|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-362 |
1.30e-90 |
|
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: 275.93 E-value: 1.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 1 MRIAEIHVYRHDLPvLDGPYELALAEVRSVSTTLVELVADTGHVGWGETCPVGptyaeSHAAGAVAALSE-MAPGLRGAE 79
Cdd:COG4948 1 MKITDIEVYPVRLP-LKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGG-----TGAEAVAAALEEaLAPLLIGRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 80 VLPI-PLHRRMDGLLNGHNYAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYP 158
Cdd:COG4948 75 PLDIeALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 159 RLQVKVGGRPVEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDI-PFIMEQPCNT--IEDLQKIRSQVS 235
Cdd:COG4948 155 ALKLKVGGPDPEEDVERVRAVREAV-GPDARLRVDANGAWTLEEAIRLLRALEDLgLEWIEQPLPAedLEGLAELRRATP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 236 HGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCDDSWGGDIIAAACTHIGATVApel 315
Cdd:COG4948 234 VPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALP--- 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 502713827 316 legvwlAAPYIEGHYDP-------VNGIRAEGGYIERPQGPGLGVTPDAGLFGA 362
Cdd:COG4948 311 ------NFDIVELDGPLlladdlvEDPLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-311 |
2.81e-48 |
|
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: 162.88 E-value: 2.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 6 IHVYRHDLPVLDGPYeLALAEVRSVSTTLVELVADTGHVGWGETcpvgptyaeshaagavaalsemapglrgaevlpipl 85
Cdd:cd00308 1 VEVYAVRLPTSRPFY-LAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 86 hrrmdgllnghnyaKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYStgvgppdetarlaaekraegyprlqvkvg 165
Cdd:cd00308 44 --------------ISGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS----------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 166 grpveedIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPD-IPFIMEQPCNT--IEDLQKIRSQVSHGIYMDE 242
Cdd:cd00308 81 -------IERVRAVREAF-GPDARLAVDANGAWTPKEAIRLIRALEKyGLAWIEEPCAPddLEGYAALRRRTGIPIAADE 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502713827 243 NSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCDDSWGGDIIAAACTHIGATV 311
Cdd:cd00308 153 SVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAAL 221
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-354 |
3.96e-48 |
|
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: 166.25 E-value: 3.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 2 RIAEIHVYrhdlpVLDGPYELALAEVRSVSTTLVELVADTGHVGWGETcpvGPTYAESHAAGAVAAlsEMAPGLRGAEVL 81
Cdd:cd03316 1 KITDVETF-----VLRVPLPEPGGAVTWRNLVLVRVTTDDGITGWGEA---YPGGRPSAVAAAIED--LLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 82 PI---------PLHRRMDGLLNGHnyAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTG--VGPPDETARLAA 150
Cdd:cd03316 71 DIerlweklyrRLFWRGRGGVAMA--AISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGgyDDSPEELAEEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 151 EKRAEGYPRLQVKVGGRP-----VEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDI-PFIMEQPC--N 222
Cdd:cd03316 149 RAVAEGFTAVKLKVGGPDsggedLREDLARVRAVREAV-GPDVDLMVDANGRWDLAEAIRLARALEEYdLFWFEEPVppD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 223 TIEDLQKIRSQVSHGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNL---PHtcddSWGGDI 299
Cdd:cd03316 228 DLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVrvaPH----GAGGPI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 502713827 300 IAAACTHIGATVA-PELLEGVWLAAPYIEGHYDpvNGIRAEGGYIERPQGPGLGVT 354
Cdd:cd03316 304 GLAASLHLAAALPnFGILEYHLDDLPLREDLFK--NPPEIEDGYVTVPDRPGLGVE 357
|
|
| 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 |
1.77e-47 |
|
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: 163.51 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 5 EIHVYRHDLPvLDGPYELALAEVRSVSTTLVELVADtGHVGWGETCPVGPTYAEShAAGAVAALSEMAPGLRGAEVLPIP 84
Cdd:cd03319 1 KISLRPERLP-LKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGET-VESVLAALKSVRPALIGGDPRLEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 85 LHRRMDGLLNGHNYAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYPRLQVKV 164
Cdd:cd03319 78 LLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 165 GGrPVEEDIETIRKVWEAIRGSgmRLAVDGNRSLTTRDALRLSRECPD--IPFImEQPCNT--IEDLQKIRSQVSHGIYM 240
Cdd:cd03319 158 GG-DLEDDIERIRAIREAAPDA--RLRVDANQGWTPEEAVELLRELAElgVELI-EQPVPAgdDDGLAYLRDKSPLPIMA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502713827 241 DENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLP 288
Cdd:cd03319 234 DESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLK 281
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
144-356 |
5.60e-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: 143.47 E-value: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 144 ETARLAAEKRAE-GYPRLQVKVGGRPVEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDI-PFIMEQPC 221
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAV-GPGVDLMVDANGAWSVAEAIRLARALEELgLLWIEEPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 222 --NTIEDLQKIRSQVSHGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCdDSWGGDI 299
Cdd:pfam13378 80 ppDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAP-HSGGGPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502713827 300 IAAACTHIGATVaPELLEGVWLAAPYIEGHYDPVNGIRAEGGYIERPQGPGLGVTPD 356
Cdd:pfam13378 159 GLAASLHLAAAV-PNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELD 214
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-356 |
1.02e-40 |
|
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: 147.08 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 2 RIAEIHVyrhDLPVLDgPYELALAEVRSVSTTLVELVADTGHVGWGETCPV-GPTYAESHAAGAVAALSE-MAPGLRGAE 79
Cdd:cd03318 4 AIETTIV---DLPTRR-PHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPgGPAWGGESPETIKAIIDRyLAPLLIGRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 80 VLPI-PLHRRMDGLLNGHNYAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEG-Y 157
Cdd:cd03318 80 ATNIgAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 158 PRLQVKVGGRPVEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDI-PFIMEQPC--NTIEDLQKIRSQV 234
Cdd:cd03318 160 RRFKLKMGARPPADDLAHVEAIAKAL-GDRASVRVDVNQAWDESTAIRALPRLEAAgVELIEQPVprENLDGLARLRSRN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 235 SHGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCDDSWGGDIIAAACTHIGATVaPE 314
Cdd:cd03318 239 RVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATL-PS 317
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502713827 315 LLEGVWLAAPYIEGHyDPVN-GIRAEGGYIERPQGPGLGVTPD 356
Cdd:cd03318 318 LPFGCELFGPLLLAE-DLLEePLAYRDGELHVPTGPGLGVRLD 359
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-356 |
1.06e-33 |
|
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: 127.74 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 6 IHVYRHDLPvLDGPYELALAEVRSVSTTLVELVADTGHVGWGE-TCPVGPTYAESHAAGAVAALSE-MAPGLRGAEVL-P 82
Cdd:cd03317 1 IELFHVRMP-LKFPFETSFGTLNEREFLIVELTDEEGITGYGEvVAFEGPFYTEETNATAWHILKDyLLPLLLGREFShP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 83 IPLHRRMDGLLnGHNYAKAAVDIAAHDLLGKHLGVSVSDLLGGaVTDRVPSYYSTGVGP-PDETARLAAEKRAEGYPRLQ 161
Cdd:cd03317 80 EEVSERLAPIK-GNNMAKAGLEMAVWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGIQDdVEQLLKQIERYLEEGYKRIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 162 VKVggRPvEEDIETIRKVWEAIrgSGMRLAVDGNRSLTTRDALRLsRECPDIPFIM-EQPC--NTIEDLQKIRSQVSHGI 238
Cdd:cd03317 158 LKI--KP-GWDVEPLKAVRERF--PDIPLMADANSAYTLADIPLL-KRLDEYGLLMiEQPLaaDDLIDHAELQKLLKTPI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 239 YMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPhtcddSWGGDIIAAActhIG--ATVAPELL 316
Cdd:cd03317 232 CLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIP-----VWCGGMLESG---IGraHNVALASL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 502713827 317 EGVWLAAP-------YIEghyDPV-NGIRAEGGYIERPQGPGLGVTPD 356
Cdd:cd03317 304 PNFTYPGDisassryFEE---DIItPPFELENGIISVPTGPGIGVTVD 348
|
|
| mucon_cyclo |
TIGR02534 |
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase ... |
12-356 |
3.81e-33 |
|
muconate and chloromuconate cycloisomerases; This model encompasses muconate cycloisomerase (EC 5.5.1.1) and chloromuconate cycloisomerase (EC 5.5.1.7), enzymes that often overlap in specificity. It excludes more distantly related proteins such as mandelate racemase (5.1.2.2).
Pssm-ID: 162905 [Multi-domain] Cd Length: 368 Bit Score: 126.83 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 12 DLPVLDgPYELALAEVRSVSTTLVELVADTGHVGWGE-TCPVGPTYAESHAAGAVAALSE-MAPGLRGAEV-LPIPLHRR 88
Cdd:TIGR02534 10 DVPTIR-PHKLATTTMTEQTLVLVRIRTEDGVIGYGEgTTIGGLWWGGESPETIKANIDTyLAPVLVGRDAtEIAAIMAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 89 MDGLLNGHNYAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAE-GYPRLQVKVGGR 167
Cdd:TIGR02534 89 LEKVVAGNRFAKAAVDTALHDAQARRLGVPVSELLGGRVRDSVDVTWTLASGDTDRDIAEAEERIEEkRHRSFKLKIGAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 168 PVEEDIETIRKVWEAIRGSGmRLAVDGNRSLTTRDALRLSRECPDIPF-IMEQPC--NTIEDLQKIRSQVSHGIYMDENS 244
Cdd:TIGR02534 169 DPADDVAHVVAIAKALGDRA-SVRVDVNAAWDERTALHYLPQLADAGVeLIEQPTpaENREALARLTRRFNVPIMADESV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 245 TSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCDDSWGGDIIAAACTHIGATVaPELLEGVWLAAP 324
Cdd:TIGR02534 248 TGPADALAIAKASAADVFALKTTKSGGLLESKKIAAIAEAAGIALYGGTMLEGPIGTIASAHFFATF-PALSFGTELFGP 326
|
330 340 350
....*....|....*....|....*....|..
gi 502713827 325 YIEGHYDPVNGIRAEGGYIERPQGPGLGVTPD 356
Cdd:TIGR02534 327 LLLKDEILTEPLQYEDFQLHLPQGPGLGVEVD 358
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
6-310 |
3.62e-31 |
|
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: 118.98 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 6 IHVYRHDLPvLDGPYELALAEVRSVSTTLVELVADTGHVGWGETcpvgptyaeshaagavaalsemapglrgaevlpipl 85
Cdd:cd03315 1 VEAIPVRLP-LKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEA------------------------------------ 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 86 hrrmdgllnghnyAKAAVDIAAHDLLGKHLGVSVSDLLGGaVTDRVPSYYSTGVGPPDETARLAAEKRAEGYPRLQVKVG 165
Cdd:cd03315 44 -------------TKAAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 166 GRPvEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPD--IPFImEQPCNT--IEDLQKIRSQVSHGIYMD 241
Cdd:cd03315 110 RDP-ARDVAVVAALREAV-GDDAELRVDANRGWTPKQAIRALRALEDlgLDYV-EQPLPAddLEGRAALARATDTPIMAD 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502713827 242 ENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLPHTCDDSWGGDIIAAACTHIGAT 310
Cdd:cd03315 187 ESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAA 255
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
34-356 |
3.68e-26 |
|
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: 107.03 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 34 LVELVADTGHVGWGEtcpvgPTyAESHAAGAVAALSEMAPGLRGAEVLPIPLHRRM---DGLLNG---HNYAKAAVDIAA 107
Cdd:cd03325 16 FVKIETDEGVVGWGE-----PT-VEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVmyrGGFYRGgpvLMSAISGIDQAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 108 HDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYPrlQVKVGGRPVEEDIETIRKVWEAIR--- 184
Cdd:cd03325 90 WDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFT--AVKMNATEELQWIDTSKKVDAAVErva 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 185 ------GSGMRLAVDGNRSLTTRDALRLSREC-PDIPFIMEQPC--NTIEDLQKIRSQVSHGIYMDENSTSLNTAITAAG 255
Cdd:cd03325 168 alreavGPDIDIGVDFHGRVSKPMAKDLAKELePYRLLFIEEPVlpENVEALAEIAARTTIPIATGERLFSRWDFKELLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 256 TGLVDGFGMKVTRIGGLHPMR-------AFrDVCAArnlPHTCDdswgGDIIAAACTHIGAT----VAPELLEGV--WLA 322
Cdd:cd03325 248 DGAVDIIQPDISHAGGITELKkiaamaeAY-DVALA---PHCPL----GPIALAASLHVDAStpnfLIQEQSLGIhyNEG 319
|
330 340 350
....*....|....*....|....*....|....
gi 502713827 323 APYIEGHYDPVnGIRAEGGYIERPQGPGLGVTPD 356
Cdd:cd03325 320 DDLLDYLVDPE-VFDMENGYVKLPTGPGLGIEID 352
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
33-356 |
2.44e-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: 85.45 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 33 TLVELVADTGHVGWGEtCPVGptyaeshaAGAVAALSEMAPGLRGAEVLPIPLHRRMDGLLNGHN--------------- 97
Cdd:cd03323 31 NIVELTDDNGNTGVGE-SPGG--------AEALEALLEAARSLVGGDVFGAYLAVLESVRVAFADrdaggrglqtfdlrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 98 --YAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVP-SYYSTGVGP--------------------PDETARLA-AEKR 153
Cdd:cd03323 102 tvHVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVPfLAYLFYKGDrhktdlpypwfrdrwgealtPEGVVRLArAAID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 154 AEGYPRLQVKVGGRPVEEDIETIRKVWEAIRGSgmRLAVDGNRSLTTRDALRLSRECPDIPFIMEQPCNTIEDLQKIRSq 233
Cdd:cd03323 182 RYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGA--RLRLDPNGAWSLETAIRLAKELEGVLAYLEDPCGGREGMAEFRR- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 234 vshgiymdenSTSLNTAITAAGTG---LVDGFGMKVTRI--------GGLHPMRAFRDVCaarnlpHTCDDSWGG----- 297
Cdd:cd03323 259 ----------ATGLPLATNMIVTDfrqLGHAIQLNAVDIpladhhfwGGMRGSVRVAQVC------ETWGLGWGMhsnnh 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502713827 298 -DIIAAACTHIGAtVAPELLEGVwlAAPYIEGHYDPVNG--IRAEGGYIERPQGPGLGVTPD 356
Cdd:cd03323 323 lGISLAMMTHVAA-AAPGLITAC--DTHWIWQDGQVITGepLRIKDGKVAVPDKPGLGVELD 381
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
34-356 |
7.70e-18 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 83.79 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 34 LVELVADTGHVGWGEtcPVgptyAESHAAGAVAALSEMAPGLRGAEVLPIPLH-RRM--DGLLNG---HNYAKAAVDIAA 107
Cdd:PRK14017 17 FLKIETDEGIVGWGE--PV----VEGRARTVEAAVHELADYLIGKDPRRIEDHwQVMyrGGFYRGgpiLMSAIAGIDQAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 108 HDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYPrlQVKVGG----------RPVEEDIETIR 177
Cdd:PRK14017 91 WDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFT--AVKMNGteelqyidspRKVDAAVARVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 178 KVWEAIrGSGMRLAVDGNRSLTTRDALRLSREC-PDIPFIMEQPC--NTIEDLQKIRSQVSHGIYMDENSTSLNTAITAA 254
Cdd:PRK14017 169 AVREAV-GPEIGIGVDFHGRVHKPMAKVLAKELePYRPMFIEEPVlpENAEALPEIAAQTSIPIATGERLFSRWDFKRVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 255 GTGLVDGFGMKVTRIGGLHPMR-------AFrDVCAArnlPHtCDdswGGDIIAAACTHIGATVAPELLE----GVwlaa 323
Cdd:PRK14017 248 EAGGVDIIQPDLSHAGGITECRkiaamaeAY-DVALA---PH-CP---LGPIALAACLQVDAVSPNAFIQeqslGI---- 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502713827 324 pyiegHYDPVNGI----------RAEGGYIERPQGPGLGVTPD 356
Cdd:PRK14017 316 -----HYNQGADLldyvknkevfAYEDGFVAIPTGPGLGIEID 353
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
5-288 |
7.06e-17 |
|
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: 80.92 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 5 EIHVYR--HDLPVLDGPYELAlaevrsvSTTLVELVADTGhvgwGETcpvGPTYAESHAAGAVAALSEMAPGLRGAEVLP 82
Cdd:cd03328 6 EARAYTvpTDAPEADGTLAWD-------ATTLVLVEVRAG----GRT---GLGYTYADAAAAALVDGLLAPVVEGRDALD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 83 IP-----LHRRMDGLLNGHNYAKA--AVDIAAHDLLGKHLGVSVSDLLgGAVTDRVPSYYSTGVG--PPDETARLAAEKR 153
Cdd:cd03328 72 PPaaweaMQRAVRNAGRPGVAAMAisAVDIALWDLKARLLGLPLARLL-GRAHDSVPVYGSGGFTsyDDDRLREQLSGWV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 154 AEGYPRLQVKVGGRPvEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDIPFI-MEQPCNT--IEDLQKI 230
Cdd:cd03328 151 AQGIPRVKMKIGRDP-RRDPDRVAAARRAI-GPDAELFVDANGAYSRKQALALARAFADEGVTwFEEPVSSddLAGLRLV 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 231 RSQVSHG--IYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLP 288
Cdd:cd03328 229 RERGPAGmdIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVD 288
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
34-272 |
3.62e-15 |
|
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: 75.60 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 34 LVELVADTGHVGWGETCpvgpTYAESHAAGAVAALSEMAPGLRGAEVLPIPLHRRMD------GLLNGHNYAKAAVDIAA 107
Cdd:cd03321 33 LIDLATDEGVTGHSYLF----TYTPAALKSLKQLLDDMAALLVGEPLAPAELERALAkrfrllGYTGLVRMAAAGIDMAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 108 HDLLGKHLGVSVSDLLGGAVTDrVPSYYSTGVGPPDETARLAAEKRAEGYPRLQVKVGGRPVEEDIETIRKVWEAIrGSG 187
Cdd:cd03321 109 WDALAKVHGLPLAKLLGGNPRP-VQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAV-GDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 188 MRLAVDGNRSLTTRDALRLSRECPD--IPFImEQPC--NTIEDLQKIRSQVSHGIYMDENSTSLNTAITAAGTGLVDGFG 263
Cdd:cd03321 187 VGLMVDYNQSLTVPEAIERGQALDQegLTWI-EEPTlqHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVM 265
|
....*....
gi 502713827 264 MKVTRIGGL 272
Cdd:cd03321 266 PDLMKIGGV 274
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
26-354 |
1.27e-14 |
|
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: 73.91 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 26 EVRS-VSTTLVELVADTGHVGWGETcpvgptyaeshAAGAVAA---LSEMAPGLRGAEVLPIP-LHRRM--DGLLNGHN- 97
Cdd:cd03327 4 SVRTrVGWLFVEIETDDGTVGYANT-----------TGGPVACwivDQHLARFLIGKDPSDIEkLWDQMyrATLAYGRKg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 98 ---YAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYS-TGVGPPDETARLAAEKRAEGYPRLQVKVGGRP----- 168
Cdd:cd03327 73 iamAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASgLYPTDLDELPDEAKEYLKEGYRGMKMRFGYGPsdgha 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 169 -VEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECP--DIPFIMEQ-PCNTIEDLQKIRSQVSHGIYMDENS 244
Cdd:cd03327 153 gLRKNVELVRAIREAV-GYDVDLMLDCYMSWNLNYAIKMARALEkyELRWIEEPlIPDDIEGYAELKKATGIPISTGEHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 245 TSL---NTAITAAGtglVDGFGMKVTRIGGLHPMRAFRDVCAARN---LPHtcddswGGDIIAAACThIGATVAP--ELL 316
Cdd:cd03327 232 YTVygfKRLLEGRA---VDILQPDVNWVGGITELKKIAALAEAYGvpvVPH------ASQIYNYHFI-MSEPNSPfaEYL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 502713827 317 --EGVWLAAPYIEGHYdpVNGIRAEGGYIERPQGPGLGVT 354
Cdd:cd03327 302 pnSPDEVGNPLFYYIF--LNEPVPVNGYFDLSDKPGFGLE 339
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
101-220 |
2.33e-14 |
|
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: 73.58 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 101 AAVDIAAHDLLGKHLGVSVSDLLGGaVTDRVPSYYSTGVG-------PPDETARLAAEKRAEGYPRLQVKVGGRP-VEED 172
Cdd:cd03329 97 GLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGddlegleSPEAYADFAEECKALGYRAIKLHPWGPGvVRRD 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 502713827 173 IETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDIPFI-MEQP 220
Cdd:cd03329 176 LKACLAVREAV-GPDMRLMHDGAHWYSRADALRLGRALEELGFFwYEDP 223
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
6-288 |
2.70e-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: 71.91 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 6 IHVYRHDLPvLDGPYELALAEVRSVSTTLVELVADTGHVGWGETCPVgptyaeSHAAGAVAALSEMAPGLRGAEvlpipl 85
Cdd:cd03320 1 ARLYPYSLP-LSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGEIAPL------PLAFGIESALANLEALLVGFT------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 86 hrrmdgllnghnyakaavdiaahdllGKHLGVSVSDLLGGavtdrvpsyystgvgPPDETARLAAEKRAEGYPRLQVKVG 165
Cdd:cd03320 68 --------------------------RPRNRIPVNALLPA---------------GDAAALGEAKAAYGGGYRTVKLKVG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 166 GRPVEEDIETIRKVWEAiRGSGMRLAVDGNRSLTTRDALRLSRECP--DIPFImEQPCNTIEDLQKIRSQVSHGIYMDEN 243
Cdd:cd03320 107 ATSFEEDLARLRALREA-LPADAKLRLDANGGWSLEEALAFLEALAagRIEYI-EQPLPPDDLAELRRLAAGVPIALDES 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502713827 244 STSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCAARNLP 288
Cdd:cd03320 185 LRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIP 229
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
6-124 |
1.20e-10 |
|
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: 58.25 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 6 IHVYRHDLPVLDGPYELALAEVRSVSTTLVELVADTGHVGWGETCPVGPtyaeSHAAGAVAALSEMAPGLRGAEVLPIPL 85
Cdd:pfam02746 2 IEVFVVDVGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYGG----RAETIKAILDDHLAPLLIGRDAANISD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 502713827 86 HRR-MDGLLNGHNYAKAAVDIAAHDLLGKHLGVSVSDLLG 124
Cdd:pfam02746 78 LWQlMYRAALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
97-283 |
2.86e-09 |
|
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: 57.83 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 97 NYAKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYPRLQVKvggrpveedietI 176
Cdd:cd03322 82 MNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQ------------L 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 177 RKVWEAIR---GSGMRLAVDGNRSLTTRDALRLSRECPDI-PFIMEQ--PCNTIEDLQKIRSQVSHGIYMDENSTSLNTA 250
Cdd:cd03322 150 PKLFEAVRekfGFEFHLLHDVHHRLTPNQAARFGKDVEPYrLFWMEDptPAENQEAFRLIRQHTATPLAVGEVFNSIWDW 229
|
170 180 190
....*....|....*....|....*....|...
gi 502713827 251 ITAAGTGLVDGFGMKVTRIGGLHPMRAFRDVCA 283
Cdd:cd03322 230 QNLIQERLIDYIRTTVSHAGGITPARKIADLAS 262
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
99-361 |
6.18e-08 |
|
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: 53.94 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 99 AKAAvDIAAHDLLGKHLGVSVSDllggavtDRVPSYYSTGV-GPPDETARLAAEKR---AEGYPRLQVKVGGRPVEEDIE 174
Cdd:cd03326 122 AKIA-GLPLYRLLARRYGRGQAD-------PRVPVYAAGGYyYPGDDLGRLRDEMRrylDRGYTVVKIKIGGAPLDEDLR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 175 TIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECPDIP-FIMEQPCNTIE-DLQKIRSQVSHG-IYMDENSTSLNTAi 251
Cdd:cd03326 194 RIEAALDVL-GDGARLAVDANGRFDLETAIAYAKALAPYGlRWYEEPGDPLDyALQAELADHYDGpIATGENLFSLQDA- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 252 taagTGLVdgfgmkvtRIGGlhpMRAFRDV----CA--------ARNLPHTCDDSW--------GGDI----IAAACTHI 307
Cdd:cd03326 272 ----RNLL--------RYGG---MRPDRDVlqfdPGlsyglpeyLRMLDVLEAHGWsrrrffphGGHLmslhIAAGLGLG 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502713827 308 GATVAPELLegvwlaAPYiEGHYDpvnGIRAEGGYIERPQGPGLGVTPDAGLFG 361
Cdd:cd03326 337 GNESYPDVF------QPF-GGFAD---GCKVENGYVRLPDAPGIGFEGKAELAA 380
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
99-276 |
2.81e-06 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 48.75 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 99 AKAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVPSYYSTGVGPPDETARLAAEKRAEGYP--RLQVKV------------ 164
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKaiRVQCGVpglkttygvskg 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 165 ----------GGRPVEEDIET------IRKVWEAIR---GSGMRLAVDGNRSLTTRDALRLSREC-PDIPFIMEQPcnTI 224
Cdd:PRK15072 165 kglayepatkGLLPEEELWSTekylrfVPKLFEAVRnkfGFDLHLLHDVHHRLTPIEAARLGKSLePYRLFWLEDP--TP 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502713827 225 EDLQK----IRSQVSHGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMR 276
Cdd:PRK15072 243 AENQEafrlIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLR 298
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
126-290 |
5.24e-05 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 126 AVTDRVPSYYSTGVGPPDETARLAAekRAEGYPRLQVKVG--GRPVEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDA 203
Cdd:PRK02901 74 PVRDRVPVNATVPAVDAAQVPEVLA--RFPGCRTAKVKVAepGQTLADDVARVNAVRDAL-GPDGRVRVDANGGWSVDEA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 204 LRLSRE-CPDIPF-IMEQPCNTIEDLQKIRSQVSHGIYMDE----NSTSLNTAITAAGTGLVdgfgMKVTRIGGlhpMRA 277
Cdd:PRK02901 151 VAAARAlDADGPLeYVEQPCATVEELAELRRRVGVPIAADEsirrAEDPLRVARAGAADVAV----LKVAPLGG---VRA 223
|
170
....*....|...
gi 502713827 278 FRDVCAARNLPHT 290
Cdd:PRK02901 224 ALDIAEQIGLPVV 236
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
154-278 |
1.04e-04 |
|
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: 43.64 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 154 AEGYPRLQVKVGGRPVEEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLSRECP-----DIPFImEQPCNTIEDLQ 228
Cdd:TIGR01927 122 AEGFRTFKWKVGVGELAREGMLVNLLLEAL-PDKAELRLDANGGLSPDEAQQFLKALDpnlrgRIAFL-EEPLPDADEMS 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 502713827 229 KIRSQVSHGIYMDENSTSLNTAITAAGTGLVDGFGMKVTRIGGLHPMRAF 278
Cdd:TIGR01927 200 AFSEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDL 249
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
32-141 |
2.10e-04 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 42.79 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 32 TTLVELVADTGHVGWGETcpvgptyaeshAAGAVAAL---SEMAPGLRGAEVLPIplHRRMDGLLNGHNY---------A 99
Cdd:PRK15440 58 TLVVEVEAENGQVGFAVS-----------TAGEMGAFiveKHLNRFIEGKCVSDI--ELIWDQMLNATLYygrkglvmnT 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 502713827 100 KAAVDIAAHDLLGKHLGVSVSDLLGGAVTDRVpSYYSTGVGP 141
Cdd:PRK15440 125 ISCVDLALWDLLGKVRGLPVYKLLGGAVRDEL-QFYATGARP 165
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
140-242 |
9.26e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 41.38 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502713827 140 GPPDETARLAAEKRAEGYPRLQVKVGGR--PVeEDIETIRKVWEAIrGSGMRLAVDGNRSLTTRDALRLS---RECpDIP 214
Cdd:PLN02980 1089 GSPLEVAYVARKLVEEGFSAIKLKVGRRvsPI-QDAAVIQEVRKAV-GYQIELRADANRNWTYEEAIEFGslvKSC-NLK 1165
|
90 100
....*....|....*....|....*...
gi 502713827 215 FImEQPCNTIEDLQKIRSQVSHGIYMDE 242
Cdd:PLN02980 1166 YI-EEPVQDEDDLIKFCEETGLPVALDE 1192
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
135-195 |
1.74e-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: 40.02 E-value: 1.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502713827 135 YSTGVG----PPDETARLAAEKRAEGYPRLQVKVGGRPvEEDIETIRKVWEAIrGSGMRLAVDGN 195
Cdd:cd03324 186 YTTSAGwlgySDEKLRRLCKEALAQGFTHFKLKVGADL-EDDIRRCRLAREVI-GPDNKLMIDAN 248
|
|
| |
