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Conserved domains on  [gi|1227484157|ref|NP_001340994|]
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mitochondrial enolase superfamily member 1 isoform rTSalpha [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

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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 ...
 19-337 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: 686.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEA 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 179 VEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLS 258
Cdd:cd03324   257 IEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLA 336

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227484157 259 VLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 337
Cdd:cd03324   337 VLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 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 ...
 19-337 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: 686.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEA 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 179 VEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLS 258
Cdd:cd03324   257 IEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLA 336

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227484157 259 VLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 337
Cdd:cd03324   337 VLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 14-344 4.50e-68

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: 218.15  E-value: 4.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  14 LWEKALKLIGpekgVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGK 93
Cdd:COG4948    81 LWQRLYRALP----GNPAAKAAVDMALWDLLGKALGVPVYQLL-----------------------------------GG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  94 KEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQ 171
Cdd:COG4948   122 KVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 172 RWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLG 251
Cdd:COG4948   192 AWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 252 SVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASY 324
Cdd:COG4948   269 GLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYL 339

                         330       340
                  ....*....|....*....|
gi 1227484157 325 MPPKDPGYSTEMKEESVKKH 344
Cdd:COG4948   340 TVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 122-340 2.54e-62

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: 198.56  E-value: 2.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 122 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSP 199
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 200 DDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGL 279
Cdd:pfam13378  82 DDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227484157 280 cELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 340
Cdd:pfam13378 159 -GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 119-212 5.84e-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: 105.06  E-value: 5.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  119 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 198
Cdd:smart00922   2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81

                           90
                   ....*....|....
gi 1227484157  199 PDDILGHATISKAL 212
Cdd:smart00922  82 PDDLEGLAELRRAT 95
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 145-277 5.57e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 69.37  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 145 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 224
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1227484157 225 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 277
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 ...
 19-337 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: 686.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  19 LKLIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIDFRYITDVLTEEDALEILQKGQIGKKEREK 98
Cdd:cd03324    97 LRWIGPEKGVIHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIDFRYITDALTPEEALEILRRGQPGKAAREA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  99 QMLAQGYPAYTTSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEA 178
Cdd:cd03324   177 DLLAEGYPAYTTSAGWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEA 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 179 VEWMSKLAKFKPLWIEEPTSPDDILGHATISKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLS 258
Cdd:cd03324   257 IEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLA 336

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227484157 259 VLLMAKKFEIPVCPHAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 337
Cdd:cd03324   337 VLLMAAKFGVPVCPHAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 14-344 4.50e-68

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: 218.15  E-value: 4.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  14 LWEKALKLIGpekgVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGK 93
Cdd:COG4948    81 LWQRLYRALP----GNPAAKAAVDMALWDLLGKALGVPVYQLL-----------------------------------GG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  94 KEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQ 171
Cdd:COG4948   122 KVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpDPEEDVERVRAVREAVGPDARLRVDANG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 172 RWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLG 251
Cdd:COG4948   192 AWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRA---TPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 252 SVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVCEYVDHL---HEHFKYPVMIQRASY 324
Cdd:COG4948   269 GLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIVELDGPLllaDDLVEDPLRIEDGYL 339

                         330       340
                  ....*....|....*....|
gi 1227484157 325 MPPKDPGYSTEMKEESVKKH 344
Cdd:COG4948   340 TVPDGPGLGVELDEDALARY 359
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 122-340 2.54e-62

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: 198.56  E-value: 2.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 122 LKQLCAQALKD-GWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSP 199
Cdd:pfam13378   2 LAAEARRAVEArGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 200 DDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGL 279
Cdd:pfam13378  82 DDLEGLARLRRA---TPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227484157 280 cELVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 340
Cdd:pfam13378 159 -GLAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 13-335 1.97e-61

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: 200.92  E-value: 1.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  13 SLWEKALK--LIGPEKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgq 90
Cdd:cd03316    74 RLWEKLYRrlFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLL---------------------------------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  91 iGKKEREKqmlaqgYPAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKT 164
Cdd:cd03316   120 -GGKVRDR------VRVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVD 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 165 LMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQ 244
Cdd:cd03316   192 LMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQA---TSVPIAAGENLYTRWEFRDLLEAGAVDIIQ 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 245 IDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVM 318
Cdd:cd03316   269 PDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPE 340

