NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370473613|ref|XP_024306977|]
View 

mitochondrial enolase superfamily member 1 isoform X10 [Homo sapiens]

Protein Classification

enolase-like domain-containing protein( domain architecture ID 1750080)

enolase-like domain-containing protein is an enzyme 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

CATH:  3.20.20.120|3.30.390.10
Gene Ontology:  GO:0000287|GO:0003824
PubMed:  8987982|15581566

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
enolase_like super family cl40480
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 4-343 0e+00

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.


The actual alignment was detected with superfamily member cd03324:

Pssm-ID: 477366 [Multi-domain]  Cd Length: 415  Bit Score: 605.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   4 GRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAeDGIKGCGITFTLGKGTEV------------------- 64
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdles 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  65 ---DWSRKGRGAPGDS-----GrPKRGV-------------GLVGQAGGKACLEVTCG---------------------- 101
Cdd:cd03324    80 ivaDMGKFWRRLTSDSqlrwiG-PEKGVihlataavvnavwDLWAKAEGKPLWKLLVDmtpeelvscidfryitdaltpe 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 102 ---------------HEKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIG 166
Cdd:cd03324   159 ealeilrrgqpgkaaREADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 167 PEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKAL 246
Cdd:cd03324   239 PDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 247 QFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQ 326
Cdd:cd03324   319 DVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQ 398

                         410
                  ....*....|....*..
gi 1370473613 327 RASYMPPKDPGYSTEMK 343
Cdd:cd03324   399 NGAYMPPTDPGYSIEMK 415
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 4-343 0e+00

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: 605.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   4 GRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAeDGIKGCGITFTLGKGTEV------------------- 64
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdles 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  65 ---DWSRKGRGAPGDS-----GrPKRGV-------------GLVGQAGGKACLEVTCG---------------------- 101
Cdd:cd03324    80 ivaDMGKFWRRLTSDSqlrwiG-PEKGVihlataavvnavwDLWAKAEGKPLWKLLVDmtpeelvscidfryitdaltpe 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 102 ---------------HEKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIG 166
Cdd:cd03324   159 ealeilrrgqpgkaaREADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 167 PEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKAL 246
Cdd:cd03324   239 PDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 247 QFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQ 326
Cdd:cd03324   319 DVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQ 398

                         410
                  ....*....|....*..
gi 1370473613 327 RASYMPPKDPGYSTEMK 343
Cdd:cd03324   399 NGAYMPPTDPGYSIEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 5-350 2.81e-63

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: 205.83  E-value: 2.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   5 RISRLSVRDVRFPTSLGGHGAdaMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVDWSR---------KGRgapg 75
Cdd:COG4948     2 KITDIEVYPVRLPLKRPFTIS--RGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAAleealapllIGR---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  76 DSGRP-------KRGVGLVGQAggKACLEVTC----GHEK-----QMLAQGYPAYTTSCAWLGY-SDDTLKQLCAQALKD 138
Cdd:COG4948    74 DPLDIealwqrlYRALPGNPAA--KAAVDMALwdllGKALgvpvyQLLGGKVRDRVPVYATLGIdTPEEMAEEAREAVAR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 139 GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKA 217
Cdd:COG4948   152 GFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 218 lvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhlii 294
Cdd:COG4948   232 ---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---- 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 295 fdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKH 350
Cdd:COG4948   305 -----LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 126-346 1.10e-61

Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.


Pssm-ID: 463862 [Multi-domain]  Cd Length: 217  Bit Score: 197.02  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 126 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 204
Cdd:pfam13378   1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 205 PDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVG 284
Cdd:pfam13378  81 PDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473613 285 LcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 346
Cdd:pfam13378 158 I-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 125-218 1.05e-28

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: 106.98  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  125 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 203
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80

                           90
                   ....*....|....*
gi 1370473613  204 SPDDILGHATISKAL 218
Cdd:smart00922  81 PPDDLEGLAELRRAT 95
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 151-283 8.12e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 68.99  E-value: 8.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 151 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 230
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370473613 231 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 283
Cdd:PRK15440  270 EATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 4-343 0e+00

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: 605.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   4 GRISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAeDGIKGCGITFTLGKGTEV------------------- 64
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAMNPDPDYSAAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdles 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  65 ---DWSRKGRGAPGDS-----GrPKRGV-------------GLVGQAGGKACLEVTCG---------------------- 101
Cdd:cd03324    80 ivaDMGKFWRRLTSDSqlrwiG-PEKGVihlataavvnavwDLWAKAEGKPLWKLLVDmtpeelvscidfryitdaltpe 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 102 ---------------HEKQMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIG 166
Cdd:cd03324   159 ealeilrrgqpgkaaREADLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 167 PEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKAL 246
Cdd:cd03324   239 PDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 247 QFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQ 326
Cdd:cd03324   319 DVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQ 398

