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Conserved domains on  [gi|1370473615|ref|XP_024306978|]
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mitochondrial enolase superfamily member 1 isoform X11 [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

Gene Ontology:  GO:0000287|GO:0003824
PubMed:  8987982|15581566

Graphical summary

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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 ...
19-342 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: 681.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRW 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKL-----MIDANQRW 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 179 DVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSV 258
Cdd:cd03324   252 DVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGV 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 259 NENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYS 338
Cdd:cd03324   332 NENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYS 411

                  ....
gi 1370473615 339 TEMK 342
Cdd:cd03324   412 IEMK 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 ...
19-342 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: 681.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRW 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKL-----MIDANQRW 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 179 DVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSV 258
Cdd:cd03324   252 DVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGV 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 259 NENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYS 338
Cdd:cd03324   332 NENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYS 411

                  ....
gi 1370473615 339 TEMK 342
Cdd:cd03324   412 IEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
14-349 6.02e-66

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: 212.76  E-value: 6.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  14 LWEKALKLIGpekgVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGK 93
Cdd:COG4948    81 LWQRLYRALP----GNPAAKAAVDMALWDLLGKALGVPVYQLL-----------------------------------GG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  94 KEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqM 171
Cdd:COG4948   122 KVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARL-----R 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 172 MDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQID 251
Cdd:COG4948   187 VDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 252 SCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMI 324
Cdd:COG4948   264 LSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRI 334
                         330       340
                  ....*....|....*....|....*
gi 1370473615 325 QRASYMPPKDPGYSTEMKEESVKKH 349
Cdd:COG4948   335 EDGYLTVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
122-345 4.56e-60

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: 192.78  E-value: 4.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 122 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIE 199
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDL-----MVDANGAWSVAEAIRLARALEELGLLWIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 200 EPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHA 279
Cdd:pfam13378  77 EPVPPDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370473615 280 GGVGLcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 345
Cdd:pfam13378 154 GGGPI-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
119-217 9.35e-26

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: 99.28  E-value: 9.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  119 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLW 197
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADL-----MVDANGAWTAEEAIRALEALDELGLEW 75
                           90       100
                   ....*....|....*....|
gi 1370473615  198 IEEPTSPDDILGHATISKAL 217
Cdd:smart00922  76 IEEPVPPDDLEGLAELRRAT 95
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
145-282 7.48e-12

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 65.91  E-value: 7.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 145 LQDDMRRCQIIRDMIGPEktlslFLQMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGI 224
Cdd:PRK15440  191 LRKNAAMVADMREKVGDD-----FWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMV 264
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473615 225 ATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 282
Cdd:PRK15440  265 TSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 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 ...
19-342 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: 681.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRW 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKL-----MIDANQRW 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 179 DVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSV 258
Cdd:cd03324   252 DVPEAIEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGV 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 259 NENLSVLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYS 338
Cdd:cd03324   332 NENLAVLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYS 411

                  ....
gi 1370473615 339 TEMK 342
Cdd:cd03324   412 IEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
14-349 6.02e-66

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: 212.76  E-value: 6.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  14 LWEKALKLIGpekgVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGK 93
Cdd:COG4948    81 LWQRLYRALP----GNPAAKAAVDMALWDLLGKALGVPVYQLL-----------------------------------GG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  94 KEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqM 171
Cdd:COG4948   122 KVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARL-----R 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 172 MDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQID 251
Cdd:COG4948   187 VDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 252 SCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMI 324
Cdd:COG4948   264 LSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRI 334
                         330       340
                  ....*....|....*....|....*
gi 1370473615 325 QRASYMPPKDPGYSTEMKEESVKKH 349
Cdd:COG4948   335 EDGYLTVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
122-345 4.56e-60

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: 192.78  E-value: 4.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 122 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIE 199
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDL-----MVDANGAWSVAEAIRLARALEELGLLWIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 200 EPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHA 279
Cdd:pfam13378  77 EPVPPDDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370473615 280 GGVGLcELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 345
Cdd:pfam13378 154 GGGPI-GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
13-340 2.73e-59

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: 195.52  E-value: 2.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  13 SLWEKALK--LIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgq 90
Cdd:cd03316    74 RLWEKLYRrlFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLL---------------------------------- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  91 iGKKEREKqmlaqgYPAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKT 164
Cdd:cd03316   120 -GGKVRDR------VRVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVD 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 165 LslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALvplGIGIATGEQCHNRVIFKQLLQAKA 244
Cdd:cd03316   192 L-----MVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQAT---SVPIAAGENLYTRWEFRDLLEAGA 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 245 LQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----F 318
Cdd:cd03316   264 VDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlF 335
                         330       340
                  ....*....|....*....|..
gi 1370473615 319 KYPVMIQRASYMPPKDPGYSTE 340
Cdd:cd03316   336 KNPPEIEDGYVTVPDRPGLGVE 357
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
14-342 6.28e-34