                         330
                  ....*....|....*..
gi 1227484157 319 IQRASYMPPKDPGYSTE 335
Cdd:cd03316   341 IEDGYVTVPDRPGLGVE 357
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
 14-337 3.93e-36

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: 134.00  E-value: 3.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  14 LWEKALKLIGP--EKGVVHLATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqi 91
Cdd:cd03327    57 LWDQMYRATLAygRKGIAMAAISAVDLALWDLLGKIRGEPVYKLL----------------------------------- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  92 GKKEREKqmlaqgYPAYTTScawLGYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPEK 163
Cdd:cd03327   102 GGRTRDK------IPAYASG---LYPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYDV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 164 TLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFL 243
Cdd:cd03327   173 DLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKA---TGIPISTGEHEYTVYGFKRLLEGRAVDIL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 244 QIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQR 321
Cdd:cd03327   250 QPDVNWVGGITELKKIAALAEAYGVPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVN 325

                         330
                  ....*....|....*.
gi 1227484157 322 ASYMPPKDPGYSTEMK 337
Cdd:cd03327   326 GYFDLSDKPGFGLELN 341
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
 12-273 2.08e-28

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239444 [Multi-domain]  Cd Length: 352  Bit Score: 113.28  E-value: 2.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  12 PSLWE---KALKLIGPEkGVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMlvscidfryitdvlteedaleilqk 88
Cdd:cd03328    73 PAAWEamqRAVRNAGRP-GVAAMAISAVDIALWDLKARLLGLPLARLLGRAHDSV------------------------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  89 gqigkkerekqmlaqgyPAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMD 168
Cdd:cd03328   127 -----------------PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 169 ANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATIsKALVPLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSC 248
Cdd:cd03328   189 ANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLV-RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVT 267

                         250       260
                  ....*....|....*....|....*
gi 1227484157 249 RLGSVNENLSVLLMAKKFEIPVCPH 273
Cdd:cd03328   268 RCGGVTGFLQAAALAAAHHVDLSAH 292
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 119-212 5.84e-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: 105.06  E-value: 5.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  119 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 198
Cdd:smart00922   2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81

                           90
                   ....*....|....
gi 1227484157  199 PDDILGHATISKAL 212
Cdd:smart00922  82 PDDLEGLAELRRAT 95
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 125-286 2.03e-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: 105.10  E-value: 2.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 125 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 197
Cdd:cd00308    54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 198 SPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 277
Cdd:cd00308   130 APDDLEGYAALRRR---TGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE 206

                         170
                  ....*....|.
gi 1227484157 278 G--LCELVQHL 286
Cdd:cd00308   207 SsiGTAAALHL 217
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
 27-286 3.37e-17

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: 80.46  E-value: 3.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  27 GVVHLATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVScidfrYITDVLTEEDALEilqkgqigkkerekqmlaqgyp 106
Cdd:cd03315    39 GWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVA-----HMLGLGEPAEVAE---------------------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 107 ayttscawlgysddtlkqLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLA 186
Cdd:cd03315    92 ------------------EARRALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALE 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 187 KFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKF 266
Cdd:cd03315   154 DLGLDYVEQPLPADDLEGRAALARA---TDTPIMADESAFTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEAL 230

                         250       260
                  ....*....|....*....|...
gi 1227484157 267 EIPV---CPHAGGVGLCELVqHL 286
Cdd:cd03315   231 GLPVmvgSMIESGLGTLANA-HL 252
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
 128-345 5.07e-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: 80.99  E-value: 5.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 128 QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 206
Cdd:cd03321   151 TAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 207 TISKAL-VPLGIgiatGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqh 285
Cdd:cd03321   231 RIASALrTPVQM----GENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH------------ 294

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1227484157 286 liIFDYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 345
Cdd:cd03321   295 --LFQEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 27-279 7.67e-17

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: 80.45  E-value: 7.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  27 GVVHL-ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKqmlAQGY 105
Cdd:cd03325    75 GPVLMsAISGIDQALWDIKGKVLGVPVHQLL-----------------------------------GGQVRDR---VRVY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 106 payttscAWLG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDV 175
Cdd:cd03325   117 -------SWIGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSK 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 176 PEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNE 255
Cdd:cd03325   190 PMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAAR---TTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITE 266