                         410
                  ....*....|....*..
gi 1370473613 327 RASYMPPKDPGYSTEMK 343
Cdd:cd03324   399 NGAYMPPTDPGYSIEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 5-350 2.81e-63

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: 205.83  E-value: 2.81e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   5 RISRLSVRDVRFPTSLGGHGAdaMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVDWSR---------KGRgapg 75
Cdd:COG4948     2 KITDIEVYPVRLPLKRPFTIS--RGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAAleealapllIGR---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  76 DSGRP-------KRGVGLVGQAggKACLEVTC----GHEK-----QMLAQGYPAYTTSCAWLGY-SDDTLKQLCAQALKD 138
Cdd:COG4948    74 DPLDIealwqrlYRALPGNPAA--KAAVDMALwdllGKALgvpvyQLLGGKVRDRVPVYATLGIdTPEEMAEEAREAVAR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 139 GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKA 217
Cdd:COG4948   152 GFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 218 lvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhlii 294
Cdd:COG4948   232 ---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---- 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 295 fdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKH 350
Cdd:COG4948   305 -----LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 126-346 1.10e-61

Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.


Pssm-ID: 463862 [Multi-domain]  Cd Length: 217  Bit Score: 197.02  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 126 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 204
Cdd:pfam13378   1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 205 PDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVG 284
Cdd:pfam13378  81 PDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473613 285 LcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 346
Cdd:pfam13378 158 I-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 5-341 4.53e-52

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: 176.65  E-value: 4.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   5 RISRLSVRDVRFPTSLGGHgadamhTDPDYSAAYVVIETDaeDGIKGCGITFTLGKG--------------------TEV 64
Cdd:cd03316     1 KITDVETFVLRVPLPEPGG------AVTWRNLVLVRVTTD--DGITGWGEAYPGGRPsavaaaiedllaplligrdpLDI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  65 D--WsRKGRGAPGDSGRpkRGVGLVGQAG---------GKAcLEVTCGhekQMLA----QGYPAYTTSCAWlGYSDDTLK 129
Cdd:cd03316    73 ErlW-EKLYRRLFWRGR--GGVAMAAISAvdialwdikGKA-AGVPVY---KLLGgkvrDRVRVYASGGGY-DDSPEELA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 130 QLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 203
Cdd:cd03316   145 EEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 204 SPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 283
Cdd:cd03316   225 PPDDLEGLARLRQA---TSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGG 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370473613 284 GLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVMIQRASYMPPKDPGYSTE 341
Cdd:cd03316   302 PIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPEIEDGYVTVPDRPGLGVE 357
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
 112-343 9.81e-31

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: 9.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 112 PAYTTScawLGYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPE 183
Cdd:cd03327   110 PAYASG---LYPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNY 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 184 AVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENL 263
Cdd:cd03327   187 AIKMARALEKYELRWIEEPLIPDDIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELK 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 264 SVLLMAKKFEIPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTE 341
Cdd:cd03327   264 KIAALAEAYGVPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGYFDLSDKPGFGLE 339


                  ..
gi 1370473613 342 MK 343
Cdd:cd03327   340 LN 341
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 125-218 1.05e-28

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: 106.98  E-value: 1.05e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  125 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 203
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80

                           90
                   ....*....|....*
gi 1370473613  204 SPDDILGHATISKAL 218
Cdd:smart00922  81 PPDDLEGLAELRRAT 95
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 131-292 4.97e-26

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: 103.95  E-value: 4.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 131 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 203
Cdd:cd00308    54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 204 SPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 283
Cdd:cd00308   130 APDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE 206

                         170
                  ....*....|.
gi 1370473613 284 G--LCELVQHL 292
Cdd:cd00308   207 SsiGTAAALHL 217
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
 112-279 9.28e-24

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: 100.56  E-value: 9.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 112 PAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKL 191
Cdd:cd03328   127 PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAF 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 192 AKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKK 271
Cdd:cd03328   206 ADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAA 284


                  ....*...
gi 1370473613 272 FEIPVCPH 279
Cdd:cd03328   285 HHVDLSAH 292
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
 134-351 4.30e-17

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: 81.37  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 134 QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 212
Cdd:cd03321   151 TAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 213 TISKAL-VPLGIgiatGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqh 291
Cdd:cd03321   231 RIASALrTPVQM----GENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH------------ 294

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473613 292 liIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 351
Cdd:cd03321   295 --LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
 134-292 2.19e-15

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: 75.07  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 134 QALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHAT 213
Cdd:cd03315    95 RALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAA 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 214 ISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV---CPHAGGVGLCELVq 290
Cdd:cd03315   175 LARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVmvgSMIESGLGTLANA- 250


                  ..
gi 1370473613 291 HL 292
Cdd:cd03315   251 HL 252
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
 116-276 3.16e-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: 74.60  E-value: 3.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 116 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 194
Cdd:cd03320    74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 195 KPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVNENLSV 265
Cdd:cd03320   154 RIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPRALLEL 219

