|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-355 |
2.49e-103 |
|
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: 308.77 E-value: 2.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 2 KIVRIETFPLFHRLEKPYGDANGfkryRTCYLIRIITESGIDGWGECVDWL--PALHVGFTKRIIPFLLGKQAGSRLSLV 79
Cdd:cd03316 1 KITDVETFVLRVPLPEPGGAVTW----RNLVLVRVTTDDGITGWGEAYPGGrpSAVAAAIEDLLAPLLIGRDPLDIERLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 80 RTIQKWH---------QRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASFQSYSDSPQwisRSVSNVEAQLKK 150
Cdd:cd03316 77 EKLYRRLfwrgrggvaMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDSPE---ELAEEAKRAVAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 151 GFEQIKVKIGGTS-----FKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDY 225
Cdd:cd03316 154 GFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEY-DLFWFEEPVPPDDLEGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 226 AMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRLYALFAQ 305
Cdd:cd03316 233 ARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489337848 306 ACLPpwskmkNDHI-EPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTE 355
Cdd:cd03316 313 AALP------NFGIlEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-364 |
2.88e-86 |
|
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: 265.15 E-value: 2.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 1 MKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGECVDW---LPALHVGFTKRIIPFLLGKQAGSRLS 77
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGgtgAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 78 LVRTIQK---WHQRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASfqSYSDSPQwisRSVSNVEAQLKKGFEQ 154
Cdd:COG4948 81 LWQRLYRalpGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYAT--LGIDTPE---EMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 155 IKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLRSRLSV 234
Cdd:COG4948 156 LKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDL-GLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 235 PVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAY-DGSLSRLYALFAQACLPpwsk 313
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMlESGIGLAAALHLAAALP---- 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489337848 314 mkndHIEPIEWDVMENPFTDLVS--LQPSKGMVHIPKGKGIGTEINMEIVNRY 364
Cdd:COG4948 311 ----NFDIVELDGPLLLADDLVEdpLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
145-360 |
1.64e-51 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 170.82 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 145 EAQLKKGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQD 224
Cdd:pfam13378 8 RAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEEL-GLLWIEEPVPPDDLEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 225 YAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRLYALFA 304
Cdd:pfam13378 87 LARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPIGLAASLHL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489337848 305 QACLPPwskmkNDHIEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINMEI 360
Cdd:pfam13378 167 AAAVPN-----LLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-361 |
6.31e-17 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 81.10 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 1 MKIVRIETFPLfhrleKPygdangfkryRTCYLiRIITESGIDGWGECVDWLPALHV-GFTKRIIPFLLGKQAgsrlslv 79
Cdd:PRK14017 1 MKITKLETFRV-----PP----------RWLFL-KIETDEGIVGWGEPVVEGRARTVeAAVHELADYLIGKDP------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 80 RTIQKWHQ---RAA---------SAVS---MALTEIAAKAADCSVCELWGGRYREEIPVYasfqsysdspQWI-----SR 139
Cdd:PRK14017 58 RRIEDHWQvmyRGGfyrggpilmSAIAgidQALWDIKGKALGVPVHELLGGLVRDRIRVY----------SWIggdrpAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 140 SVSNVEAQLKKGFEQIKVkiGGTsfkEDVRHIN-------------ALQHTAGSSITMILDANQSYDAAAAfkwERYFSE 206
Cdd:PRK14017 128 VAEAARARVERGFTAVKM--NGT---EELQYIDsprkvdaavarvaAVREAVGPEIGIGVDFHGRVHKPMA---KVLAKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 207 WTNIG--WLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFG 284
Cdd:PRK14017 200 LEPYRpmFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 285 VRASAHAYDGSLSRLYALFAQACLPpwskmkNDHIEPIEWDVMENPFTDLVS-------LQPSKGMVHIPKGKGIGTEIN 357
Cdd:PRK14017 280 VALAPHCPLGPIALAACLQVDAVSP------NAFIQEQSLGIHYNQGADLLDyvknkevFAYEDGFVAIPTGPGLGIEID 353
|
....
gi 489337848 358 MEIV 361
Cdd:PRK14017 354 EAKV 357
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
149-234 |
1.25e-15 |
|
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: 71.54 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 149 KKGFEQIKVKIGGTSfKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFsEWTNIGWLEEPLPFDQPQDYAML 228
Cdd:smart00922 14 EAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEAL-DELGLEWIEEPVPPDDLEGLAEL 91
|
....*.
gi 489337848 229 RSRLSV 234
Cdd:smart00922 92 RRATPI 97
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
151-310 |
9.33e-08 |
|
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: 52.89 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 151 GFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYF--SEWTNIGWLEEPLPfdQPQDYAML 228
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALdpNLRGRIAFLEEPLP--DADEMSAF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 229 RSRLSVPVAGGENMKGPAQYVPLLSQ--RCLDIIQPDVMhvNGIDEFRDCLQLARYFGVRAS-AHAYDGSLSR-LYALFA 304
Cdd:TIGR01927 202 SEATGTAIALDESLWELPQLADEYGPgwRGALVIKPAII--GSPAKLRDLAQKAHRLGLQAVfSSVFESSIALgQLARLA 279
|
....*.
gi 489337848 305 QACLPP 310
Cdd:TIGR01927 280 AKLSPD 285
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-355 |
2.49e-103 |
|
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: 308.77 E-value: 2.49e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 2 KIVRIETFPLFHRLEKPYGDANGfkryRTCYLIRIITESGIDGWGECVDWL--PALHVGFTKRIIPFLLGKQAGSRLSLV 79
Cdd:cd03316 1 KITDVETFVLRVPLPEPGGAVTW----RNLVLVRVTTDDGITGWGEAYPGGrpSAVAAAIEDLLAPLLIGRDPLDIERLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 80 RTIQKWH---------QRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASFQSYSDSPQwisRSVSNVEAQLKK 150
Cdd:cd03316 77 EKLYRRLfwrgrggvaMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGYDDSPE---ELAEEAKRAVAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 151 GFEQIKVKIGGTS-----FKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDY 225
Cdd:cd03316 154 GFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEY-DLFWFEEPVPPDDLEGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 226 AMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRLYALFAQ 305
Cdd:cd03316 233 ARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489337848 306 ACLPpwskmkNDHI-EPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTE 355
Cdd:cd03316 313 AALP------NFGIlEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-364 |
2.88e-86 |
|
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: 265.15 E-value: 2.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 1 MKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGECVDW---LPALHVGFTKRIIPFLLGKQAGSRLS 77
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGgtgAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 78 LVRTIQK---WHQRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASfqSYSDSPQwisRSVSNVEAQLKKGFEQ 154
Cdd:COG4948 81 LWQRLYRalpGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYAT--LGIDTPE---EMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 155 IKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLRSRLSV 234
Cdd:COG4948 156 LKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDL-GLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 235 PVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAY-DGSLSRLYALFAQACLPpwsk 313
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMlESGIGLAAALHLAAALP---- 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489337848 314 mkndHIEPIEWDVMENPFTDLVS--LQPSKGMVHIPKGKGIGTEINMEIVNRY 364
Cdd:COG4948 311 ----NFDIVELDGPLLLADDLVEdpLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
145-360 |
1.64e-51 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 170.82 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 145 EAQLKKGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQD 224
Cdd:pfam13378 8 RAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEEL-GLLWIEEPVPPDDLEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 225 YAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRLYALFA 304
Cdd:pfam13378 87 LARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPIGLAASLHL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489337848 305 QACLPPwskmkNDHIEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINMEI 360
Cdd:pfam13378 167 AAAVPN-----LLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
34-357 |
1.07e-30 |
|
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: 119.36 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 34 IRIITESGIDGWGECVDWLPALHVgFTKRIIPFLLGKqagsrlsLVRTIQKWHQR----------------AASAVSMAL 97
Cdd:cd03327 14 VEIETDDGTVGYANTTGGPVACWI-VDQHLARFLIGK-------DPSDIEKLWDQmyratlaygrkgiamaAISAVDLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 98 TEIAAKAADCSVCELWGGRYREEIPVYASFQSYSDSPQWISRSVSnveaQLKKGFEQIKVKI------GGTSFKEDVRHI 171
Cdd:cd03327 86 WDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKE----YLKEGYRGMKMRFgygpsdGHAGLRKNVELV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 172 NALQHTAGSSITMILDANQSYDAAAAFKW----ERYfsewtNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQ 247
Cdd:cd03327 162 RAIREAVGYDVDLMLDCYMSWNLNYAIKMaralEKY-----ELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 248 YVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAydGSLSRLYALFAQACLP--------PWSKMKndhi 319
Cdd:cd03327 237 FKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA--SQIYNYHFIMSEPNSPfaeylpnsPDEVGN---- 310
|
330 340 350
....*....|....*....|....*....|....*...
gi 489337848 320 ePIEWDVMENPftdlvsLQPSKGMVHIPKGKGIGTEIN 357
Cdd:cd03327 311 -PLFYYIFLNE------PVPVNGYFDLSDKPGFGLELN 341
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-363 |
5.93e-30 |
|
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: 117.80 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 2 KIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGECVDWLPALHVGFT----KRII-----PFLLGKQA 72
Cdd:cd03318 1 KIEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESpetiKAIIdrylaPLLIGRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 73 ----GSRLSLVRTIQKwHQRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASFQSySDSPQWISRSVSNVEAql 148
Cdd:cd03318 81 tnigAAMALLDRAVAG-NLFAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLAS-GDTERDIAEAEEMLEA-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 149 kKGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPFDQPQDYAML 228
Cdd:cd03318 157 -GRHRRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEA-AGVELIEQPVPRENLDGLARL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 229 RSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRA-SAHAYDGSLSRLYALFAQAC 307
Cdd:cd03318 235 RSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALyGGTMLESSIGTAASAHLFAT 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 308 LP--PWSkmkNDHIEP--IEWDVMENPftdlvsLQPSKGMVHIPKGKGIGTEINMEIVNR 363
Cdd:cd03318 315 LPslPFG---CELFGPllLAEDLLEEP------LAYRDGELHVPTGPGLGVRLDEDKVRR 365
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
89-290 |
1.47e-28 |
|
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: 114.05 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 89 AASAVSMALTEIAAKAADCSVCELWGgRYREEIPVYAS--FQSYSDSpqwisRSVSNVEAQLKKGFEQIKVKIGgTSFKE 166
Cdd:cd03328 95 AISAVDIALWDLKARLLGLPLARLLG-RAHDSVPVYGSggFTSYDDD-----RLREQLSGWVAQGIPRVKMKIG-RDPRR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 167 DVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPFDQPQDYAMLRSRL--SVPVAGGENMKG 244
Cdd:cd03328 168 DPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFAD-EGVTWFEEPVSSDDLAGLRLVRERGpaGMDIAAGEYAYT 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489337848 245 PAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAH 290
Cdd:cd03328 247 LAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH 292
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
1-364 |
1.02e-25 |
|
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: 106.03 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 1 MKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDG--------------WGECVDWLPALHVGftKRIIPF 66
Cdd:cd03321 1 VLITGLRARAVNVPMQYPVHTSVGTVATAPLVLIDLATDEGVTGhsylftytpaalksLKQLLDDMAALLVG--EPLAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 67 LLGKQAGSRLSLV--RTIQKWhqrAASAVSMALTEIAAKAADCSVCELWGGRYREeIPVYASfqsysDSPQWISRSVSNV 144
Cdd:cd03321 79 ELERALAKRFRLLgyTGLVRM---AAAGIDMAAWDALAKVHGLPLAKLLGGNPRP-VQAYDS-----HGLDGAKLATERA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 145 EAQLKKGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPFDQPQD 224
Cdd:cd03321 150 VTAAEEGFHAVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQ-EGLTWIEEPTLQHDYEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 225 YAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRLYALFA 304
Cdd:cd03321 229 HARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLFQEISAHLLAVTP 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489337848 305 QAclpPWskmkndhIEPIEW--DVMENPftdlvsLQPSKGMVHIPKGKGIGTEINMEIVNRY 364
Cdd:cd03321 309 TA---HW-------LEYVDWagAILEPP------LKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-363 |
2.81e-25 |
|
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: 105.17 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 2 KIVRIETfplfHRLEKPYGDANGFKRY--------RTCYLIRIITESGIDG--WGECVDWLPALHVGFTKriiPFLLGKQ 71
Cdd:cd03329 1 KITDVEV----TVFEYPTQPVSFDGGHhhpgpagtRKLALLTIETDEGAKGhaFGGRPVTDPALVDRFLK---KVLIGQD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 72 AGSRLSLVRTIQKWHQ----RAASAVSMALTEIAAKAADCSVCELWGGrYREEIPVYASFQSYSDSPQWISRSVSNVEAQ 147
Cdd:cd03329 74 PLDRERLWQDLWRLQRgltdRGLGLVDIALWDLAGKYLGLPVHRLLGG-YREKIPAYASTMVGDDLEGLESPEAYADFAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 148 --LKKGFEQIKVKI-GGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPFDQPQD 224
Cdd:cd03329 153 ecKALGYRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEE-LGFFWYEDPLREASISS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 225 YAMLRSRLSVPVAGGENMKGPAQ-YVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAydGSLSRLYALF 303
Cdd:cd03329 232 YRWLAEKLDIPILGTEHSRGALEsRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHG--NGAANLHVIA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489337848 304 A-QAClpPWSKMKNDHiEPIEWDVMENPFTDLVSLQPSKGMVHIPKGKGIGTEINMEIVNR 363
Cdd:cd03329 310 AiRNT--RYYERGLLH-PSQKYDVYAGYLSVLDDPVDSDGFVHVPKGPGLGVEIDFDYIER 367
|
|
| 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 ... |
4-260 |
1.65e-23 |
|
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: 99.19 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 4 VRIETFPLfhrlEKPYGDANGFKRYRTCYLIRIiTESGIDGWGECVdwlPALHV---------GFTKRIIPFLLGK--QA 72
Cdd:cd03319 4 LRPERLPL----KRPFTIARGSRTEAENVIVEI-ELDGITGYGEAA---PTPRVtgetvesvlAALKSVRPALIGGdpRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 73 GSRLSLVRTIQKWHQRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPvyASFQSYSDSPQwisRSVSNVEAQLKKGF 152
Cdd:cd03319 76 EKLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLE--TDYTISIDTPE---AMAAAAKKAAKRGF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 153 EQIKVKIGGtSFKEDVRHINALQHTAGSsITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPFDQPQDYAMLRSRL 232
Cdd:cd03319 151 PLLKIKLGG-DLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELLRELAE-LGVELIEQPVPAGDDDGLAYLRDKS 227
|
250 260
....*....|....*....|....*...
gi 489337848 233 SVPVAGGENMKGPAQYVPLLSQRCLDII 260
Cdd:cd03319 228 PLPIMADESCFSAADAARLAGGGAYDGI 255
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
29-367 |
5.49e-23 |
|
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: 98.67 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 29 RTCYLIRIITESGIDGWGECVDWLPALHVG--FTKRIIPFLLGKQAGsrlslvRTIQKWH--------------QRAASA 92
Cdd:cd03322 14 RNFVTLKITTDQGVTGLGDATLNGRELAVKayLREHLKPLLIGRDAN------RIEDIWQylyrgaywrrgpvtMNAIAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 93 VSMALTEIAAKAADCSVCELWGGRYREEIPVYaSFQSYSDSPQwisrSVSNVEAQLKKGFEQIKVKIggtsfkedVRHIN 172
Cdd:cd03322 88 VDMALWDIKGKAAGMPLYQLLGGKSRDGIMVY-SHASGRDIPE----LLEAVERHLAQGYRAIRVQL--------PKLFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 173 ALQHTAGSSITMILDANQSYDAAAAFKWERYFsEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYVPLL 252
Cdd:cd03322 155 AVREKFGFEFHLLHDVHHRLTPNQAARFGKDV-EPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 253 SQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAyDGSLSrlyalfaqaclpPWSKMKNDHIE------PIEWDV 326
Cdd:cd03322 234 QERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHG-PTDLS------------PVGMAAALHLDlwvpnfGIQEYM 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489337848 327 MENPFTDLV---SLQPSKGMVHIPKGKGIGTEINMEIVNRYKWD 367
Cdd:cd03322 301 RHAEETLEVfphSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYV 344
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
85-287 |
1.99e-21 |
|
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: 92.40 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 85 WHQRAASAVSMALTEIAAKAADCSVCELwGGRYREEIPVyasfqSYSDSPQWISRSVSNVEAQLKKGFEQIKVKIGGTSf 164
Cdd:cd03315 40 WAEATKAAVDMALWDLWGKRLGVPVYLL-LGGYRDRVRV-----AHMLGLGEPAEVAEEARRALEAGFRTFKLKVGRDP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 165 KEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKG 244
Cdd:cd03315 113 ARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDL-GLDYVEQPLPADDLEGRAALARATDTPIMADESAFT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489337848 245 PAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRA 287
Cdd:cd03315 192 PHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPV 234
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-357 |
4.73e-21 |
|
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: 92.77 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 2 KIVRIETFplfhRLEKPYgdangfkryrtcYLIRIITESGIDGWGE-CVDWLPALHVGFTKRIIPFLLGK---------Q 71
Cdd:cd03325 1 KITKIETF----VVPPRW------------LFVKIETDEGVVGWGEpTVEGKARTVEAAVQELEDYLIGKdpmniehhwQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 72 AGSRLSLVR--TIqkwHQRAASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYasfqsysdspQWI-SRSVSNVEAQL 148
Cdd:cd03325 65 VMYRGGFYRggPV---LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVY----------SWIgGDRPSDVAEAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 149 KKGFEQ--IKVKIGGT----------SFKEDVRHINALQHTAGSSITMILDANQSYDAAAAfkwERYFSEWTNIG--WLE 214
Cdd:cd03325 132 RARREAgfTAVKMNATeelqwidtskKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMA---KDLAKELEPYRllFIE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 215 EPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDG 294
Cdd:cd03325 209 EPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLG 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489337848 295 SLSRLYALFAQACLPPW---SKMKNDH--IEPIEWDVMENPftdlVSLQPSKGMVHIPKGKGIGTEIN 357
Cdd:cd03325 289 PIALAASLHVDASTPNFliqEQSLGIHynEGDDLLDYLVDP----EVFDMENGYVKLPTGPGLGIEID 352
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
4-311 |
7.00e-21 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 90.08 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 4 VRIETFPLFHRLEKPYGDANGFKRYrtcyLIRIITESGIDGWGECVdwlpalhvgftkriipfllgkqagsrlslvrtiq 83
Cdd:cd00308 3 VYAVRLPTSRPFYLAGGTADTNDTV----LVKLTTDSGVVGWGEVI---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 84 kwhqraaSAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASfqsysdspqwisrsvsnveaqlkkgfeqikvkiggts 163
Cdd:cd00308 45 -------SGIDMALWDLAAKALGVPLAELLGGGSRDRVPAYGS------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 164 fkedVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMK 243
Cdd:cd00308 81 ----IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKY-GLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVT 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 244 GPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHA-YDGSLSRLYAL-FAQACLPPW 311
Cdd:cd00308 156 TVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGtLESSIGTAAALhLAAALPNDR 225
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-363 |
1.49e-19 |
|
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: 88.45 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 6 IETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGECV-DWLP---------ALHVgfTKR-IIPFLLGK---Q 71
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVaFEGPfyteetnatAWHI--LKDyLLPLLLGRefsH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 72 AGSRLSLVRTIqKWHQRAASAVSMALTEIAAKAADCSVCELWGGRyREEIPVYASFQSYSDSPQWISRsvsnVEAQLKKG 151
Cdd:cd03317 79 PEEVSERLAPI-KGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGT-RDSIPVGVSIGIQDDVEQLLKQ----IERYLEEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 152 FEQIKVKIGGTsfkEDVRHINALQHTAGsSITMILDANQSY---DAAAAFKWERYfsewtNIGWLEEPLPFDQPQDYAML 228
Cdd:cd03317 153 YKRIKLKIKPG---WDVEPLKAVRERFP-DIPLMADANSAYtlaDIPLLKRLDEY-----GLLMIEQPLAADDLIDHAEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 229 RSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVrasaHAYDGS-----LSRLYALf 303
Cdd:cd03317 224 QKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI----PVWCGGmlesgIGRAHNV- 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489337848 304 AQACLP----PWSKMKNDH--IEpiewDVMENPFTdlvsLQPskGMVHIPKGKGIGTEINMEIVNR 363
Cdd:cd03317 299 ALASLPnftyPGDISASSRyfEE----DIITPPFE----LEN--GIISVPTGPGIGVTVDREALKK 354
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-361 |
6.31e-17 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 81.10 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 1 MKIVRIETFPLfhrleKPygdangfkryRTCYLiRIITESGIDGWGECVDWLPALHV-GFTKRIIPFLLGKQAgsrlslv 79
Cdd:PRK14017 1 MKITKLETFRV-----PP----------RWLFL-KIETDEGIVGWGEPVVEGRARTVeAAVHELADYLIGKDP------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 80 RTIQKWHQ---RAA---------SAVS---MALTEIAAKAADCSVCELWGGRYREEIPVYasfqsysdspQWI-----SR 139
Cdd:PRK14017 58 RRIEDHWQvmyRGGfyrggpilmSAIAgidQALWDIKGKALGVPVHELLGGLVRDRIRVY----------SWIggdrpAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 140 SVSNVEAQLKKGFEQIKVkiGGTsfkEDVRHIN-------------ALQHTAGSSITMILDANQSYDAAAAfkwERYFSE 206
Cdd:PRK14017 128 VAEAARARVERGFTAVKM--NGT---EELQYIDsprkvdaavarvaAVREAVGPEIGIGVDFHGRVHKPMA---KVLAKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 207 WTNIG--WLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFG 284
Cdd:PRK14017 200 LEPYRpmFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 285 VRASAHAYDGSLSRLYALFAQACLPpwskmkNDHIEPIEWDVMENPFTDLVS-------LQPSKGMVHIPKGKGIGTEIN 357
Cdd:PRK14017 280 VALAPHCPLGPIALAACLQVDAVSP------NAFIQEQSLGIHYNQGADLLDyvknkevFAYEDGFVAIPTGPGLGIEID 353
|
....