                         250       260
                  ....*....|....*....|....*.
gi 1227484157 256 NLSVLLMAKKFEIPVCPHA--GGVGL 279
Cdd:cd03325   267 LKKIAAMAEAYDVALAPHCplGPIAL 292
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
 110-270 5.10e-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: 74.22  E-value: 5.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 110 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 188
Cdd:cd03320    74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 189 KPLWIEEPTSPDDILGHatisKALVpLGIGIATGEqchnrvifkQLLQAKALQFLQIDSC---------RLGSVNENLSV 259
Cdd:cd03320   154 RIEYIEQPLPPDDLAEL----RRLA-AGVPIALDE---------SLRRLDDPLALAAAGAlgalvlkpaLLGGPRALLEL 219

                         170
                  ....*....|.
gi 1227484157 260 LLMAKKFEIPV 270
Cdd:cd03320   220 AEEARARGIPA 230
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
 32-223 1.74e-14

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: 73.97  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  32 ATAAVLNAVWDLWAKQEGKPVWKLLVDmdprmlvscidfRYitdvlteedaleilqkGQIGKKEREKQMLAQGYPaytts 111
Cdd:cd03326   109 AVGALDMAVWDAVAKIAGLPLYRLLAR------------RY----------------GRGQADPRVPVYAAGGYY----- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 112 cawlgYSDDTLKQLCAQA---LKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 187
Cdd:cd03326   156 -----YPGDDLGRLRDEMrryLDRGYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAP 230

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1227484157 188 FKPLWIEEPTSPDDILGHATISKALVPlgiGIATGE 223
Cdd:cd03326   231 YGLRWYEEPGDPLDYALQAELADHYDG---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 ...
 32-228 3.71e-14

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: 72.22  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  32 ATAAVLNAVWDLWAKQEGKPVWKLLVDMDPRMLVSCIdfryiTDVLTEEDALeilqkgqigkKEREKQMLAQGYPAytts 111
Cdd:cd03319    92 ARAAVDIALWDLEAKLLGLPLYQLWGGGAPRPLETDY-----TISIDTPEAM----------AAAAKKAAKRGFPL---- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 112 cawlgysddtlkqlcaqalkdgwtrFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL 191
Cdd:cd03319   153 -------------------------LKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVE 206

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1227484157 192 WIEEPTSPDDILGHATISKAlvpLGIGIATGEQCHNR 228
Cdd:cd03319   207 LIEQPVPAGDDDGLAYLRDK---SPLPIMADESCFSA 240
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 145-277 5.57e-13

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 69.37  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 145 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKAlVPLGIGIATGEQ 224
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN-APAGMMVTSGEH 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1227484157 225 CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 277
Cdd:PRK15440  270 EATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
PRK14017 PRK14017
galactonate dehydratase; Provisional
 32-343 4.08e-11

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 63.76  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  32 ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkgqiGKKEREKQMlaqgypAYtts 111
Cdd:PRK14017   82 AIAGIDQALWDIKGKALGVPVHELL-----------------------------------GGLVRDRIR------VY--- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 112 cAWLGYSDDTLKQLCAQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEW 181
Cdd:PRK14017  118 -SWIGGDRPADVAEAARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 182 MSKLAKFKPLWIEEPTSPD------DILGHATISkalvplgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNE 255
Cdd:PRK14017  197 AKELEPYRPMFIEEPVLPEnaealpEIAAQTSIP---------IATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITE 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 256 NLSVLLMAKKFEIPVCPHA--GGVGLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRAS 323
Cdd:PRK14017  268 CRKIAAMAEAYDVALAPHCplGPIALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDG 338

                         330       340
                  ....*....|....*....|.
gi 1227484157 324 YM-PPKDPGYSTEMKEESVKK 343
Cdd:PRK14017  339 FVaIPTGPGLGIEIDEAKVRE 359
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
 30-215 5.46e-11

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: 63.10  E-value: 5.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  30 HLATAAVLNAVWDLWAKQEGKPVWKLL----VDMDPrmlVSCIdfryITDVLTEEDALEILQkgqigkkerekqMLAQGY 105
Cdd:cd03318    98 LFAKAAIEMALLDAQGRRLGLPVSELLggrvRDSLP---VAWT----LASGDTERDIAEAEE------------MLEAGR 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 106 payttscawlgysddtlkqlcaqalkdgWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSK 184
Cdd:cd03318   159 ----------------------------HRRFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPR 210

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1227484157 185 LAKFKPLWIEEPTSPDDILGHATI-SKALVPL 215
Cdd:cd03318   211 LEAAGVELIEQPVPRENLDGLARLrSRNRVPI 242
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
 31-343 8.36e-09

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: 56.47  E-value: 8.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  31 LATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGQIGKKerekqmlaqgypaytt 110
Cdd:cd03317    94 MAKAGLEMAVWDLYAKAQGQSLAQYL--------------------------------GGTRDS---------------- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 111 scAWLGYS-------DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEave 180
Cdd:cd03317   126 --IPVGVSigiqddvEQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL--- 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 181 wMSKLAKFKPLWIEEPTSPDDILGHATISKAL---VPLGIGIATGEQChnrvifKQLLQAKALQFLQIDSCRLGSVNENL 257
Cdd:cd03317   197 -LKRLDEYGLLMIEQPLAADDLIDHAELQKLLktpICLDESIQSAEDA------RKAIELGACKIINIKPGRVGGLTEAL 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 258 SVLLMAKKFEIPVCpHAG----GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKD 329
Cdd:cd03317   270 KIHDLCQEHGIPVW-CGGmlesGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTG 340

                         330
                  ....*....|....
gi 1227484157 330 PGYSTEMKEESVKK 343
Cdd:cd03317   341 PGIGVTVDREALKK 354
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
 23-353 4.03e-08

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: 54.37  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  23 GPekgVVHLATAAVLNAVWDLWAKQEGKPVWKLL--VDMDPRMLVSCIDFRYITDVLteedaleilqkgqigkkEREKQM 100
Cdd:cd03322    78 GP---VTMNAIAAVDMALWDIKGKAAGMPLYQLLggKSRDGIMVYSHASGRDIPELL-----------------EAVERH 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 101 LAQGYpayttscawlgysddtlKQLCAQALKdgwtRFKVkvgadlqddmrrcqiIRDMIGPEKTLMMDANQRWDVPEAVE 180
Cdd:cd03322   138 LAQGY-----------------RAIRVQLPK----LFEA---------------VREKFGFEFHLLHDVHHRLTPNQAAR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 181 WMSKLAKFKPLWIEEPTSPDDILGHATI-SKALVPlgigIATGEQCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSV 259
Cdd:cd03322   182 FGKDVEPYRLFWMEDPTPAENQEAFRLIrQHTATP----LAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 260 LLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsaslenrvceYVDHLHEHFKYPVMIQRASYMPPK 328
Cdd:cd03322   258 ADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR-----------HAEETLEVFPHSVRFEDGYLHPGE 325

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1227484157 329 DPGYSTEMKEESVKKHQY----------PDGEVWK 353
Cdd:cd03322   326 EPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
 133-196 4.58e-08

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 54.20  E-value: 4.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227484157 133 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 196
Cdd:PRK02901  102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
 32-277 6.94e-08

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: 53.55  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  32 ATAAVLNAVWDLWAKQEGKPVWKLLvdmdprmlvscidfryitdvlteedaleilqkGqiGKKERekqmlaqgYPAY-TT 110
Cdd:cd03329    95 GLGLVDIALWDLAGKYLGLPVHRLL--------------------------------G--GYREK--------IPAYaST 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 111 SCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKL 185
Cdd:cd03329   133 MVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRAL 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 186 AKFKPLWIEEPTSPDDILGHATISKAL-VPLGIGIATGEQCHNRVIFkqlLQAKALQFLQIDSCRLGSVNENLSVLLMAK 264
Cdd:cd03329   213 EELGFFWYEDPLREASISSYRWLAEKLdIPILGTEHSRGALESRADW---VLAGATDFLRADVNLVGGITGAMKTAHLAE 289

                         250
                  ....*....|...
gi 1227484157 265 KFEIPVCPHAGGV 277
Cdd:cd03329   290 AFGLDVELHGNGA 302
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 125-203 2.63e-06

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 49.47  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157  125 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 201
Cdd:PLN02980  1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176


                   ..
gi 1227484157  202 IL 203
Cdd:PLN02980  1177 LI 1178
PRK02714 PRK02714
o-succinylbenzoate synthase;
109-200 3.32e-04

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 41.92  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227484157 109 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 187
Cdd:PRK02714  110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188

                          90
                  ....*....|....*.
gi 1227484157 188 FKPL---WIEEPTSPD 200
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.
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