGLIGWGE-TCPVGPVYQPQHAAGARAALAE-MAPGLIGADPLQPLRLQRRMDGLLnGHRYAKAAIDIAA 108
Cdd:cd03317 25 EFLIVELTDEEGITGYGEvVAFEGPFYTEETNATAWHILKDyLLPLLLGREFSHPEEVSERLAPIK-GNNMAKAGLEMAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 109 HDLMGKAWGVRVADLLGGaVTERVPSYYASGVGE-PDEIARIAAERADEGYPRMQVKIggRPvEIDIETIRKVWERVGTr 187
Cdd:cd03317 104 WDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDdVEQLLKQIERYLEEGYKRIKLKI--KP-GWDVEPLKAVRERFPD- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 188 MRLAVDGNRGLTTRDALRLSR------ECPEIPFileqPCNSIEEIAAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDG 261
Cdd:cd03317 179 IPLMADANSAYTLADIPLLKRldeyglLMIEQPL----AADDLIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 262 FGMKVTRIGGLRPMAVFRDICEVRSMPhtcddAWGGDIIAAActhIG--ATVQPRLMEGVWLA-------QPYIEGHFDP 332
Cdd:cd03317 255 INIKPGRVGGLTEALKIHDLCQEHGIP-----VWCGGMLESG---IGraHNVALASLPNFTYPgdisassRYFEEDIITP 326
|
330 340
....*....|....*....|....*
gi 499650543 333 EngLRIEGGHIRLPEGPGLGIVPDE 357
Cdd:cd03317 327 P--FELENGIISVPTGPGIGVTVDR 349
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-352 |
2.74e-20 |
|
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: 90.92 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 2 KIT--ELHLYAHPL-PVRDGPYRMASTEVWSLDTTLVKLVTDSGLIGWGETcpvGPVYQPQHAAGARaalaeMAPGLIGA 78
Cdd:cd03329 1 KITdvEVTVFEYPTqPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFG---GRPVTDPALVDRF-----LKKVLIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 79 DPLQPLRLQRRMDGLLNGH-RYAKAAIDIAAHDLMGKAWGVRVADLLGGaVTERVPSY-------YASGVGEPDEIARIA 150
Cdd:cd03329 73 DPLDRERLWQDLWRLQRGLtDRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYastmvgdDLEGLESPEAYADFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 151 AERADEGYPRMQVKIGGRP-VEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEIPFI-LEQPCN--SIEE 226
Cdd:cd03329 152 EECKALGYRAIKLHPWGPGvVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFwYEDPLReaSISS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 227 IAAIRGQLHHAVYLDETAeDVATVLRA--VGQGVCDGFGMKVTRIGGLRPM-------AVFRDICEVrsmpHTCDdawgg 297
Cdd:cd03329 232 YRWLAEKLDIPILGTEHS-RGALESRAdwVLAGATDFLRADVNLVGGITGAmktahlaEAFGLDVEL----HGNG----- 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 298 diiaAACTHIGATVQPRLMEGVWLAQPYIEGHFDPENGLRIE-----GGHIRLPEGPGLG 352
Cdd:cd03329 302 ----AANLHVIAAIRNTRYYERGLLHPSQKYDVYAGYLSVLDdpvdsDGFVHVPKGPGLG 357
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-357 |
1.67e-19 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 88.80 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 1 MKITELHLYAhpLPVRdgpyrmastevWsldtTLVKLVTDSGLIGWGEtcpvgPVYQpQHAAGARAALAEMAPGLIGADP 80
Cdd:PRK14017 1 MKITKLETFR--VPPR-----------W----LFLKIETDEGIVGWGE-----PVVE-GRARTVEAAVHELADYLIGKDP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 81 LQPLRLQRRM--DGLLNG---HRYAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYASGVGEPDEIARIAAERAD 155
Cdd:PRK14017 58 RRIEDHWQVMyrGGFYRGgpiLMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 156 EGYprMQVKIGG----------RPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSREC-PEIPFILEQPCNSi 224
Cdd:PRK14017 138 RGF--TAVKMNGteelqyidspRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELePYRPMFIEEPVLP- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 225 eeiaairgqlHHAVYLDETAEDVATVLrAVGQGVCDGFGMK--------------VTRIGGlrpmavfrdICEVR---SM 287
Cdd:PRK14017 215 ----------ENAEALPEIAAQTSIPI-ATGERLFSRWDFKrvleaggvdiiqpdLSHAGG---------ITECRkiaAM 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 288 PHTCDDAWG-----GDIIAAACTHIGATVQPRLMEGVWLAQPYIEGH------FDPENgLRIEGGHIRLPEGPGLGIVPD 356
Cdd:PRK14017 275 AEAYDVALAphcplGPIALAACLQVDAVSPNAFIQEQSLGIHYNQGAdlldyvKNKEV-FAYEDGFVAIPTGPGLGIEID 353
|
.
gi 499650543 357 E 357
Cdd:PRK14017 354 E 354
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
2-353 |
1.08e-18 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 86.61 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 2 KITELHLYahPLPVRDGPYRMASTEVWSLDT-TLVKLVTDSGLIGWGEtCPVGpvyqpqhaAGARAALAEMAPGLIG--- 77
Cdd:cd03323 1 KITEMRVT--PVAGHDSPLLNLSGAHEPFFTrNIVELTDDNGNTGVGE-SPGG--------AEALEALLEAARSLVGgdv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 78 ---------------ADPLQPLRLQRRMDGLLNGHryAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVP--------- 133
Cdd:cd03323 70 fgaylavlesvrvafADRDAGGRGLQTFDLRTTVH--VVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPflaylfykg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 134 ---------SYYASGVGE---PDEIARIaAERADE--GYPRMQVKIGGRPVEIDIETIRKVWERVgTRMRLAVDGNRGLT 199
Cdd:cd03323 148 drhktdlpyPWFRDRWGEaltPEGVVRL-ARAAIDryGFKSFKLKGGVLPGEEEIEAVKALAEAF-PGARLRLDPNGAWS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 200 TRDALRLSRECPEIPFILEQPCNSIEEIAAIRG----------------QLHHAVYLDetAEDVA-------TVLRA--- 253
Cdd:cd03323 226 LETAIRLAKELEGVLAYLEDPCGGREGMAEFRRatglplatnmivtdfrQLGHAIQLN--AVDIPladhhfwGGMRGsvr 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 254 VGQgVCDGFGMKVTrigglrpmavfrdiceVRSMPHTcddawggDIIAAACTHIGATVqPRLMEGV-----WLAQPYIEG 328
Cdd:cd03323 304 VAQ-VCETWGLGWG----------------MHSNNHL-------GISLAMMTHVAAAA-PGLITACdthwiWQDGQVITG 358
|
410 420
....*....|....*....|....*
gi 499650543 329 hfdpeNGLRIEGGHIRLPEGPGLGI 353
Cdd:cd03323 359 -----EPLRIKDGKVAVPDKPGLGV 378
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
24-353 |
4.68e-17 |
|
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: 81.23 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 24 STEVWSlDTTLVKLVTDSGLIGWGETC--PVGPVYQPQHaagaraalaeMAPGLIGADPLQPLRLQRRM--DGLLNGHR- 98
Cdd:cd03327 4 SVRTRV-GWLFVEIETDDGTVGYANTTggPVACWIVDQH----------LARFLIGKDPSDIEKLWDQMyrATLAYGRKg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 99 ---YAKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSYYA-SGVGEPDEIARIAAERADEGYPRMQVKIGGRPVEID- 173
Cdd:cd03327 73 iamAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYLKEGYRGMKMRFGYGPSDGHa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 174 -----IETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPC--NSIEEIAAIR---------GQLHH 236
Cdd:cd03327 153 glrknVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYeLRWIEEPLipDDIEGYAELKkatgipistGEHEY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 237 AVY-----LDETAEDVATvlravgqgvCDgfgmkVTRIGGLRPMAVFRDICEVRS---MPHTCDDAWGGDIIAAACTHIg 308
Cdd:cd03327 233 TVYgfkrlLEGRAVDILQ---------PD-----VNWVGGITELKKIAALAEAYGvpvVPHASQIYNYHFIMSEPNSPF- 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499650543 309 ATVQPRLMegVWLAQPYIEGHFdpENGLRIEGGHIRLPEGPGLGI 353
Cdd:cd03327 298 AEYLPNSP--DEVGNPLFYYIF--LNEPVPVNGYFDLSDKPGFGL 338
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-357 |
8.27e-16 |
|
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: 77.52 E-value: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 1 MKITELHLYAHPLPVRDgPYRMASTEVWSLDTTLVKLVTDSGLIGWGETCpvgpVYQPQHAAGARAALAEMAPGLIGaDP 80
Cdd:cd03321 1 VLITGLRARAVNVPMQY-PVHTSVGTVATAPLVLIDLATDEGVTGHSYLF----TYTPAALKSLKQLLDDMAALLVG-EP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 81 LQPLRLQRRMD------GLLNGHRYAKAAIDIAAHDLMGKAWGVRVADLLGGaVTERVPSYYASGVGepdeIARIAAERA 154
Cdd:cd03321 75 LAPAELERALAkrfrllGYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLGG-NPRPVQAYDSHGLD----GAKLATERA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 155 ----DEGYPRMQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECP-EIPFILEQPC--NSIEEI 227
Cdd:cd03321 150 vtaaEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDqEGLTWIEEPTlqHDYEGH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 228 AAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGG----LRPMAvfrdICEVRSMPHTcddawggdiiaaa 303
Cdd:cd03321 230 ARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGvtgwLRASA----LAEQAGIPMS------------- 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499650543 304 cTHIGATVQPRLM---------EGVWLAQPYIeghfdpENGLRIEGGHIRLPEGPGLGIVPDE 357
Cdd:cd03321 293 -SHLFQEISAHLLavtptahwlEYVDWAGAIL------EPPLKFEDGNAVIPDEPGNGIIWRE 348
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
12-273 |
1.59e-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: 72.68 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 12 PLPVRDGPYRmastevwSLDTTLVKLVTDSGLIGWGETCPvgpvyqpqhaagaraalaemapgligadplqpLRLQrrmd 91
Cdd:cd03320 13 PLGTSRGRLT-------RRRGLLLRLEDLTGPVGWGEIAP--------------------------------LPLA---- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 92 gllnghryakAAIDIAAHDLMGKAWGvrvadllGGAVTERVPSYYASGVGEPDEIARIAAeRADEGYPRMQVKIGGRPVE 171
Cdd:cd03320 50 ----------FGIESALANLEALLVG-------FTRPRNRIPVNALLPAGDAAALGEAKA-AYGGGYRTVKLKVGATSFE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 172 IDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEIPF-ILEQPCnSIEEIAAIRGQLH-HAVYLDETAEDVAT 249
Cdd:cd03320 112 EDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIeYIEQPL-PPDDLAELRRLAAgVPIALDESLRRLDD 190
|
250 260
....*....|....*....|....
gi 499650543 250 VLRAVGQGVCDGFGMKVTRIGGLR 273
Cdd:cd03320 191 PLALAAAGALGALVLKPALLGGPR 214
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
14-125 |
2.44e-13 |
|
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: 65.96 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 14 PVRDGPYRMASTEVWSLDTTLVKLVTDSGLIGWGETCPVGPVyqpqHAAGARAALAEMAPGLIGADPLQPLRLQRRMDGL 93
Cdd:pfam02746 10 GWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGGR----AETIKAILDDHLAPLLIGRDAANISDLWQLMYRA 85
|
90 100 110
....*....|....*....|....*....|..
gi 499650543 94 LNGHRYAKAAIDIAAHDLMGKAWGVRVADLLG 125
Cdd:pfam02746 86 ALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
70-354 |
2.85e-12 |
|
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: 67.05 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 70 EMAPGLIGADPLQP----LRLQRRMDGLLNGHRYAKA--AIDIAAHDLMGKAWGVRVADLLgGAVTERVPSYYASG-VGE 142
Cdd:cd03328 59 LLAPVVEGRDALDPpaawEAMQRAVRNAGRPGVAAMAisAVDIALWDLKARLLGLPLARLL-GRAHDSVPVYGSGGfTSY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 143 PDEIARIAAER-ADEGYPRMQVKIGGRPVEiDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEIPFI-LEQP 220
Cdd:cd03328 138 DDDRLREQLSGwVAQGIPRVKMKIGRDPRR-DPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTwFEEP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 221 CNS--IEEIAAIR--GQLHHAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRPMAVFRDICEVRSMP---HTcdd 293
Cdd:cd03328 217 VSSddLAGLRLVRerGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDlsaHC--- 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499650543 294 awggdiiAAACTHIGATVQPRLMEGVW------LAQPYIEGHFDPENG-LRIEgghirlPEGPGLGIV 354
Cdd:cd03328 294 -------APALHAHVACAVPRLRHLEWfhdhvrIERMLFDGAPDPSGGaLRPD------LSRPGLGLE 348
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-352 |
9.64e-11 |
|
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: 62.41 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 2 KITELHLYAHPLpvrDGPYRMASTEVWSLDTTLVKLVTD-----SGLIGWGETcPVGPVYQPqhaagaRAALAEMAPGLI 76
Cdd:cd03326 1 RIVAIREKAIPL---SSPIANAYVDFSGLTTSLVAVVTDvvrdgRPVVGYGFD-SIGRYAQG------GLLRERFIPRLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 77 GADP----------LQPLRLQRRM--DGLLNGH---RYAKAAIDIAAHDLMGKAWGV----RVADLLG-GAVTERVPSYY 136
Cdd:cd03326 71 AAAPdsllddaggnLDPARAWAAMmrNEKPGGHgerAVAVGALDMAVWDAVAKIAGLplyrLLARRYGrGQADPRVPVYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 137 ASGVGEP-DEIARIAAE---RADEGYPRMQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPE 212
Cdd:cd03326 151 AGGYYYPgDDLGRLRDEmrrYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 213 IP-FILEQPCNSIEEIAairgqlhHAVYLDETAEDVATvlravGQGVcdgFGMK----VTRIGGLRPMavfRDICE---- 283
Cdd:cd03326 231 YGlRWYEEPGDPLDYAL-------QAELADHYDGPIAT-----GENL---FSLQdarnLLRYGGMRPD---RDVLQfdpg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 284 --------VRSMPHTCDDAW--------GGDI----IAAACTHIGATVQPRLMegvwlaQPYieGHFdpENGLRIEGGHI 343
Cdd:cd03326 293 lsyglpeyLRMLDVLEAHGWsrrrffphGGHLmslhIAAGLGLGGNESYPDVF------QPF--GGF--ADGCKVENGYV 362
|
....*....
gi 499650543 344 RLPEGPGLG 352
Cdd:cd03326 363 RLPDAPGIG 371
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
141-283 |
8.17e-10 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 59.44 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 141 GEPDEIARIAAEraDEGYPRMQVKIGGRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECP-----EIPF 215
Cdd:TIGR01927 110 GDPALLLLRSAK--AEGFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDpnlrgRIAF 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499650543 216 IlEQPCNSIEEIAAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDGFGMKVTRIGGLRpmaVFRDICE 283
Cdd:TIGR01927 188 L-EEPLPDADEMSAFSEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPA---KLRDLAQ 251
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
143-276 |
1.74e-07 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 52.28 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 143 PDEIARIAAerADEGYPRMQVKIG--GRPVEIDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPEIPFI--LE 218
Cdd:PRK02901 90 AAQVPEVLA--RFPGCRTAKVKVAepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeyVE 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499650543 219 QPCNSIEEIAAIRGQLHHAVYLDET---AEDVATVLRAvgqGVCDGFGMKVTRIGGLRPMA 276
Cdd:PRK02901 168 QPCATVEELAELRRRVGVPIAADESirrAEDPLRVARA---GAADVAVLKVAPLGGVRAAL 225
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
33-359 |
5.01e-06 |
|
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: 47.82 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 33 TLVKLVTDSGLIGWGETcpvgpVYQPQHAAGARAALAEMAPGLIGADPLQPLRL-QRRMDGLL--NG--HRYAKAAIDIA 107
Cdd:cd03322 17 VTLKITTDQGVTGLGDA-----TLNGRELAVKAYLREHLKPLLIGRDANRIEDIwQYLYRGAYwrRGpvTMNAIAAVDMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 108 AHDLMGKAWGVRVADLLGGAVTERVPSY-YASGvGEPDEIARIAAERADEGYPRMQVKIggrpveidIETIRKVWERVGT 186
Cdd:cd03322 92 LWDIKGKAAGMPLYQLLGGKSRDGIMVYsHASG-RDIPELLEAVERHLAQGYRAIRVQL--------PKLFEAVREKFGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 187 RMRLAVDGNRGLTTRDALRLSREC-PEIPFILEQ--PCNSIEEIAAIRGQLHHAVYLDETAEDVATVLRAVGQGVCDGFG 263
Cdd:cd03322 163 EFHLLHDVHHRLTPNQAARFGKDVePYRLFWMEDptPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 264 MKVTRIGGLRPMAVFRDICE---VRSMPHTCDDAwgGDIIAAACTHIGATVqPRLmeGVwlaQPYIeGHfdPEN------ 334
Cdd:cd03322 243 TTVSHAGGITPARKIADLASlygVRTGWHGPTDL--SPVGMAAALHLDLWV-PNF--GI---QEYM-RH--AEEtlevfp 311
|
330 340
....*....|....*....|....*.
gi 499650543 335 -GLRIEGGHIRLPEGPGLGIVPDESL 359
Cdd:cd03322 312 hSVRFEDGYLHPGEEPGLGVEIDEKA 337
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
141-247 |
6.43e-06 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 48.31 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 141 GEPDEIARIAAERADEGYPRMQVKIGGR--PVEiDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLS---RECpEIPF 215
Cdd:PLN02980 1089 GSPLEVAYVARKLVEEGFSAIKLKVGRRvsPIQ-DAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGslvKSC-NLKY 1166
|
90 100 110
....*....|....*....|....*....|..
gi 499650543 216 IlEQPCNSIEEIAAIRGQLHHAVYLDETAEDV 247
Cdd:PLN02980 1167 I-EEPVQDEDDLIKFCEETGLPVALDETIDKF 1197
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
35-359 |
9.18e-06 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 47.21 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 35 VKLVTDSGLIGWGETCPVG---PV--YQPQHaagaraalaeMAPGLIGADPlqplrlqRRMDG----LLNGHRY------ 99
Cdd:PRK15072 20 LKITTDDGVTGLGDATLNGrelAVasYLQDH----------VCPLLIGRDA-------HRIEDiwqyLYRGAYWrrgpvt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 100 --AKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVPSY-YASGVGEPDEIARIaAERADEGYP--RMQVKI--------- 165
Cdd:PRK15072 83 msAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYgHANGRDIDELLDDV-ARHLELGYKaiRVQCGVpglkttygv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 166 -------------GGRPVEIDIET----------IRKVWERVGTRMRLAVDGNRGLTTRDALRLSREC-PEIPFILEQpC 221
Cdd:PRK15072 162 skgkglayepatkGLLPEEELWSTekylrfvpklFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLePYRLFWLED-P 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 222 NSIEEIAAIRGQLHHAVyldeTAEDVATVLRAV-------GQGVCDGFGMKVTRIGG---LRPMAVFRDICEVRSMPHTC 291
Cdd:PRK15072 241 TPAENQEAFRLIRQHTT----TPLAVGEVFNSIwdckqliEEQLIDYIRTTVTHAGGithLRRIADFAALYQVRTGSHGP 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499650543 292 DDAwgGDIIAAACTHIGATVqPRLmeGVwlaQPYIeGHFDPEN-----GLRIEGGHIRLPEGPGLGIVPDESL 359
Cdd:PRK15072 317 TDL--SPVCMAAALHFDLWV-PNF--GI---QEYM-GHSEETLevfphSYTFEDGYLHPGDAPGLGVDFDEKL 380
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
100-212 |
5.54e-03 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 38.56 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 100 AKAAIDIAAHDLMGKAWGVRVADLLGGAVTERVpSYYASGvGEPDeiarIAAERadeGYprmqvkIGGR------PVE-- 171
Cdd:PRK15440 124 TISCVDLALWDLLGKVRGLPVYKLLGGAVRDEL-QFYATG-ARPD----LAKEM---GF------IGGKmplhhgPADgd 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499650543 172 ----IDIETIRKVWERVGTRMRLAVDGNRGLTTRDALRLSRECPE 212
Cdd:PRK15440 189 aglrKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAP 233
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
103-231 |
7.53e-03 |
|
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: 38.09 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499650543 103 AIDIAAHDLMGKAwgVRVADLLGgavtERVPSYYASG--VGEPDE-IARIAAERADEGYPRMQVKIGGRPvEIDIETIRK 179
Cdd:cd03324 160 ALEILRRGQPGKA--AREADLLA----EGYPAYTTSAgwLGYSDEkLRRLCKEALAQGFTHFKLKVGADL-EDDIRRCRL 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499650543 180 VWERVGTRMRLAVDGNRGLTTRDALRLSRECPEI-PFILEQPCN--SIEEIAAIR 231
Cdd:cd03324 233 AREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFkPWWIEEPTSpdDILGHAAIR 287
|
|
| |