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: 128.22  E-value: 6.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  14 LWEKALKLIGP--EKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqi 91
Cdd:cd03327    57 LWDQMYRATLAygRKGIAMAAISAVDLALWDLLGKIRGEPVYKLL----------------------------------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  92 GKKEREKqmlaqgYPAYTTScawLGYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEK 163
Cdd:cd03327   102 GGRTRDK------IPAYASG---LYPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 164 TLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAK 243
Cdd:cd03327   173 DL-----MLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGR 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 244 ALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYP 321
Cdd:cd03327   245 AVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNE 320
                         330       340
                  ....*....|....*....|.
gi 1370473615 322 VMIQRASYMPPKDPGYSTEMK 342
Cdd:cd03327   321 PVPVNGYFDLSDKPGFGLELN 341
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
12-278 3.88e-26

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: 107.11  E-value: 3.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  12 PSLWE---KALKLIGPEkGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMlvscidfryitdvlteedaleilqk 88
Cdd:cd03328    73 PAAWEamqRAVRNAGRP-GVAAMAISAVDIALWDLKARLLGLPLARLLGRAHDSV------------------------- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  89 gqigkkerekqmlaqgyPAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslf 168
Cdd:cd03328   127 -----------------PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAEL--- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 169 lqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFL 248
Cdd:cd03328   186 --FVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVL 262
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370473615 249 QIDSCRLGSVNENLSVLLMAKKFEIPVCPH 278
Cdd:cd03328   263 QADVTRCGGVTGFLQAAALAAAHHVDLSAH 292
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
119-217 9.35e-26

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: 99.28  E-value: 9.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  119 DDTLKQLCAQALKD-GWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLW 197
Cdd:smart00922   1 PEELAEAARRAVAEaGFRAVKVKVGGGPLEDLARVAAVREAVGPDADL-----MVDANGAWTAEEAIRALEALDELGLEW 75
                           90       100
                   ....*....|....*....|
gi 1370473615  198 IEEPTSPDDILGHATISKAL 217
Cdd:smart00922  76 IEEPVPPDDLEGLAELRRAT 95
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
125-291 8.19e-25

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: 100.86  E-value: 8.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 125 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMSKLAKFKPLW 197
Cdd:cd00308    54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAV-----DANGAWTPKEAIRLIRALEKYGLAW 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 198 IEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 277
Cdd:cd00308   125 IEEPCAPDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMV 201
                         170
                  ....*....|....*.
gi 1370473615 278 HAGGVG--LCELVQHL 291
Cdd:cd00308   202 HGTLESsiGTAAALHL 217
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
27-291 6.04e-16

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: 77.00  E-value: 6.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  27 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfrYITDVLTEEDALEilqkgqigkkerekqmlaqgyp 106
Cdd:cd03315    39 GWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVA-----HMLGLGEPAEVAE---------------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 107 ayttscawlgysddtlkqLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEktLSLFLqmmDANQRWDVPEAVEW 186
Cdd:cd03315    92 ------------------EARRALEAGFRTFKLKVGRDPARDVAVVAALREAVGDD--AELRV---DANRGWTPKQAIRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 187 MSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLL 266
Cdd:cd03315   149 LRALEDLGLDYVEQPLPADDLEGRAALARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLA 225
                         250       260
                  ....*....|....*....|....*...
gi 1370473615 267 MAKKFEIPV---CPHAGGVGLCELVqHL 291
Cdd:cd03315   226 VAEALGLPVmvgSMIESGLGTLANA-HL 252
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
27-284 1.23e-15

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: 76.98  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  27 GVVHL-ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlAQGY 105
Cdd:cd03325    75 GPVLMsAISGIDQALWDIKGKVLGVPVHQLL-----------------------------------GGQVRDR---VRVY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 106 payttscAWLG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEktlslFLQMMDAN 175
Cdd:cd03325   117 -------SWIGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPD-----IDIGVDFH 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 176 QRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKALvplGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRL 255
Cdd:cd03325   185 GRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAART---TIPIATGERLFSRWDFKELLEDGAVDIIQPDISHA 261
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370473615 256 GSVNENLSVLLMAKKFEIPVCPHA--GGVGL 284
Cdd:cd03325   262 GGITELKKIAAMAEAYDVALAPHCplGPIAL 292
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
128-350 5.67e-15

Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239437 [Multi-domain]  Cd Length: 355  Bit Score: 75.21  E-value: 5.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 128 QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDD 206
Cdd:cd03321   151 TAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGL-----MVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHD 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 207 ILGHATISKAL-VPLGIgiatGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglc 285
Cdd:cd03321   226 YEGHARIASALrTPVQM----GENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH------- 294
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473615 286 elvqhliIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 350
Cdd:cd03321   295 -------LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
110-275 1.70e-13

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: 69.60  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 110 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWMS 188
Cdd:cd03320    74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRL-----DANGGWSLEEALAFLE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 189 KLAKFKPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVN 259
Cdd:cd03320   149 ALAAGRIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPR 214
                         170
                  ....*....|....*.
gi 1370473615 260 ENLSVLLMAKKFEIPV 275
Cdd:cd03320   215 ALLELAEEARARGIPA 230
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 ...
32-233 6.42e-13

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: 68.75  E-value: 6.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  32 ATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIdfryiTDVLTEEDALeilqkgqigkKEREKQMLAQGYPAytts 111
Cdd:cd03319    92 ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDY-----TISIDTPEAM----------AAAAKKAAKRGFPL---- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 112 cawlgysddtlkqlcaqalkdgwtrFKVKVGADLQDDMRRCQIIRDMIgPEKTLSLflqmmDANQRWDVPEAVEWMSKLA 191
Cdd:cd03319   153 -------------------------LKIKLGGDLEDDIERIRAIREAA-PDARLRV-----DANQGWTPEEAVELLRELA 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370473615 192 KFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNR 233
Cdd:cd03319   202 ELGVELIEQPVPAGDDDGLAYLRDK---SPLPIMADESCFSA 240
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
32-228 9.85e-13

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: 68.57  E-value: 9.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  32 ATAAVLNAVWDLWAKQEGKPVWKLLVDmdprmlvscidfRYitdvlteedaleilqkGQIGKKEREKQMLAQGYPaytts 111
Cdd:cd03326   109 AVGALDMAVWDAVAKIAGLPLYRLLAR------------RY----------------GRGQADPRVPVYAAGGYY----- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 112 cawlgYSDDTLKQLCAQA---LKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWM 187
Cdd:cd03326   156 -----YPGDDLGRLRDEMrryLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAV-----DANGRFDLETAIAYA 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370473615 188 SKLAKFKPLWIEEPTSPDDILGHATISKALVPlgiGIATGE 228
Cdd:cd03326   226 KALAPYGLRWYEEPGDPLDYALQAELADHYDG---PIATGE 263
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
145-282 7.48e-12

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 65.91  E-value: 7.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 145 LQDDMRRCQIIRDMIGPEktlslFLQMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGI 224
Cdd:PRK15440  191 LRKNAAMVADMREKVGDD-----FWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMV 264
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370473615 225 ATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 282
Cdd:PRK15440  265 TSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
PRK14017 PRK14017
galactonate dehydratase; Provisional
32-348 7.15e-10

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 59.91  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  32 ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKQMlaqgypAYtts 111
Cdd:PRK14017   82 AIAGIDQALWDIKGKALGVPVHELL-----------------------------------GGLVRDRIR------VY--- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 112 cAWLGYSDDTLKQLCAQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLSLflqmmDANQRWDVP 181
Cdd:PRK14017  118 -SWIGGDRPADVAEAARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGV-----DFHGRVHKP 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 182 EAVEWMSKLAKFKPLWIEEPTSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRL 255
Cdd:PRK14017  192 MAKVLAKELEPYRPMFIEEPVLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHA 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 256 GSVNENLSVLLMAKKFEIPVCPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvm 323
Cdd:PRK14017  263 GGITECRKIAAMAEAYDVALAPHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY--- 335
                         330       340
                  ....*....|....*....|....*.
gi 1370473615 324 iqRASYM-PPKDPGYSTEMKEESVKK 348
Cdd:PRK14017  336 --EDGFVaIPTGPGLGIEIDEAKVRE 359
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
30-220 5.79e-09