                         170
                  ....*....|.
gi 1370473613 266 LLMAKKFEIPV 276
Cdd:cd03320   220 AEEARARGIPA 230
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 119-280 1.04e-13

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: 71.20  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 119 AWLG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWM 188
Cdd:cd03325   117 SWIGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 189 SKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLM 268
Cdd:cd03325   197 KELEPYRLLFIEEPVLPENVEALAEIAAR---TTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAM 273

                         170
                  ....*....|..
gi 1370473613 269 AKKFEIPVCPHA 280
Cdd:cd03325   274 AEAYDVALAPHC 285
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 151-283 8.12e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 68.99  E-value: 8.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 151 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 230
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370473613 231 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 283
Cdd:PRK15440  270 EATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
 139-229 1.01e-11

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239442 [Multi-domain]  Cd Length: 385  Bit Score: 65.49  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 139 GWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKA 217
Cdd:cd03326   175 GYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADH 254

                          90
                  ....*....|..
gi 1370473613 218 LVPlgiGIATGE 229
Cdd:cd03326   255 YDG---PIATGE 263
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 ...
 133-234 4.47e-11

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: 62.98  E-value: 4.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 133 AQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 212
Cdd:cd03319   143 KKAAKRGFPLLKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLA 221

                          90       100
                  ....*....|....*....|..
gi 1370473613 213 TISKAlvpLGIGIATGEQCHNR 234
Cdd:cd03319   222 YLRDK---SPLPIMADESCFSA 240
PRK14017 PRK14017
galactonate dehydratase; Provisional
 133-349 6.88e-11

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 62.99  E-value: 6.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 133 AQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP 202
Cdd:PRK14017  132 ARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 203 TSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV 276
Cdd:PRK14017  212 VLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVAL 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 277 CPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASYM-PPKDPGYSTEMK 343
Cdd:PRK14017  283 APHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGFVaIPTGPGLGIEID 353


                  ....*.
gi 1370473613 344 EESVKK 349
Cdd:PRK14017  354 EAKVRE 359
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
 142-221 1.75e-10

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: 61.56  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 142 RFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALV 219
Cdd:cd03318   161 RFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLrSRNRV 240


                  ..
gi 1370473613 220 PL 221
Cdd:cd03318   241 PI 242
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
 139-202 6.26e-08

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 53.82  E-value: 6.26e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473613 139 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 202
Cdd:PRK02901  102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
 157-359 4.98e-07

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: 50.90  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 157 RCQI------IRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGE 229
Cdd:cd03322   146 RVQLpklfeaVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 230 QCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYI 298
Cdd:cd03322   222 VFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYM 300

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370473613 299 SvsaslenrvceYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQY----------PDGEVWK 359
Cdd:cd03322   301 R-----------HAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
 125-349 5.84e-07

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: 50.70  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 125 DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEavewMSKLAKFKPLWIEE 201
Cdd:cd03317   139 EQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL----LKRLDEYGLLMIEQ 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 202 PTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCp 278
Cdd:cd03317   211 PLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVW- 283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370473613 279 HAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKDPGYSTEMKEESVKK 349
Cdd:cd03317   284 CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTGPGIGVTVDREALKK 354
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 131-209 2.15e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 49.86  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  131 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 207
Cdd:PLN02980  1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176


                   ..
gi 1370473613  208 IL 209
Cdd:PLN02980  1177 LI 1178
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
 6-283 2.95e-06

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: 48.55  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613   6 ISRLSVRDVRFPTSLGGHGADAMHTDPDYSAAYVVIETDAEDGIKGCGIT----------------FTLGKGT---EVDW 66
Cdd:cd03329     2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGHAFGgrpvtdpalvdrflkkVLIGQDPldrERLW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613  67 SRKGRGapgDSGRPKRGVGLVGQA----GGKAClevtcGHEKQMLAQGY----PAY-TTSCAWLGYSDDTLKQLC--AQA 135
Cdd:cd03329    82 QDLWRL---QRGLTDRGLGLVDIAlwdlAGKYL-----GLPVHRLLGGYrekiPAYaSTMVGDDLEGLESPEAYAdfAEE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 136 LKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 212
Cdd:cd03329   154 CKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYR 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370473613 213 TISKAL-VPLGIGIATGEQCHNRVIFkqlLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 283
Cdd:cd03329   234 WLAEKLdIPILGTEHSRGALESRADW---VLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNGA 302
PRK02714 PRK02714
o-succinylbenzoate synthase;
115-206 1.56e-04

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 43.08  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473613 115 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 193
Cdd:PRK02714  110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188

                          90
                  ....*....|....*.
gi 1370473613 194 FKPL---WIEEPTSPD 206
Cdd:PRK02714  189 RLSGkieFIEQPLPPD 204
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH