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Conserved domains on  [gi|1279761744|ref|XP_022933092|]
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L-Ala-D/L-amino acid epimerase isoform X1 [Cucurbita moschata]

Protein Classification

dipeptide epimerase( domain architecture ID 10129519)

dipeptide epimerase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
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 ...
71-396 1.88e-101

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: 304.50  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  71 RAESRALNVPLFEPFTIASSRLEMVENVAIRIELSnGCVGWGEAPILPFVTAEDQPTAITKAGEVGELLQQRPPcNLGSA 150
Cdd:cd03319     1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDP-RLEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGheFASVRAGVEMALIDAVANSINIPLWRLFGGVS-NSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK 229
Cdd:cd03319    79 LEALQELLPG--NGAARAAVDIALWDLEAKLLGLPLYQLWGGGApRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGKDLRADIEVLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLGIVsriaRDKYGVS 309
Cdd:cd03319   157 LGGDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGV--ELIEQPVPAGDDDGLAYL----RDKSPLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 310 VAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAglGCFKYI 388
Cdd:cd03319   231 IMADESCFSAADAARLAGGGAYDGINIKLMKTgGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAA--AKADFV 308

                  ....*...
gi 1279761744 389 DLDTPLLL 396
Cdd:cd03319   309 DLDGPLLL 316
 
Name Accession Description Interval E-value
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 ...
71-396 1.88e-101

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: 304.50  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  71 RAESRALNVPLFEPFTIASSRLEMVENVAIRIELSnGCVGWGEAPILPFVTAEDQPTAITKAGEVGELLQQRPPcNLGSA 150
Cdd:cd03319     1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDP-RLEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGheFASVRAGVEMALIDAVANSINIPLWRLFGGVS-NSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK 229
Cdd:cd03319    79 LEALQELLPG--NGAARAAVDIALWDLEAKLLGLPLYQLWGGGApRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGKDLRADIEVLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLGIVsriaRDKYGVS 309
Cdd:cd03319   157 LGGDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGV--ELIEQPVPAGDDDGLAYL----RDKSPLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 310 VAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAglGCFKYI 388
Cdd:cd03319   231 IMADESCFSAADAARLAGGGAYDGINIKLMKTgGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAA--AKADFV 308

                  ....*...
gi 1279761744 389 DLDTPLLL 396
Cdd:cd03319   309 DLDGPLLL 316
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
71-430 3.03e-83

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: 259.37  E-value: 3.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  71 RAESRALNVPLFEPFTIASSRLEMVENVAIRIELSNGCVGWGEAPILPfVTAEDQPTAITKAgeVGELLQQRPPCNLGSA 150
Cdd:COG4948     5 DIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGG-TGAEAVAAALEEA--LAPLLIGRDPLDIEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGHefASVRAGVEMALIDAVANSINIPLWRLFGG-VSNSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK 229
Cdd:COG4948    82 WQRLYRALPGN--PAAKAAVDMALWDLLGKALGVPVYQLLGGkVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGK-DLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVTptLFEQPVHRDNWEGLGIVsriaRDKYG 307
Cdd:COG4948   160 VGGpDPEEDVERVRAVReAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE--WIEQPLPAEDLEGLAEL----RRATP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 308 VSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLGCFK 386
Cdd:COG4948   234 VPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFD 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1279761744 387 YIDLDTPLLLSEDPVHGGYEVSGAVYKFTNARGHGGFLHWDNLA 430
Cdd:COG4948   314 IVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALA 357
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
211-421 8.50e-36

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: 131.15  E-value: 8.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 211 AAKLAAKYRDQGFKTLKLKVG-KDLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVH 288
Cdd:pfam13378   3 AAEARRAVEARGFRAFKLKVGgPDPEEDVERVRAVReAVGPGVDLMVDANGAWSVAEAIRLARALEELG--LLWIEEPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 289 RDNWEGLgivSRIARdKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMiE 367
Cdd:pfam13378  81 PDDLEGL---ARLRR-ATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVgGITEALKIAALAEAFGVPVAPHSG-G 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1279761744 368 TRLAMGFSGHLAAGLGCFKY-IDLDTPLLLSEDPVHGGYEVSGAVYKFTNARGHG 421
Cdd:pfam13378 156 GPIGLAASLHLAAAVPNLLIqEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLG 210
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
211-300 1.55e-20

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: 85.80  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  211 AAKLAAKYRDQGFKTLKLKVGKDLRADIEVLQRIRT-VHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHR 289
Cdd:smart00922   5 AEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREaVGPDADLMVDANGAWTAEEAIRALEALDELG--LEWIEEPVPP 82
                           90
                   ....*....|.
gi 1279761744  290 DNWEGLGIVSR 300
Cdd:smart00922  83 DDLEGLAELRR 93
PRK15129 PRK15129
L-Ala-D/L-Glu epimerase; Provisional
80-399 8.74e-16

L-Ala-D/L-Glu epimerase; Provisional


Pssm-ID: 185083 [Multi-domain]  Cd Length: 321  Bit Score: 77.87  E-value: 8.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  80 PLFEPFTIA-SSRLEmVENVAIRIElSNGCVGWGEAPILPFVTAED-----QPTAITKAGEVG---ELLQQRPPCnlGSA 150
Cdd:PRK15129   12 PLHTPFVIArGSRSE-ARVVVVELE-EEGIKGTGECTPYPRYGESDasvmaQIMSVVPQLEKGltrEALQKLLPA--GAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 mmqigetlpghefasvRAGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNA-AKLAAKYRDQGFKTLKLK 229
Cdd:PRK15129   88 ----------------RNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQmANSASALWQAGAKLLKVK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGKDLRAdiEVLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVTptLFEQPVHRDNWEGLgivsriARDKYGVS 309
Cdd:PRK15129  152 LDNHLIS--ERMVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVA--MLEQPLPAQDDAAL------ENFIHPLP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 310 VAADESCRSLSDVKRIVEEdlADVINIKLAKVGVL-GAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLgcfKYI 388
Cdd:PRK15129  222 ICADESCHTRSSLKALKGR--YEMVNIKLDKTGGLtEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQV---RFA 296
                         330
                  ....*....|.
gi 1279761744 389 DLDTPLLLSED 399
Cdd:PRK15129  297 DLDGPTWLAVD 307
menC_gamma/gm+ TIGR01927
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ...
78-382 3.46e-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: 72.92  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  78 NVPLFEPFTIASSRLEMVENVAIRIElSNGCVGWGEAPILPFVTAEDQPTAitkagevGELLQQRPPCNLGSAMMQIGET 157
Cdd:TIGR01927   4 QMPFDAPVVTRHGLLARREGLIVRLT-DEGRTGWGEIAPLPGFGTETLAEA-------LDFCRALIEEITRGDIEAIDDQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 158 LPghefaSVRAGVEMALidavansiniplWRLFGGVSNSITTDITIPITSASNAAKLAAKYRDQ-GFKTLKLKVGK-DLR 235
Cdd:TIGR01927  76 LP-----SVAFGFESAL------------IELESGDELPPASNYYVALLPAGDPALLLLRSAKAeGFRTFKWKVGVgELA 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 236 ADIEVL-QRIRTVHSDCEFILDANEGYDTEEAIQVLDKL-HELGVTPTLFEQPVHRDNweglgIVSRIARDkYGVSVAAD 313
Cdd:TIGR01927 139 REGMLVnLLLEALPDKAELRLDANGGLSPDEAQQFLKALdPNLRGRIAFLEEPLPDAD-----EMSAFSEA-TGTAIALD 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 314 ESCRSLSDVKRIVEEDLADVINIKLAKVGVLGAI-EIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGL 382
Cdd:TIGR01927 213 ESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLrDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKL 282
 
Name Accession Description Interval E-value
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 ...
71-396 1.88e-101

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: 304.50  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  71 RAESRALNVPLFEPFTIASSRLEMVENVAIRIELSnGCVGWGEAPILPFVTAEDQPTAITKAGEVGELLQQRPPcNLGSA 150
Cdd:cd03319     1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIELD-GITGYGEAAPTPRVTGETVESVLAALKSVRPALIGGDP-RLEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGheFASVRAGVEMALIDAVANSINIPLWRLFGGVS-NSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK 229
Cdd:cd03319    79 LEALQELLPG--NGAARAAVDIALWDLEAKLLGLPLYQLWGGGApRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGKDLRADIEVLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLGIVsriaRDKYGVS 309
Cdd:cd03319   157 LGGDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAVELLRELAELGV--ELIEQPVPAGDDDGLAYL----RDKSPLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 310 VAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAglGCFKYI 388
Cdd:cd03319   231 IMADESCFSAADAARLAGGGAYDGINIKLMKTgGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAA--AKADFV 308