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: 56.94  E-value: 5.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  30 HLATAAVLNAVWDLWAKQEGKPVWKLL----VDMDPrmlVSCIdfryITDVLTEEDALEILQkgqigkkerekqMLAQGY 105
Cdd:cd03318    98 LFAKAAIEMALLDAQGRRLGLPVSELLggrvRDSLP---VAWT----LASGDTERDIAEAEE------------MLEAGR 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 106 payttscawlgysddtlkqlcaqalkdgWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAV 184
Cdd:cd03318   159 ----------------------------HRRFKLKMGArPPADDLAHVEAIAKALGDRASV-----RVDVNQAWDESTAI 205
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370473615 185 EWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPL 220
Cdd:cd03318   206 RALPRLEAAGVELIEQPVPRENLDGLARLrSRNRVPI 242
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
31-348 8.46e-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: 50.31  E-value: 8.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  31 LATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGQIGKKerekqmlaqgypaytt 110
Cdd:cd03317    94 MAKAGLEMAVWDLYAKAQGQSLAQYL--------------------------------GGTRDS---------------- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 111 scAWLGYS-------DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLslflqMMDAN---QRWDV 180
Cdd:cd03317   126 --IPVGVSigiqddvEQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPL-----MADANsayTLADI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 181 PEavewMSKLAKFKPLWIEEPTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGS 257
Cdd:cd03317   195 PL----LKRLDEYGLLMIEQPLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGG 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 258 VNENLSVLLMAKKFEIPVCpHAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASY 329
Cdd:cd03317   265 LTEALKIHDLCQEHGIPVW-CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGII 335
                         330
                  ....*....|....*....
gi 1370473615 330 MPPKDPGYSTEMKEESVKK 348
Cdd:cd03317   336 SVPTGPGIGVTVDREALKK 354
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
23-358 3.29e-06

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: 48.59  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  23 GPekgVVHLATAAVLNAVWDLWAKQEGKPVWKLL--VDMDPRMLVSCIDFRYITDVLteedaleilqkgqigkkEREKQM 100
Cdd:cd03322    78 GP---VTMNAIAAVDMALWDIKGKAAGMPLYQLLggKSRDGIMVYSHASGRDIPELL-----------------EAVERH 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 101 LAQGYpayttscawlgysddtlKQLCAQALKdgwtRFKVkvgadlqddmrrcqiIRDMIGPEKTLslflqMMDANQRWDV 180
Cdd:cd03322   138 LAQGY-----------------RAIRVQLPK----LFEA---------------VREKFGFEFHL-----LHDVHHRLTP 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 181 PEAVEWMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVN 259
Cdd:cd03322   177 NQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGIT 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 260 ENLSVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsaslenrvceYVDHLHEHFKYPVMIQRAS 328
Cdd:cd03322   253 PARKIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR-----------HAEETLEVFPHSVRFEDGY 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1370473615 329 YMPPKDPGYSTEMKEESVKKHQY----------PDGEVWK 358
Cdd:cd03322   321 LHPGEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
133-201 3.35e-06

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 48.43  E-value: 3.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370473615 133 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLSlflqmMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 201
Cdd:PRK02901  102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVR-----VDANGGWSVDEAVAAARALDADGPLeYVEQP 169
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
32-282 6.31e-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: 47.78  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  32 ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGqiGKKERekqmlaqgYPAY-TT 110
Cdd:cd03329    95 GLGLVDIALWDLAGKYLGLPVHRLL--------------------------------G--GYREK--------IPAYaST 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 111 SCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLslflqMMDANQRWDVPEAVE 185
Cdd:cd03329   133 MVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRL-----MHDGAHWYSRADALR 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 186 WMSKLAKFKPLWIEEPTSPDDILGHATISKAL-VPLGIGIATGEQCHNRVIFkqlLQAKALQFLQIDSCRLGSVNENLSV 264
Cdd:cd03329   208 LGRALEELGFFWYEDPLREASISSYRWLAEKLdIPILGTEHSRGALESRADW---VLAGATDFLRADVNLVGGITGAMKT 284
                         250
                  ....*....|....*...
gi 1370473615 265 LLMAKKFEIPVCPHAGGV 282
Cdd:cd03329   285 AHLAEAFGLDVELHGNGA 302
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
125-208 1.95e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 43.69  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615  125 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLSlflqmMDANQRWDVPEAVEWMSKLAKFKPLWIEEP- 201
Cdd:PLN02980  1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELR-----ADANRNWTYEEAIEFGSLVKSCNLKYIEEPv 1171

                   ....*..
gi 1370473615  202 TSPDDIL 208
Cdd:PLN02980  1172 QDEDDLI 1178
PRK02714 PRK02714
o-succinylbenzoate synthase;
109-205 6.33e-03

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 38.07  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370473615 109 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLSLflqmmDANQRWDVPEAVEWM 187
Cdd:PRK02714  110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRL-----DANGGLSLEEAKRWL 183
                          90       100
                  ....*....|....*....|.
gi 1370473615 188 SKLAKFKPL---WIEEPTSPD 205
Cdd:PRK02714  184 QLCDRRLSGkieFIEQPLPPD 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.
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