gi 489337848 358 MEIV 361
Cdd:PRK14017 354 EAKV 357
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
14-310 |
1.22e-15 |
|
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: 76.14 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 14 RLEKPYGDANGFKRYRTCYLIRIITESGIDGWGEcvdwlpalhvgftkrIIPFLLgkqagsrlslvrtiqkwhqraASAV 93
Cdd:cd03320 9 PLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGE---------------IAPLPL---------------------AFGI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 94 SMALTEIAAKAadcsvceLWGGRYREEIPVYASFqSYSDSPQwisrsVSNVEAQLKKGFEQIKVKIGGTSFKEDVRHINA 173
Cdd:cd03320 53 ESALANLEALL-------VGFTRPRNRIPVNALL-PAGDAAA-----LGEAKAAYGGGYRTVKLKVGATSFEEDLARLRA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 174 LQHTAGSSITMILDANQSYDAAAAFKWERYFSEwTNIGWLEEPLPfdQPQDYAMLRSRLSVPVAGGE---NMKGPAQYVP 250
Cdd:cd03320 120 LREALPADAKLRLDANGGWSLEEALAFLEALAA-GRIEYIEQPLP--PDDLAELRRLAAGVPIALDEslrRLDDPLALAA 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489337848 251 LLSQRCLdIIQPdvMHVNGIDEFRDCLQLARYFGVRAS-AHAYDGSLSRL-YALFAQACLPP 310
Cdd:cd03320 197 AGALGAL-VLKP--ALLGGPRALLELAEEARARGIPAVvSSALESSIGLGaLAHLAAALPPL 255
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
149-234 |
1.25e-15 |
|
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: 71.54 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 149 KKGFEQIKVKIGGTSfKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFsEWTNIGWLEEPLPFDQPQDYAML 228
Cdd:smart00922 14 EAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEAL-DELGLEWIEEPVPPDDLEGLAEL 91
|
....*.
gi 489337848 229 RSRLSV 234
Cdd:smart00922 92 RRATPI 97
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
118-291 |
2.21e-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: 77.00 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 118 REEIPVYASFQSYSDSPQWISRSVSNV-----EAqLKKGFEQIKVKIGGtSFKEDVRHINALQHTAGSSITMILDANQSY 192
Cdd:cd03324 174 READLLAEGYPAYTTSAGWLGYSDEKLrrlckEA-LAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRW 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 193 DAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLR---SRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNG 269
Cdd:cd03324 252 DVPEAIEWVKQLAEF-KPWWIEEPTSPDDILGHAAIRkalAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGG 330
|
170 180
....*....|....*....|..
gi 489337848 270 IDEFRDCLQLARYFGVRASAHA 291
Cdd:cd03324 331 VNENLAVLLMAAKFGVPVCPHA 352
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
89-300 |
3.93e-15 |
|
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: 75.89 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 89 AASAVSMALTEIAAKAADCSVCELWGGRYREE-----IPVYASFQSYSDSpQWISRSVSNVEAQLKKGFEQIKVKIGGTS 163
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLARRYGRGqadprVPVYAAGGYYYPG-DDLGRLRDEMRRYLDRGYTVVKIKIGGAP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 164 FKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPlpfDQPQDYAM---LRSRLSVPVAGGE 240
Cdd:cd03326 188 LDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPY-GLRWYEEP---GDPLDYALqaeLADHYDGPIATGE 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489337848 241 NMKGPAQYVPLLS----QRCLDIIQPDVMHVNGIDEFRDCLQLARYFGV-RASAHAYDGSLSRLY 300
Cdd:cd03326 264 NLFSLQDARNLLRyggmRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWsRRRFFPHGGHLMSLH 328
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
89-290 |
5.91e-08 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 53.96 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 89 AASAVSMALTEIAAKAADCSVCELWGGRYREEIPVYASfqsysdspqwisrsvsNVEAQLKK--GFeqikvkIGGT---- 162
Cdd:PRK15440 124 TISCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFYAT----------------GARPDLAKemGF------IGGKmplh 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 163 --------SFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYFSEWtNIGWLEEPLPFDQPQDYAMLRSRlsV 234
Cdd:PRK15440 182 hgpadgdaGLRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPY-GLKWIEECLPPDDYWGYRELKRN--A 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 235 P----VAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAH 290
Cdd:PRK15440 259 PagmmVTSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
151-310 |
9.33e-08 |
|
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: 52.89 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 151 GFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFKWERYF--SEWTNIGWLEEPLPfdQPQDYAML 228
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALdpNLRGRIAFLEEPLP--DADEMSAF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 229 RSRLSVPVAGGENMKGPAQYVPLLSQ--RCLDIIQPDVMhvNGIDEFRDCLQLARYFGVRAS-AHAYDGSLSR-LYALFA 304
Cdd:TIGR01927 202 SEATGTAIALDESLWELPQLADEYGPgwRGALVIKPAII--GSPAKLRDLAQKAHRLGLQAVfSSVFESSIALgQLARLA 279
|
....*.
gi 489337848 305 QACLPP 310
Cdd:TIGR01927 280 AKLSPD 285
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
33-359 |
2.33e-06 |
|
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: 49.24 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 33 LIRIITESGIDGWGECVDWLPALHVgfTKRIIPFLLG---------------KQAGSRLSLVRTIQKWHQR----AASAV 93
Cdd:cd03323 32 IVELTDDNGNTGVGESPGGAEALEA--LLEAARSLVGgdvfgaylavlesvrVAFADRDAGGRGLQTFDLRttvhVVTAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 94 SMALTEIAAKAADCSVCELWGGRYREEIPVYAS-FQSYSDSP-----QWISRS----------VSNVEAQLKK-GFEQIK 156
Cdd:cd03323 110 EVALLDLLGQALGVPVADLLGGGQRDSVPFLAYlFYKGDRHKtdlpyPWFRDRwgealtpegvVRLARAAIDRyGFKSFK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 157 VKIGGTSFKEDVRHINAL-QHTAGSSITmiLDANQSYDAAAAFKWERYFSEwtNIGWLEEPLPfdQPQDYAMLRSRLSVP 235
Cdd:cd03323 190 LKGGVLPGEEEIEAVKALaEAFPGARLR--LDPNGAWSLETAIRLAKELEG--VLAYLEDPCG--GREGMAEFRRATGLP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 236 VAggENM--KGPAQYVPLLSQRCLDIIQPDVMHVNGIdefRDCLQLA---RYFGVRASAHA---YDGSLSRLYALFAQ-- 305
Cdd:cd03323 264 LA--TNMivTDFRQLGHAIQLNAVDIPLADHHFWGGM---RGSVRVAqvcETWGLGWGMHSnnhLGISLAMMTHVAAAap 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 306 ----ACLPPWSKMKNDHI--EPIEWDvmenpftdlvslqpsKGMVHIPKGKGIGTEINME 359
Cdd:cd03323 339 glitACDTHWIWQDGQVItgEPLRIK---------------DGKVAVPDKPGLGVELDRD 383
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
89-290 |
8.81e-05 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 44.13 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 89 AASAVSMALTEIAAKAADCSVCELWGGRYREEIPVY--ASFQSysdspqwISRSVSNVEAQLKKGFEQIKVKIG------ 160
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYghANGRD-------IDELLDDVARHLELGYKAIRVQCGvpglkt 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 161 -----------------GTSFKEDV-------RHI----NALQHTAGSSITMILDANQSY---DAAAAFK-WERYfsewt 208
Cdd:PRK15072 158 tygvskgkglayepatkGLLPEEELwstekylRFVpklfEAVRNKFGFDLHLLHDVHHRLtpiEAARLGKsLEPY----- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337848 209 NIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYVPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRAS 288
Cdd:PRK15072 233 RLFWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTG 312
|
..
gi 489337848 289 AH 290
Cdd:PRK15072 313 SH 314
|
|
| |
