|
Name |
Accession |
Description |
Interval |
E-value |
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-363 |
1.06e-140 |
|
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: 403.82 E-value: 1.06e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 1 MKIKTIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPdehiTGETPESTYAMLKNTLAPKLIGQNPM 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVP----GGTGAEAVAAALEEALAPLLIGRDPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 81 EFEKIHELMDKTVHRAPAAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPVTHVLSIDEPEKMADEAEEKLEEGYRSF 160
Cdd:COG4948 77 DIEALWQRLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 161 KMKVG-LDVSGDVKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVP 239
Cdd:COG4948 157 KLKVGgPDPEEDVERVRAVREAVGPDARLRVDANGAW-TLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRATPVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 240 QMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSKKIIKSV 319
Cdd:COG4948 236 IAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFDIV 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1546417147 320 ELTGPVKFSQDIgdLKSSYVI--PYIQINEQPGLGVSIDEVVLAEL 363
Cdd:COG4948 316 ELDGPLLLADDL--VEDPLRIedGYLTVPDGPGLGVELDEDALARY 359
|
|
| 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 ... |
5-327 |
1.02e-114 |
|
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: 336.08 E-value: 1.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 5 TIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTEcGLVGWGESVPDEHITGETPESTYAMLkNTLAPKLIGQNPMeFEK 84
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAAL-KSVRPALIGGDPR-LEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 85 IHELMDKTVHRAPAAKAALDIACFDVVGKKLGVPVYQLLGGRyHEKFPVTHV-LSIDEPEKMADEAEEKLEEGYRSFKMK 163
Cdd:cd03319 78 LLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGG-APRPLETDYtISIDTPEAMAAAAKKAAKRGFPLLKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 164 VGLDVSGDVKRIKAVRARVGEeIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMID 243
Cdd:cd03319 157 LGGDLEDDIERIRAIREAAPD-ARLRVDANQGW-TPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 244 EGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSKkiIKSVELTG 323
Cdd:cd03319 235 ESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAAK--ADFVDLDG 312
|
....
gi 1546417147 324 PVKF 327
Cdd:cd03319 313 PLLL 316
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-357 |
1.46e-87 |
|
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: 268.80 E-value: 1.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 2 KIKTIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPDEHIT--GETPESTYAMLKNTLAPKLIGQNP 79
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAwgGESPETIKAIIDRYLAPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 80 MEFEKIHELMDKTVHRAPAAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPVTHVLSIDEPEKMADEAEEKLEEG-YR 158
Cdd:cd03318 81 TNIGAAMALLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 159 SFKMKVG-LDVSGDVKRIKAVRARVGEEIAIRVDVNQGWENSaNTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTS 237
Cdd:cd03318 161 RFKLKMGaRPPADDLAHVEAIAKALGDRASVRVDVNQAWDES-TAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 238 VPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSKKIIK 317
Cdd:cd03318 240 VPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFATLPSLP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1546417147 318 -SVELTGPVKFSQDIGDLKSSYVIPYIQINEQPGLGVSIDE 357
Cdd:cd03318 320 fGCELFGPLLLAEDLLEEPLAYRDGELHVPTGPGLGVRLDE 360
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
6-313 |
2.70e-78 |
|
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: 241.48 E-value: 2.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 6 IEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGEsvpdehitgetpestyamlkntlapkligqnpmefeki 85
Cdd:cd03315 1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 86 helmdktvhrapAAKAALDIACFDVVGKKLGVPVYQLLGGrYHEKFPVTHVLSIDEPEKMADEAEEKLEEGYRSFKMKVG 165
Cdd:cd03315 43 ------------ATKAAVDMALWDLWGKRLGVPVYLLLGG-YRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 166 LDVSGDVKRIKAVRARVGEEIAIRVDVNQGWENSAnTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEG 245
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQ-AIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADES 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1546417147 246 IRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSK 313
Cdd:cd03315 189 AFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAAL 256
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-353 |
1.59e-76 |
|
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: 240.21 E-value: 1.59e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 2 KIKTIEIFSIHLPLIKPFIisyaTYPHIQSIIVKLTTECGLVGWGESVPdehitGETPESTYAMLKNTLAPKLIGQNPME 81
Cdd:cd03316 1 KITDVETFVLRVPLPEPGG----AVTWRNLVLVRVTTDDGITGWGEAYP-----GGRPSAVAAAIEDLLAPLLIGRDPLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 82 FEKIHELMDKTVHRAP------AAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPV--THVLSIDEPEKMADEAEEKL 153
Cdd:cd03316 72 IERLWEKLYRRLFWRGrggvamAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVyaSGGGYDDSPEELAEEAKRAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 154 EEGYRSFKMKVGLDVSG------DVKRIKAVRARVGEEIAIRVDVNQGWenSANT-LQALRQLESLGLDWLEQPVAQDDI 226
Cdd:cd03316 152 AEGFTAVKLKVGGPDSGgedlreDLARVRAVREAVGPDVDLMVDANGRW--DLAEaIRLARALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 227 DGMVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMvESSVGSAAG 306
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGA-GGPIGLAAS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1546417147 307 FHVAFSKKIIKSVELtgPVKFSQDIGDLKSSYVIP---YIQINEQPGLGV 353
Cdd:cd03316 309 LHLAAALPNFGILEY--HLDDLPLREDLFKNPPEIedgYVTVPDRPGLGV 356
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
144-357 |
2.24e-61 |
|
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: 196.25 E-value: 2.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 144 KMADEAEEKLEE-GYRSFKMKVG-LDVSGDVKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQPV 221
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGgPDPEEDVERVRAVREAVGPGVDLMVDANGAW-SVAEAIRLARALEELGLLWIEEPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 222 AQDDIDGMVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMvESSV 301
Cdd:pfam13378 80 PPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1546417147 302 GSAAGFHVAFSKKIIKSVELT-GPVKFSQDIGDLKSSYVIPYIQINEQPGLGVSIDE 357
Cdd:pfam13378 159 GLAASLHLAAAVPNLLIQEYFlDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-362 |
7.98e-58 |
|
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: 191.68 E-value: 7.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 6 IEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPDEH--ITGETPESTYAMLKNTLAPKLIGQNPMEFE 83
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGpfYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 84 KIHELMDKtVHRAPAAKAALDIACFDVVGKKLGVPVYQLLGGRyHEKFPVTHVLSIDE-PEKMADEAEEKLEEGYRSFKM 162
Cdd:cd03317 81 EVSERLAP-IKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVGVSIGIQDdVEQLLKQIERYLEEGYKRIKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 163 KvgLDVSGDVKRIKAVRARVGEeIAIRVDVNqgwenSANTLQ---ALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVP 239
Cdd:cd03317 159 K--IKPGWDVEPLKAVRERFPD-IPLMADAN-----SAYTLAdipLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 240 QMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSKKIIKSV 319
Cdd:cd03317 231 ICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALASLPNFTYPG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1546417147 320 ELTGPVK-FSQDIgdLKSSYVIP--YIQINEQPGLGVSIDEVVLAE 362
Cdd:cd03317 311 DISASSRyFEEDI--ITPPFELEngIISVPTGPGIGVTVDREALKK 354
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-321 |
3.93e-49 |
|
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: 165.19 E-value: 3.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 6 IEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGEsvpdehitgetpestyamlkntlapkligqnpmefeki 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGE-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 86 helmdktvhrapaAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPVthvlsidepekmadeaeekleegYRSfkmkvg 165
Cdd:cd00308 43 -------------VISGIDMALWDLAAKALGVPLAELLGGGSRDRVPA-----------------------YGS------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 166 ldvsgdVKRIKAVRARVGEEIAIRVDVNQGWensaNTLQAL---RQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMI 242
Cdd:cd00308 81 ------IERVRAVREAFGPDARLAVDANGAW----TPKEAIrliRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1546417147 243 DEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFSKKIIKSVEL 321
Cdd:cd00308 151 DESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIET 229
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
2-356 |
5.49e-49 |
|
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: 168.28 E-value: 5.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 2 KIKTIEIFsihlplikpfiisyatyphIQSIIVKLTTECGLVGWGesvpdehiTGETPESTYAMLKNTLAPKLIGQNPME 81
Cdd:cd03327 1 KIKSVRTR-------------------VGWLFVEIETDDGTVGYA--------NTTGGPVACWIVDQHLARFLIGKDPSD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 82 FEKIHELMDKTVHR------APAAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPV--THvLSIDEPEKMADEAEEKL 153
Cdd:cd03327 54 IEKLWDQMYRATLAygrkgiAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAyaSG-LYPTDLDELPDEAKEYL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 154 EEGYRSFKMKVG-------LDVSGDVKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQPVAQDDI 226
Cdd:cd03327 133 KEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDVDLMLDCYMSW-NLNYAIKMARALEKYELRWIEEPLIPDDI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 227 DGMVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIecqigsMVESSVGSAAG 306
Cdd:cd03327 212 EGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGV------PVVPHASQIYN 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 307 FHVA-------FSKKIIKSVELTGPVKFsqdiGDLKSSYVIP---YIQINEQPGLGVSID 356
Cdd:cd03327 286 YHFImsepnspFAEYLPNSPDEVGNPLF----YYIFLNEPVPvngYFDLSDKPGFGLELN 341
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
34-356 |
2.71e-37 |
|
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: 137.46 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 34 VKLTTECGLVGWGESVpdehITGETpESTYAMLKNtLAPKLIGQNPMEFEKIHELMdktvHRAP---------AAKAALD 104
Cdd:cd03325 17 VKIETDEGVVGWGEPT----VEGKA-RTVEAAVQE-LEDYLIGKDPMNIEHHWQVM----YRGGfyrggpvlmSAISGID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 105 IACFDVVGKKLGVPVYQLLGGRYHEKFPVTHVLSIDEPEKMADEAEEKLEEGYRSFKMkVGLD----------VSGDVKR 174
Cdd:cd03325 87 QALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKM-NATEelqwidtskkVDAAVER 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 175 IKAVRARVGEEIAIRVDVNqGWENSANTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEGIRDMVDLRQ 254
Cdd:cd03325 166 VAALREAVGPDIDIGVDFH-GRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 255 IIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIecqigSMV----ESSVGSAAGFHVAFSKKIIKSVELTGPVKFSQD 330
Cdd:cd03325 245 LLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV-----ALAphcpLGPIALAASLHVDASTPNFLIQEQSLGIHYNEG 319
|
330 340 350
....*....|....*....|....*....|...
gi 1546417147 331 IGDLKS-------SYVIPYIQINEQPGLGVSID 356
Cdd:cd03325 320 DDLLDYlvdpevfDMENGYVKLPTGPGLGIEID 352
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
13-310 |
1.74e-36 |
|
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: 133.15 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 13 LPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGEsvpdehitgetpestyamlkntLAPKLIGqnpMEFEkihelmdkt 92
Cdd:cd03320 8 LPLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGE----------------------IAPLPLA---FGIE--------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 93 vhrapAAKAALDIACFDVVGKKLGVPVYQLLGGryhekfpvthvlsidEPEKMADEAEEKLEEGYRSFKMKVGL-DVSGD 171
Cdd:cd03320 54 -----SALANLEALLVGFTRPRNRIPVNALLPA---------------GDAAALGEAKAAYGGGYRTVKLKVGAtSFEED 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 172 VKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQPVAQDDIDGMVEikSKTSVPQMIDEGIRDMVD 251
Cdd:cd03320 114 LARLRALREALPADAKLRLDANGGW-SLEEALAFLEALAAGRIEYIEQPLPPDDLAELRR--LAAGVPIALDESLRRLDD 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1546417147 252 LRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVA 310
Cdd:cd03320 191 PLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLA 249
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
51-356 |
1.12e-35 |
|
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: 133.68 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 51 DEHITGET----PESTYAMLKNTLAPKLIGQNPMEFEKIHELMDKTVHRAP-AAKAALDIACFDVVGKKLGVPVYQLLGG 125
Cdd:cd03329 42 DEGAKGHAfggrPVTDPALVDRFLKKVLIGQDPLDRERLWQDLWRLQRGLTdRGLGLVDIALWDLAGKYLGLPVHRLLGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 126 rYHEKFPV---THVLS----IDEPEKMADEAEEKLEEGYRSFKMK--VGLDVSGDVKRIKAVRARVGEEIAIRVDvNQGW 196
Cdd:cd03329 122 -YREKIPAyasTMVGDdlegLESPEAYADFAEECKALGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHD-GAHW 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 197 ENSANTLQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEGIRDMVDLR-QIIAKRAADKINIKLMKCGGIY 275
Cdd:cd03329 200 YSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGALESRaDWVLAGATDFLRADVNLVGGIT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 276 PAMKLANMAEMAGIECQIGSmvessvGSAAGFHV--AFSKKIIKSVELTGPVKFSQDIGDLKSSYVIP-----YIQINEQ 348
Cdd:cd03329 280 GAMKTAHLAEAFGLDVELHG------NGAANLHViaAIRNTRYYERGLLHPSQKYDVYAGYLSVLDDPvdsdgFVHVPKG 353
|
....*...
gi 1546417147 349 PGLGVSID 356
Cdd:cd03329 354 PGLGVEID 361
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-366 |
1.59e-33 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 128.09 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 1 MKIKTIEIFsihlpLIKPfiisyatyphiQSIIVKLTTECGLVGWGESVpdehITGETpESTYAMLkNTLAPKLIGQNPM 80
Cdd:PRK14017 1 MKITKLETF-----RVPP-----------RWLFLKIETDEGIVGWGEPV----VEGRA-RTVEAAV-HELADYLIGKDPR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 81 EFEKIHELMdktvHRA------P---AAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPVTHVLSIDEPEKMADEAEE 151
Cdd:PRK14017 59 RIEDHWQVM----YRGgfyrggPilmSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 152 KLEEGYRSFKMKVG-----LD----VSGDVKRIKAVRARVGEEIAIRVDVNqGWENSANTLQALRQLESLGLDWLEQPVA 222
Cdd:PRK14017 135 RVERGFTAVKMNGTeelqyIDsprkVDAAVARVAAVREAVGPEIGIGVDFH-GRVHKPMAKVLAKELEPYRPMFIEEPVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 223 QDDIDGMVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGI----ECQIGsmve 298
Cdd:PRK14017 214 PENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDValapHCPLG---- 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1546417147 299 sSVGSAAGFHVAFSKK--IIKSVEL-------TGPVKFSQDIGDLksSYVIPYIQINEQPGLGVSIDEVVLAELTQN 366
Cdd:PRK14017 290 -PIALAACLQVDAVSPnaFIQEQSLgihynqgADLLDYVKNKEVF--AYEDGFVAIPTGPGLGIEIDEAKVRERAKT 363
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-357 |
2.98e-31 |
|
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: 121.39 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 2 KIKTIEIFsihlplikpfiisyATYPHIQSIIVKLTTECGLVGWGesvpDEHITGEtPESTYAMLKNTLAPKLIGQNPME 81
Cdd:cd03322 1 KITAIEVI--------------VTCPGRNFVTLKITTDQGVTGLG----DATLNGR-ELAVKAYLREHLKPLLIGRDANR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 82 FEKIHELMDKTVH--RAP---AAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPV-THVLSIDEPEkMADEAEEKLEE 155
Cdd:cd03322 62 IEDIWQYLYRGAYwrRGPvtmNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVySHASGRDIPE-LLEAVERHLAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 156 GYRSFKMKVgldvsgdVKRIKAVRARVGEEIAIRVDVNQGWE-NSAntLQALRQLESLGLDWLEQPVAQDDIDGMVEIKS 234
Cdd:cd03322 141 GYRAIRVQL-------PKLFEAVREKFGFEFHLLHDVHHRLTpNQA--ARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 235 KTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQI-GSMVESSVGSAAGFHVAFS- 312
Cdd:cd03322 212 HTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWhGPTDLSPVGMAAALHLDLWv 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1546417147 313 -----KKIIKSVELTGPVkFSQDIgDLKSSYVIPyiqiNEQPGLGVSIDE 357
Cdd:cd03322 292 pnfgiQEYMRHAEETLEV-FPHSV-RFEDGYLHP----GEEPGLGVEIDE 335
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-290 |
1.58e-30 |
|
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: 119.51 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 1 MKIKTIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGwgesvpdeH-----ITGETPESTYAMLKNtLAPKLI 75
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTG--------HsylftYTPAALKSLKQLLDD-MAALLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 76 GQNPMEFEkIHELMDKTVHRAPA------AKAALDIACFDVVGKKLGVPVYQLLGGRyHEKFPVTHVLSIDEPEKMADEA 149
Cdd:cd03321 72 GEPLAPAE-LERALAKRFRLLGYtglvrmAAAGIDMAAWDALAKVHGLPLAKLLGGN-PRPVQAYDSHGLDGAKLATERA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 150 EEKLEEGYRSFKMKVGL-DVSGDVKRIKAVRARVGEEIAIRVDVNQGWENSAnTLQALRQLESLGLDWLEQPVAQDDIDG 228
Cdd:cd03321 150 VTAAEEGFHAVKTKIGYpTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPE-AIERGQALDQEGLTWIEEPTLQHDYEG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1546417147 229 MVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIE 290
Cdd:cd03321 229 HARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIP 290
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
142-238 |
7.03e-30 |
|
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: 110.45 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 142 PEKMADEAEEKLEE-GYRSFKMKVGLDVSGDVKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLGLDWLEQP 220
Cdd:smart00922 1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAW-TAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 1546417147 221 VAQDDIDGMVEIKSKTSV 238
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
146-310 |
3.23e-25 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 104.28 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 146 ADEAEEKLEE--GYRSFKMKV---GLDVSGDVKRIKAVRARVGEEIAIRVDVNQGWeNSANTLQALRQLESLG-LDWLEQ 219
Cdd:PRK02901 90 AAQVPEVLARfpGCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGW-SVDEAVAAARALDADGpLEYVEQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 220 PVAQddIDGMVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLanmAEMAGIECQIGSMVES 299
Cdd:PRK02901 169 PCAT--VEELAELRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDI---AEQIGLPVVVSSALDT 243
|
170
....*....|.
gi 1546417147 300 SVGSAAGFHVA 310
Cdd:PRK02901 244 SVGIAAGLALA 254
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
34-357 |
2.30e-23 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 100.37 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 34 VKLTTECGLVGWGesvpDEHITG-ETPESTYamLKNTLAPKLIGQNPMEFEKIHELMDKTVH--RAP---AAKAALDIAC 107
Cdd:PRK15072 20 LKITTDDGVTGLG----DATLNGrELAVASY--LQDHVCPLLIGRDAHRIEDIWQYLYRGAYwrRGPvtmSAIAAVDMAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 108 FDVVGKKLGVPVYQLLGGRYHEKFPV-THVLSIDEPEkMADEAEEKLEEGYRSFKMKV---GLD----VSGD-------- 171
Cdd:PRK15072 94 WDIKAKAAGMPLYQLLGGASREGVMVyGHANGRDIDE-LLDDVARHLELGYKAIRVQCgvpGLKttygVSKGkglayepa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 172 --------------------VKRIKAVRARVGEEIAIRVDVNqgweNSANTLQALR---QLESLGLDWLEQPVAQDDIDG 228
Cdd:PRK15072 173 tkgllpeeelwstekylrfvPKLFEAVRNKFGFDLHLLHDVH----HRLTPIEAARlgkSLEPYRLFWLEDPTPAENQEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 229 MVEIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQI-GSMVESSVGSAAGF 307
Cdd:PRK15072 249 FRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGShGPTDLSPVCMAAAL 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1546417147 308 HVAFS------KKIIKSVELTGPVkFSQDIgDLKSSYVIPyiqiNEQPGLGVSIDE 357
Cdd:PRK15072 329 HFDLWvpnfgiQEYMGHSEETLEV-FPHSY-TFEDGYLHP----GDAPGLGVDFDE 378
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
58-289 |
1.06e-22 |
|
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: 97.48 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 58 TPESTYAMLKNTLAPKLIGQNPMEFEKIHELMDKTVHR------APAAKAALDIACFDVVGKKLGVPVYQLLGgRYHEKF 131
Cdd:cd03328 48 ADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRNagrpgvAAMAISAVDIALWDLKARLLGLPLARLLG-RAHDSV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 132 PV--THVLSIDEPEKMADEAEEKLEEGYRSFKMKVGLDVSGDVKRIKAVRARVGEEIAIRVDVNQGWENSantlQALRQL 209
Cdd:cd03328 127 PVygSGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRK----QALALA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 210 ES---LGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEG--IRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMA 284
Cdd:cd03328 203 RAfadEGVTWFEEPVSSDDLAGLRLVRERGPAGMDIAAGeyAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALA 282
|
....*
gi 1546417147 285 EMAGI 289
Cdd:cd03328 283 AAHHV 287
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
3-331 |
1.37e-22 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 96.74 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 3 IKTIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTtECGLVGWGESVPDEHItGETPESTYAMLKnTLAPKLigQNPMEF 82
Cdd:PRK15129 1 MRTVKVYEEAWPLHTPFVIARGSRSEARVVVVELE-EEGIKGTGECTPYPRY-GESDASVMAQIM-SVVPQL--EKGLTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 83 EKIHELMDktvhrAPAAKAALDIACFDVVGKKLGVPVYQLLGGRYHEKFPVTHVLSIDEPEKMADEAEEKLEEGYRSFKM 162
Cdd:PRK15129 76 EALQKLLP-----AGAARNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 163 KvgLDVSGDVKRIKAVRARVGEEIAIrVDVNQGWEnsANTLQALRQ-LESLGLDWLEQPV-AQDD--IDGMVEiksktSV 238
Cdd:PRK15129 151 K--LDNHLISERMVAIRSAVPDATLI-VDANESWR--AEGLAARCQlLADLGVAMLEQPLpAQDDaaLENFIH-----PL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 239 PQMIDEGIRDMVDLRQIIAKRaaDKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAfskKIIKS 318
Cdd:PRK15129 221 PICADESCHTRSSLKALKGRY--EMVNIKLDKTGGLTEALALATEARAQGFALMLGCMLCTSRAISAALPLV---PQVRF 295
|
330
....*....|...
gi 1546417147 319 VELTGPVKFSQDI 331
Cdd:PRK15129 296 ADLDGPTWLAVDV 308
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
2-366 |
2.99e-19 |
|
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: 88.15 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 2 KIKTIEIFSIHLPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPD-EHITGetpestyamlKNTLAPKLIG-QNP 79
Cdd:cd03323 1 KITEMRVTPVAGHDSPLLNLSGAHEPFFTRNIVELTDDNGNTGVGESPGGaEALEA----------LLEAARSLVGgDVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 80 MEFEKIHELMDKTVHR---------------APAAKAALDIACFDVVGKKLGVPVYQLLGGR---------Y------HE 129
Cdd:cd03323 71 GAYLAVLESVRVAFADrdaggrglqtfdlrtTVHVVTAFEVALLDLLGQALGVPVADLLGGGqrdsvpflaYlfykgdRH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 130 KFPVTHVLSIDE------PEKMADEAEEKLEE-GYRSFKMKVG-LDVSGDVKRIKAVRARVgEEIAIRVDVNQGWensaN 201
Cdd:cd03323 151 KTDLPYPWFRDRwgealtPEGVVRLARAAIDRyGFKSFKLKGGvLPGEEEIEAVKALAEAF-PGARLRLDPNGAW----S 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 202 TLQALRQLESLG--LDWLEQPVAqdDIDGMVEIKSKTSVP---QMIdegirdMVDLRQIIAKRAADKINIKLMKC---GG 273
Cdd:cd03323 226 LETAIRLAKELEgvLAYLEDPCG--GREGMAEFRRATGLPlatNMI------VTDFRQLGHAIQLNAVDIPLADHhfwGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 274 IYPAMKLANMAEMAGIECQIGSMVESSVGSAAGFHVAFS-KKIIKSVELTGPVKFSQDIGDLKSSYVIPYIQINEQPGLG 352
Cdd:cd03323 298 MRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMTHVAAAaPGLITACDTHWIWQDGQVITGEPLRIKDGKVAVPDKPGLG 377
|
410
....*....|....