                  ....*...
gi 1279761744 389 DLDTPLLL 396
Cdd:cd03319   309 DLDGPLLL 316
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
71-430 3.03e-83

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: 259.37  E-value: 3.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  71 RAESRALNVPLFEPFTIASSRLEMVENVAIRIELSNGCVGWGEAPILPfVTAEDQPTAITKAgeVGELLQQRPPCNLGSA 150
Cdd:COG4948     5 DIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGG-TGAEAVAAALEEA--LAPLLIGRDPLDIEAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGHefASVRAGVEMALIDAVANSINIPLWRLFGG-VSNSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK 229
Cdd:COG4948    82 WQRLYRALPGN--PAAKAAVDMALWDLLGKALGVPVYQLLGGkVRDRVPVYATLGIDTPEEMAEEAREAVARGFRALKLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGK-DLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVTptLFEQPVHRDNWEGLGIVsriaRDKYG 307
Cdd:COG4948   160 VGGpDPEEDVERVRAVReAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE--WIEQPLPAEDLEGLAEL----RRATP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 308 VSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLGCFK 386
Cdd:COG4948   234 VPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVgGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAALPNFD 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1279761744 387 YIDLDTPLLLSEDPVHGGYEVSGAVYKFTNARGHGGFLHWDNLA 430
Cdd:COG4948   314 IVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALA 357
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
72-380 1.96e-50

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: 171.37  E-value: 1.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  72 AESRALNVPLFEPFTIASSRLEMVENVAIRIELSNGCVGWGEAPilpfvtaedqptaitkagevgellqqrppcnlgsam 151
Cdd:cd03315     1 VEAIPVRLPLKRPLKWASGTLTTADHVLLRLHTDDGLVGWAEAT------------------------------------ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 152 mqigetlpghefasvRAGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNAAKLAAKYRDQGFKTLKLKVG 231
Cdd:cd03315    45 ---------------KAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVG 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 232 KDLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGlgivSRIARDKYGVSV 310
Cdd:cd03315   110 RDPARDVAVVAALReAVGDDAELRVDANRGWTPKQAIRALRALEDLGL--DYVEQPLPADDLEG----RAALARATDTPI 183
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1279761744 311 AADESCRSLSDVKRIVEEDLADVINIKLAKVGVL-GAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAA 380
Cdd:cd03315   184 MADESAFTPHDAFRELALGAADAVNIKTAKTGGLtKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAA 254
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
69-402 8.08e-41

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: 149.00  E-value: 8.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  69 VQRAESRALNVPLFEPFTIASSRLEMVENVAIRIELSNGCVGWGEA--PILPFVTAEdQPTAITKAGE--VGELLQQRPP 144
Cdd:cd03318     2 IEAIETTIVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEAttPGGPAWGGE-SPETIKAIIDryLAPLLIGRDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 145 CNLGSAMMQIGETLPGHEFAsvRAGVEMALIDAVANSINIPLWRLFGG-VSNSITTDITIPITSASNAAKLAAKYRDQG- 222
Cdd:cd03318    81 TNIGAAMALLDRAVAGNLFA--KAAIEMALLDAQGRRLGLPVSELLGGrVRDSLPVAWTLASGDTERDIAEAEEMLEAGr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 223 FKTLKLKVGK-DLRADIE-VLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLgivSR 300
Cdd:cd03318   159 HRRFKLKMGArPPADDLAhVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGV--ELIEQPVPRENLDGL---AR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 301 IaRDKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLA 379
Cdd:cd03318   234 L-RSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSgGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLF 312
                         330       340
                  ....*....|....*....|....
gi 1279761744 380 AGLGCFKY-IDLDTPLLLSEDPVH 402
Cdd:cd03318   313 ATLPSLPFgCELFGPLLLAEDLLE 336
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
73-421 3.79e-36

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: 135.82  E-value: 3.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  73 ESRALNVPLFEPFTIASSRlemvENVAIRIELSNGCVGWGEAPILPFVTAedQPTAITKagEVGELLQQRPPCNLGS--A 150
Cdd:cd03316     6 ETFVLRVPLPEPGGAVTWR----NLVLVRVTTDDGITGWGEAYPGGRPSA--VAAAIED--LLAPLLIGRDPLDIERlwE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 MMQIGETLPGHEFASVRA--GVEMALIDAVANSINIPLWRLFGGVSNSIT---TDITIPITSASNAAKLAAKYRDQGFKT 225
Cdd:cd03316    78 KLYRRLFWRGRGGVAMAAisAVDIALWDIKGKAAGVPVYKLLGGKVRDRVrvyASGGGYDDSPEELAEEAKRAVAEGFTA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 226 LKLKVG------KDLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHRDNWEGLGIV 298
Cdd:cd03316   158 VKLKVGgpdsggEDLREDLARVRAVReAVGPDVDLMVDANGRWDLAEAIRLARALEEYD--LFWFEEPVPPDDLEGLARL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 299 sriaRDKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMiETRLAMGFSGH 377
Cdd:cd03316   236 ----RQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVgGITEAKKIAALAEAHGVRVAPHGA-GGPIGLAASLH 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1279761744 378 LAAGLGCFKYIDLDTPLL-LSEDPVHGGYEVSGAVYKFTNARGHG 421
Cdd:cd03316   311 LAAALPNFGILEYHLDDLpLREDLFKNPPEIEDGYVTVPDRPGLG 355
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
211-421 8.50e-36

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: 131.15  E-value: 8.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 211 AAKLAAKYRDQGFKTLKLKVG-KDLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVH 288
Cdd:pfam13378   3 AAEARRAVEARGFRAFKLKVGgPDPEEDVERVRAVReAVGPGVDLMVDANGAWSVAEAIRLARALEELG--LLWIEEPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 289 RDNWEGLgivSRIARdKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLMIGGMiE 367
Cdd:pfam13378  81 PDDLEGL---ARLRR-ATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVgGITEALKIAALAEAFGVPVAPHSG-G 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1279761744 368 TRLAMGFSGHLAAGLGCFKY-IDLDTPLLLSEDPVHGGYEVSGAVYKFTNARGHG 421
Cdd:pfam13378 156 GPIGLAASLHLAAAVPNLLIqEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLG 210
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
72-380 2.87e-35

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: 133.51  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  72 AESRALNVPLFEPFTIASSRLEMVENVAIRIELSNGCVGWGEAP--ILPFVTAEDQPTA----------------ITKAG 133
Cdd:cd03317     1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVafEGPFYTEETNATAwhilkdyllplllgreFSHPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 134 EVGELLQQrppcnlgsammqigetLPGHEFAsvRAGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNA-A 212
Cdd:cd03317    81 EVSERLAP----------------IKGNNMA--KAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQDDVEQlL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 213 KLAAKYRDQGFKTLKLKV--GKdlraDIEVLQRIRTVHSDCEFILDANEGYdTEEAIQVLDKLHELGVtpTLFEQPVHRD 290
Cdd:cd03317   143 KQIERYLEEGYKRIKLKIkpGW----DVEPLKAVRERFPDIPLMADANSAY-TLADIPLLKRLDEYGL--LMIEQPLAAD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 291 NWEGLGIVSRIARdkygVSVAADESCRSLSDVKRIVEEDLADVINIKLAKVGVLG-AIEIIEVARAAGLSLMIGGMIETR 369
Cdd:cd03317   216 DLIDHAELQKLLK----TPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTeALKIHDLCQEHGIPVWCGGMLESG 291
                         330
                  ....*....|.
gi 1279761744 370 LAMGFSGHLAA 380
Cdd:cd03317   292 IGRAHNVALAS 302
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
160-383 6.97e-30

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: 115.50  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 160 GHEF-ASVRAGVEMALIDAVANSINIPLWRLFGGvsnsittditipitsaSNAAKLAAKYRDQGFKTLKLKVGKDLRadi 238
Cdd:cd00308    36 GVVGwGEVISGIDMALWDLAAKALGVPLAELLGG----------------GSRDRVPAYGSIERVRAVREAFGPDAR--- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 239 evlqrirtvhsdceFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHRDNWEGLGIVsriaRDKYGVSVAADESCRS 318
Cdd:cd00308    97 --------------LAVDANGAWTPKEAIRLIRALEKYG--LAWIEEPCAPDDLEGYAAL----RRRTGIPIAADESVTT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1279761744 319 LSDVKRIVEEDLADVINIKLAKVG-VLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLG 383
Cdd:cd00308   157 VDDALEALELGAVDILQIKPTRVGgLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALP 222
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
162-383 9.93e-24

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: 99.64  E-value: 9.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 162 EFA--SVRAGVEMALIDAVANSINIPLWR--------LFGGvsnsittditipitsASNAAKLAAKYRDQGFKTLKLKVG 231
Cdd:cd03320    42 EIAplPLAFGIESALANLEALLVGFTRPRnripvnalLPAG---------------DAAALGEAKAAYGGGYRTVKLKVG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 232 K-DLRADIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVTptLFEQPVHRDNWEGLgivsriARDKYGVS 309
Cdd:cd03320   107 AtSFEEDLARLRALReALPADAKLRLDANGGWSLEEALAFLEALAAGRIE--YIEQPLPPDDLAEL------RRLAAGVP 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1279761744 310 VAADESCRSLSDVKRIVEEDLADVINIKLAKVG-VLGAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLG 383
Cdd:cd03320   179 IALDESLRRLDDPLALAAAGALGALVLKPALLGgPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALP 253
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
211-300 1.55e-20

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: 85.80  E-value: 1.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  211 AAKLAAKYRDQGFKTLKLKVGKDLRADIEVLQRIRT-VHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHR 289
Cdd:smart00922   5 AEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREaVGPDADLMVDANGAWTAEEAIRALEALDELG--LEWIEEPVPP 82
                           90
                   ....*....|.
gi 1279761744  290 DNWEGLGIVSR 300
Cdd:smart00922  83 DDLEGLAELRR 93
PRK15129 PRK15129
L-Ala-D/L-Glu epimerase; Provisional
80-399 8.74e-16

L-Ala-D/L-Glu epimerase; Provisional


Pssm-ID: 185083 [Multi-domain]  Cd Length: 321  Bit Score: 77.87  E-value: 8.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  80 PLFEPFTIA-SSRLEmVENVAIRIElSNGCVGWGEAPILPFVTAED-----QPTAITKAGEVG---ELLQQRPPCnlGSA 150
Cdd:PRK15129   12 PLHTPFVIArGSRSE-ARVVVVELE-EEGIKGTGECTPYPRYGESDasvmaQIMSVVPQLEKGltrEALQKLLPA--GAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 151 mmqigetlpghefasvRAGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNA-AKLAAKYRDQGFKTLKLK 229
Cdd:PRK15129   88 ----------------RNAVDCALWDLAARQQQQSLAQLIGITLPETVTTAQTVVIGTPEQmANSASALWQAGAKLLKVK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 230 VGKDLRAdiEVLQRIRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVTptLFEQPVHRDNWEGLgivsriARDKYGVS 309
Cdd:PRK15129  152 LDNHLIS--ERMVAIRSAVPDATLIVDANESWRAEGLAARCQLLADLGVA--MLEQPLPAQDDAAL------ENFIHPLP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 310 VAADESCRSLSDVKRIVEEdlADVINIKLAKVGVL-GAIEIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGLgcfKYI 388
Cdd:PRK15129  222 ICADESCHTRSSLKALKGR--YEMVNIKLDKTGGLtEALALATEARAQGFALMLGCMLCTSRAISAALPLVPQV---RFA 296
                         330
                  ....*....|.
gi 1279761744 389 DLDTPLLLSED 399
Cdd:PRK15129  297 DLDGPTWLAVD 307
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
170-360 8.38e-15

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: 75.14  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 170 VEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNAAkLAAK---YRDQGFKTLKLKVGKDLRADIEVLQRIRT 246
Cdd:cd03328    99 VDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTSYDDDR-LREQlsgWVAQGIPRVKMKIGRDPRRDPDRVAAARR 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 247 -VHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLGIVSriARDKYGVSVAADESCRSLSDVKRI 325
Cdd:cd03328   178 aIGPDAELFVDANGAYSRKQALALARAFADEGV--TWFEEPVSSDDLAGLRLVR--ERGPAGMDIAAGEYAYTLAYFRRL 253
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1279761744 326 VEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSL 360
Cdd:cd03328   254 LEAHAVDVLQADVTRCgGVTGFLQAAALAAAHHVDL 289
menC_gamma/gm+ TIGR01927
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ...
78-382 3.46e-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: 72.92  E-value: 3.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  78 NVPLFEPFTIASSRLEMVENVAIRIElSNGCVGWGEAPILPFVTAEDQPTAitkagevGELLQQRPPCNLGSAMMQIGET 157
Cdd:TIGR01927   4 QMPFDAPVVTRHGLLARREGLIVRLT-DEGRTGWGEIAPLPGFGTETLAEA-------LDFCRALIEEITRGDIEAIDDQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 158 LPghefaSVRAGVEMALidavansiniplWRLFGGVSNSITTDITIPITSASNAAKLAAKYRDQ-GFKTLKLKVGK-DLR 235
Cdd:TIGR01927  76 LP-----SVAFGFESAL------------IELESGDELPPASNYYVALLPAGDPALLLLRSAKAeGFRTFKWKVGVgELA 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 236 ADIEVL-QRIRTVHSDCEFILDANEGYDTEEAIQVLDKL-HELGVTPTLFEQPVHRDNweglgIVSRIARDkYGVSVAAD 313
Cdd:TIGR01927 139 REGMLVnLLLEALPDKAELRLDANGGLSPDEAQQFLKALdPNLRGRIAFLEEPLPDAD-----EMSAFSEA-TGTAIALD 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 314 ESCRSLSDVKRIVEEDLADVINIKLAKVGVLGAI-EIIEVARAAGLSLMIGGMIETRLAMGFSGHLAAGL 382
Cdd:TIGR01927 213 ESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLrDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKL 282
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
212-352 8.40e-14

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: 72.76  E-value: 8.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 212 AKLAAKYRDQGFKTLKLKVGKDLRADIEVLQRIRTV-HSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHRD 290
Cdd:cd03324   201 RRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREViGPDNKLMIDANQRWDVPEAIEWVKQLAEFK--PWWIEEPTSPD 278
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1279761744 291 NWEGLGIVSRiARDKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKVGvlGAIEIIEV 352
Cdd:cd03324   279 DILGHAAIRK-ALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLG--GVNENLAV 337
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
207-382 1.75e-13

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 71.15  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 207 SASNAAKLAAkyRDQGFKTLKLKV---GKDLRADIEvlqRIRTVHsdcEFI-------LDANEGYDTEEAIQVLDKLHEL 276
Cdd:PRK02901   89 DAAQVPEVLA--RFPGCRTAKVKVaepGQTLADDVA---RVNAVR---DALgpdgrvrVDANGGWSVDEAVAAARALDAD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 277 GVTPTLfEQPVhrdnweglGIVSRIA--RDKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKVGvlGAIEIIEVAR 354
Cdd:PRK02901  161 GPLEYV-EQPC--------ATVEELAelRRRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLG--GVRAALDIAE 229
                         170       180
                  ....*....|....*....|....*...
gi 1279761744 355 AAGLSLMIGGMIETRLAMGFSGHLAAGL 382
Cdd:PRK02901  230 QIGLPVVVSSALDTSVGIAAGLALAAAL 257
PRK02714 PRK02714
o-succinylbenzoate synthase;
80-342 4.62e-13

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 69.66  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  80 PLFEPFTIASSRLEMVENVAIRIELSNGCVGWGE-APIlPFVTAEDQPTAITkagevgeLLQQRPPcNLGSA-MMQIGET 157
Cdd:PRK02714   13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEiAPL-PWFGSETLEEALA-------FCQQLPG-EITPEqIFSIPDA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 158 LPGHEFasvraGVEMALidavansinipLWRLFGGVSNSITTDITIPITSASNAAKLA-AKYRDQGFKTLKLKVGKD-LR 235
Cdd:PRK02714   84 LPACQF-----GFESAL-----------ENESGSRSNVTLNPLSYSALLPAGEAALQQwQTLWQQGYRTFKWKIGVDpLE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 236 ADIEVLQR-IRTVHSDCEFILDANEGYDTEEA---IQVLDKLHELGVtpTLFEQPVHRDNWEGLgivSRIARDkYGVSVA 311
Cdd:PRK02714  148 QELKIFEQlLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKI--EFIEQPLPPDQFDEM---LQLSQD-YQTPIA 221
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1279761744 312 ADESCRSLSDVKRIVEEDLADVINIKLAKVG 342
Cdd:PRK02714  222 LDESVANLAQLQQCYQQGWRGIFVIKPAIAG 252
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
168-411 6.37e-12

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: 66.35  E-value: 6.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 168 AGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSASNAAKLAAKYRDQGFKTLKLKVGK-DLRADIEVLQRIR- 245
Cdd:cd03321   102 AGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIGYpTADEDLAVVRSIRq 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 246 TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEGLGIVSRIARdkygVSVAADESCRSLSDVKRI 325
Cdd:cd03321   182 AVGDGVGLMVDYNQSLTVPEAIERGQALDQEGL--TWIEEPTLQHDYEGHARIASALR----TPVQMGENWLGPEEMFKA 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 326 VEEDLADVINIKLAKV-GVLGAIEIIEVARAAGLSLmiggmiETRLAMGFSGHLAAGLGC---FKYIDLDTPLLLSEDPV 401
Cdd:cd03321   256 LSAGACDLVMPDLMKIgGVTGWLRASALAEQAGIPM------SSHLFQEISAHLLAVTPTahwLEYVDWAGAILEPPLKF 329
                         250
                  ....*....|
gi 1279761744 402 HGGYEVSGAV 411
Cdd:cd03321   330 EDGNAVIPDE 339
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
98-356 2.79e-11

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: 64.65  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  98 VAIRIELSNGCVGWGEApilpfvTAEDQPTAITKA-GEVGELLQQRPPCN---LGSAMMQIGETLPGHEFASVRAGVEMA 173
Cdd:cd03325    15 LFVKIETDEGVVGWGEP------TVEGKARTVEAAvQELEDYLIGKDPMNiehHWQVMYRGGFYRGGPVLMSAISGIDQA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 174 LIDAVANSINIPLWRLFGG-VSNSITTDITIPITSASNAAKLAAKYRDQGFKTLK---------LKVGKDLRADIEVLQR 243
Cdd:cd03325    89 LWDIKGKVLGVPVHQLLGGqVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 244 IR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGvtPTLFEQPVHRDNWEGLGivsRIARdKYGVSVAADESCRSLSDV 322
Cdd:cd03325   169 LReAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYR--LLFIEEPVLPENVEALA---EIAA-RTTIPIATGERLFSRWDF 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1279761744 323 KRIVEEDLADVINIKLAKVGvlGAIEIIEVARAA 356
Cdd:cd03325   243 KELLEDGAVDIIQPDISHAG--GITELKKIAAMA 274
MR_MLE_N pfam02746
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ...
75-191 2.10e-07

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: 49.39  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  75 RALNVPLfEPFTIASSRLEMVENVAIRIELSNGCVGWGEAPILPfvtaedqPTAITKAGE----VGELLQQRPPCNLGSA 150
Cdd:pfam02746   7 VDVGWPL-RPIQMAFGTVQQQSLVIVRIETSEGVVGIGEATSYG-------GRAETIKAIlddhLAPLLIGRDAANISDL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1279761744 151 MMQIGETLPGHEFAsvRAGVEMALIDAVANSINIPLWRLFG 191
Cdd:pfam02746  79 WQLMYRAALGNMSA--KAAIDMALWDLKAKVLNLPLADLLG 117
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
79-268 7.70e-06