gi 1546417147 353 VSIDEVVLAELTQN 366
Cdd:cd03323 378 VELDRDKLAKAHEL 391
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
13-124 |
2.86e-18 |
|
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: 79.82 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 13 LPLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPdehiTGETPESTYAMLKNTLAPKLIGQNPMEFEKIHELMDKT 92
Cdd:pfam02746 10 GWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATS----YGGRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRA 85
|
90 100 110
....*....|....*....|....*....|..
gi 1546417147 93 VHRAPAAKAALDIACFDVVGKKLGVPVYQLLG 124
Cdd:pfam02746 86 ALGNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
143-274 |
2.47e-15 |
|
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: 76.61 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 143 EKMADEAEEKLEEGYRSFKMKVGLDVSGDVKRIKAVRARVGEEIAIRVDVNQGWE-NSAntLQALRQLESLGLDWLEQPV 221
Cdd:cd03324 198 EKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDvPEA--IEWVKQLAEFKPWWIEEPT 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1546417147 222 AQDDIDGMVEIK---SKTSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGI 274
Cdd:cd03324 276 SPDDILGHAAIRkalAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGV 331
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-302 |
1.27e-14 |
|
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: 73.69 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 9 FSIHLPLIKPFIISYATYPHIQSIIVKLTTEcGLVGWGESVPDEHITGETPESTY---AMLKNTLAPKLIGQNPME---- 81
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDE-GRTGWGEIAPLPGFGTETLAEALdfcRALIEEITRGDIEAIDDQlpsv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 82 ---FEKIHELMDKTVHRAPAAKaaldiacfdvvgkklgVPVYQLLGGRyhekfPVTHVLsidepeKMADEaeekleEGYR 158
Cdd:TIGR01927 80 afgFESALIELESGDELPPASN----------------YYVALLPAGD-----PALLLL------RSAKA------EGFR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 159 SFKMKVGL-DVSGDVKRIKAVRARVGEEIAIRVDVNQGWE--NSANTLQALRQLESLGLDWLEQPVAqdDIDGMVEIKSK 235
Cdd:TIGR01927 127 TFKWKVGVgELAREGMLVNLLLEALPDKAELRLDANGGLSpdEAQQFLKALDPNLRGRIAFLEEPLP--DADEMSAFSEA 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1546417147 236 TSVPQMIDEGIRDMVDLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAGIECQIGSMVESSVG 302
Cdd:TIGR01927 205 TGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIA 271
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
98-220 |
4.56e-12 |
|
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: 66.65 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 98 AAKAALDIACFDVVGKKLGVPVYQLLGGRY--HEKFPVTHVLSI-------DEPEKMADEAEEKLEEGYRSFKMKVG-LD 167
Cdd:cd03326 108 VAVGALDMAVWDAVAKIAGLPLYRLLARRYgrGQADPRVPVYAAggyyypgDDLGRLRDEMRRYLDRGYTVVKIKIGgAP 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1546417147 168 VSGDVKRIKAVRARVGEEIAIRVDVNqGWENSANTLQALRQLESLGLDWLEQP 220
Cdd:cd03326 188 LDEDLRRIEAALDVLGDGARLAVDAN-GRFDLETAIAYAKALAPYGLRWYEEP 239
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
14-255 |
1.39e-10 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 61.57 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 14 PLIKPFIISYATYPHIQSIIVKLTTECGLVGWGESVPDEHITGETPESTYAM---LKNTLAPKLIgqnpmefEKIHElmd 90
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEIAPLPWFGSETLEEALAFcqqLPGEITPEQI-------FSIPD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 91 ktvhRAPAAKAALDIACFDVVGKKLGVpvyqllggryhEKFPVTHVLSIDEPEKMADEAEEKLEEGYRSFKMKVGLD-VS 169
Cdd:PRK02714 83 ----ALPACQFGFESALENESGSRSNV-----------TLNPLSYSALLPAGEAALQQWQTLWQQGYRTFKWKIGVDpLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 170 GDVKRIKAVRARVGEEIAIRVDVNQGWEN-SANT-LQALRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEGIr 247
Cdd:PRK02714 148 QELKIFEQLLERLPAGAKLRLDANGGLSLeEAKRwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESV- 226
|
....*...