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 48.31  E-value: 7.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744   79 VPLFEPFTIASSRLEMV--ENVAIRIELSNGCVGWGE-API----LPFVTAEDQPTAITKAGEvGELLQQRPPCNLGSAM 151
Cdd:PLN02980   943 IQLCAPPTSASVDFSQFhrEGFILSLSLEDGSVGFGEvAPLeiheEDLLDVEEQLRFLLHVIK-GAKISFMLPLLKGSFS 1021
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744  152 MQIGETL---PGHEFASVRAGVEMALIDAVANSINIPLWRL---FGGVSNSITTDITI-------PITSASNAAKLAAKY 218
Cdd:PLN02980  1022 SWIWSELgipPSSIFPSVRCGLEMAILNAIAVRHGSSLLNIldpYQKDENGSEQSHSVqicalldSNGSPLEVAYVARKL 1101
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1279761744  219 RDQGFKTLKLKVGKDLRA--DIEVLQRIR-TVHSDCEFILDANEGYDTEEAIQ 268
Cdd:PLN02980  1102 VEEGFSAIKLKVGRRVSPiqDAAVIQEVRkAVGYQIELRADANRNWTYEEAIE 1154
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
150-394 4.49e-05

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: 45.46  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 150 AMMQiGETLPGHEFASVRAG-VEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSA-------SNAAKLAAKYR-- 219
Cdd:cd03326    93 AMMR-NEKPGGHGERAVAVGaLDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAAggyyypgDDLGRLRDEMRry 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 220 -DQGFKTLKLKVG-KDLRADIEVLQR-IRTVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQPVHRDNWEglg 296
Cdd:cd03326   172 lDRGYTVVKIKIGgAPLDEDLRRIEAaLDVLGDGARLAVDANGRFDLETAIAYAKALAPYGL--RWYEEPGDPLDYA--- 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 297 iVSRIARDKYGVSVAADESCRSLSDVKRIV-------EEDLAdVINIKLAkVGVLGAIEIIEVARAAGLSLMI----GGM 365
Cdd:cd03326   247 -LQAELADHYDGPIATGENLFSLQDARNLLryggmrpDRDVL-QFDPGLS-YGLPEYLRMLDVLEAHGWSRRRffphGGH 323
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1279761744 366 IetrlamgFSGHLAAGL---GCFKYIDLDTPL 394
Cdd:cd03326   324 L-------MSLHIAAGLglgGNESYPDVFQPF 348
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
168-342 7.73e-04

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: 41.27  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 168 AGVEMALIDAVANSINIPLWRLFGGVSNSITTDITIPITSA-SNAAKLAAKYRDQGFKTLKLKVGKDLRAdievlqrIRT 246
Cdd:cd03322    86 AAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDiPELLEAVERHLAQGYRAIRVQLPKLFEA-------VRE 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 247 VHSDCEFIL-DANEGYDTEEAIQVLDKLHELgvTPTLFEQPVHRDNWEGLgivsRIARDKYGVSVAADESCRSLSDVKRI 325
Cdd:cd03322   159 KFGFEFHLLhDVHHRLTPNQAARFGKDVEPY--RLFWMEDPTPAENQEAF----RLIRQHTATPLAVGEVFNSIWDWQNL 232
                         170
                  ....*....|....*..
gi 1279761744 326 VEEDLADVINIKLAKVG 342
Cdd:cd03322   233 IQERLIDYIRTTVSHAG 249
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
170-286 3.21e-03

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: 39.69  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 170 VEMALIDAVANSINIPLWRLFGG-------VSNSITTDITIPITSASNAAKLAAKYRDQGFKTLKLK--VGKDLRADIEV 240
Cdd:cd03329    99 VDIALWDLAGKYLGLPVHRLLGGyrekipaYASTMVGDDLEGLESPEAYADFAEECKALGYRAIKLHpwGPGVVRRDLKA 178
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1279761744 241 LQRIR-TVHSDCEFILDANEGYDTEEAIQVLDKLHELGVtpTLFEQP 286
Cdd:cd03329   179 CLAVReAVGPDMRLMHDGAHWYSRADALRLGRALEELGF--FWYEDP 223
MAL cd03314
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ...
280-364 5.67e-03

Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL 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: 239430 [Multi-domain]  Cd Length: 369  Bit Score: 38.53  E-value: 5.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1279761744 280 PTLFEQPVHRDNWEG----LG-IVSRIARDKYGVSVAADESCRSLSDVKRIVEEDLADVINIKLAKVG-VLGAIEIIEVA 353
Cdd:cd03314   229 PLRIEGPMDAGSREAqierMAaLRAELDRRGVGVRIVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGgIDNTIDAVLYC 308
                          90
                  ....*....|.
gi 1279761744 354 RAAGLSLMIGG 364
Cdd:cd03314   309 KEHGVGAYLGG 319
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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