gi 1546417147 248 dmVDLRQI 255
Cdd:PRK02714 227 --ANLAQL 232
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
31-288 |
1.06e-09 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 59.36 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 31 SIIVKLTTECGLVGWGESvpdehiTGETPESTyaMLKNTLAPKLIGQNPMEFEKIHELMDK-TVHRAPA-----AKAALD 104
Cdd:PRK15440 58 TLVVEVEAENGQVGFAVS------TAGEMGAF--IVEKHLNRFIEGKCVSDIELIWDQMLNaTLYYGRKglvmnTISCVD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 105 IACFDVVGKKLGVPVYQLLGGryhekfPVThvlsiDEPEKMADEAEEKL--EEGYRSFKMKV---------GLdvSGDVK 173
Cdd:PRK15440 130 LALWDLLGKVRGLPVYKLLGG------AVR-----DELQFYATGARPDLakEMGFIGGKMPLhhgpadgdaGL--RKNAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 174 RIKAVRARVGEEIAIRVDVnqgWE----NSANTLqaLRQLESLGLDWLEQPVAQDDIDGMVEIKSKTSVPQMIDEGIRDM 249
Cdd:PRK15440 197 MVADMREKVGDDFWLMLDC---WMsldvNYATKL--AHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVTSGEHEA 271
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1546417147 250 V--DLRQIIAKRAADKINIKLMKCGGIYPAMKLANMAEMAG 288
Cdd:PRK15440 272 TlqGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARG 312
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
142-305 |
2.54e-09 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 59.10 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 142 PEKMADEAEEKLEEGYRSFKMKVGLDVSG--DVKRIKAVRARVGEEIAIRVDVNQGWensanTLQALRQ----LESLGLD 215
Cdd:PLN02980 1091 PLEVAYVARKLVEEGFSAIKLKVGRRVSPiqDAAVIQEVRKAVGYQIELRADANRNW-----TYEEAIEfgslVKSCNLK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 216 WLEQPVAqdDIDGMVEIKSKTSVPQMIDEGIRDMV-DLRQIIAKRAADKI---NIKLMKCGGIYPAMKLANMAEMAGIEC 291
Cdd:PLN02980 1166 YIEEPVQ--DEDDLIKFCEETGLPVALDETIDKFEeCPLRMLTKYTHPGIvavVIKPSVVGGFENAALIARWAQQHGKMA 1243
|
170
....*....|....
gi 1546417147 292 QIGSMVESSVGSAA 305
Cdd:PLN02980 1244 VISAAYESGLGLSA 1257
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
175-262 |
8.49e-04 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 41.02 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 175 IKAVRARVGEEIAIRV-----DVNQGWENSANTLQALRQLESLGLDWLE-----------QPVAQDDIDGM-----VEIK 233
Cdd:cd02803 198 VAAVREAVGPDFPVGVrlsadDFVPGGLTLEEAIEIAKALEEAGVDALHvsggsyespppIIPPPYVPEGYflelaEKIK 277
|
90 100
....*....|....*....|....*....
gi 1546417147 234 SKTSVPQMIDEGIRDMVDLRQIIAKRAAD 262
Cdd:cd02803 278 KAVKIPVIAVGGIRDPEVAEEILAEGKAD 306
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
175-266 |
8.86e-03 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240084 [Multi-domain] Cd Length: 338 Bit Score: 37.56 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546417147 175 IKAVRARVGEEIAIRVDVN-----QGWENSANTLQALRQLESLGLDWLE-------QPVAQDD------------IDGMV 230
Cdd:cd04733 206 YDAIRAAVGPGFPVGIKLNsadfqRGGFTEEDALEVVEALEEAGVDLVElsggtyeSPAMAGAkkestiareayfLEFAE 285
|
90 100 110
....*....|....*....|....*....|....*.
gi 1546417147 231 EIKSKTSVPQMIDEGIRDMVDLRQIIAKRAADKINI 266
Cdd:cd04733 286 KIRKVTKTPLMVTGGFRTRAAMEQALASGAVDGIGL 321
|
|
| |
