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Conserved domains on  [gi|1227523100|ref|NP_001340997|]
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mitochondrial enolase superfamily member 1 isoform 7 [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 ...
 4-390 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100   4 GRISRLSVRDVRFPTSLGGHGADAMvsadamvsadamvsadamvsadamvsadamvsadamvsadamvsadamHTDPDYS 83
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAM------------------------------------------------NPDPDYS 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  84 AAYVVIETDAeDGIKGCGITFTLGKGTEV----------------------DWSRKGRGAPGDS-----GrPKRGV---- 132
Cdd:cd03324    33 AAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdlesivaDMGKFWRRLTSDSqlrwiG-PEKGVihla 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 133 ---------GLVGQAGGKACLEVTCGH------------------------EILQKGQIGKKEREKQMLAQGYPAYTTSC 179
Cdd:cd03324   111 taavvnavwDLWAKAEGKPLWKLLVDMtpeelvscidfryitdaltpeealEILRRGQPGKAAREADLLAEGYPAYTTSA 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 180 AWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLW 259
Cdd:cd03324   191 GWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWW 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 260 IEEPTSPDDILGHATISK--------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 325
Cdd:cd03324   271 IEEPTSPDDILGHAAIRKalaplpigvatgehCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCP 350

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227523100 326 HAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 390
Cdd:cd03324   351 HAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 4-390 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100   4 GRISRLSVRDVRFPTSLGGHGADAMvsadamvsadamvsadamvsadamvsadamvsadamvsadamvsadamHTDPDYS 83
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAM------------------------------------------------NPDPDYS 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  84 AAYVVIETDAeDGIKGCGITFTLGKGTEV----------------------DWSRKGRGAPGDS-----GrPKRGV---- 132
Cdd:cd03324    33 AAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdlesivaDMGKFWRRLTSDSqlrwiG-PEKGVihla 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 133 ---------GLVGQAGGKACLEVTCGH------------------------EILQKGQIGKKEREKQMLAQGYPAYTTSC 179
Cdd:cd03324   111 taavvnavwDLWAKAEGKPLWKLLVDMtpeelvscidfryitdaltpeealEILRRGQPGKAAREADLLAEGYPAYTTSA 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 180 AWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLW 259
Cdd:cd03324   191 GWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWW 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 260 IEEPTSPDDILGHATISK--------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 325
Cdd:cd03324   271 IEEPTSPDDILGHAAIRKalaplpigvatgehCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCP 350

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227523100 326 HAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 390
Cdd:cd03324   351 HAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 187-393 1.38e-52

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: 175.06  E-value: 1.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 187 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 265
Cdd:pfam13378   1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 266 PDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLcE 334
Cdd:pfam13378  81 PDDLEGLARLRRatpvpiatgesLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI-G 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 335 LVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 393
Cdd:pfam13378 160 LAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 75-397 5.26e-52

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: 177.71  E-value: 5.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  75 AMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVDWSR---------KGRgapgDSGRPKR-----GVGLVGQAGG 140
Cdd:COG4948    22 SRGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAAleealapllIGR----DPLDIEAlwqrlYRALPGNPAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 141 KACLEVTCgHEIL--QKGQ-----IGKKEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-D 211
Cdd:COG4948    96 KAAVDMAL-WDLLgkALGVpvyqlLGGKVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 212 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISK-----------CHN 280
Cdd:COG4948   165 PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatpvpiaadesLTS 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 281 RVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVC 356
Cdd:COG4948   245 RADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIV 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1227523100 357 EYVDHL---HEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKH 397
Cdd:COG4948   316 ELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 186-277 7.72e-27

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: 102.74  E-value: 7.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  186 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 265
Cdd:smart00922   2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81

                           90
                   ....*....|..
gi 1227523100  266 PDDILGHATISK 277
Cdd:smart00922  82 PDDLEGLAELRR 93
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 212-330 2.02e-07

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 52.81  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 212 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKC------------- 278
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNapagmmvtsgehe 270

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1227523100 279 HNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 330
Cdd:PRK15440  271 ATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
 
Name Accession Description Interval E-value
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 4-390 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100   4 GRISRLSVRDVRFPTSLGGHGADAMvsadamvsadamvsadamvsadamvsadamvsadamvsadamvsadamHTDPDYS 83
Cdd:cd03324     1 IKITALEVRDVRFPTSLELDGSDAM------------------------------------------------NPDPDYS 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  84 AAYVVIETDAeDGIKGCGITFTLGKGTEV----------------------DWSRKGRGAPGDS-----GrPKRGV---- 132
Cdd:cd03324    33 AAYVVLRTDA-AGLKGHGLTFTIGRGNEIvcaaiealahlvvgrdlesivaDMGKFWRRLTSDSqlrwiG-PEKGVihla 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 133 ---------GLVGQAGGKACLEVTCGH------------------------EILQKGQIGKKEREKQMLAQGYPAYTTSC 179
Cdd:cd03324   111 taavvnavwDLWAKAEGKPLWKLLVDMtpeelvscidfryitdaltpeealEILRRGQPGKAAREADLLAEGYPAYTTSA 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 180 AWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLW 259
Cdd:cd03324   191 GWLGYSDEKLRRLCKEALAQGFTHFKLKVGADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWW 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 260 IEEPTSPDDILGHATISK--------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCP 325
Cdd:cd03324   271 IEEPTSPDDILGHAAIRKalaplpigvatgehCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCP 350

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227523100 326 HAGGVGLCELVQHLIIFDYISVSASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMK 390
Cdd:cd03324   351 HAGGVGLCELVQHLSMIDYICVSGSKEGRVIEYVDHLHEHFVYPVVIQNGAYMPPTDPGYSIEMK 415
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 187-393 1.38e-52

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: 175.06  E-value: 1.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 187 DTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 265
Cdd:pfam13378   1 ELAAEARRAVEARGFRAFKLKVGGpDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 266 PDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLcE 334
Cdd:pfam13378  81 PDDLEGLARLRRatpvpiatgesLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPI-G 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 335 LVQHLIIfdYISVSASLENRVCEYVDHL-HEHFKYPVMIQRASYMPPKDPGYSTEMKEES 393
Cdd:pfam13378 160 LAASLHL--AAAVPNLLIQEYFLDPLLLeDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 75-397 5.26e-52

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: 177.71  E-value: 5.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  75 AMHTDPDYSAAYVVIETDaeDGIKGCGITFTLGKGTEVDWSR---------KGRgapgDSGRPKR-----GVGLVGQAGG 140
Cdd:COG4948    22 SRGTRTERDVVLVRVETD--DGITGWGEAVPGGTGAEAVAAAleealapllIGR----DPLDIEAlwqrlYRALPGNPAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 141 KACLEVTCgHEIL--QKGQ-----IGKKEREKqmlaqgYPAYttscAWLGY-SDDTLKQLCAQALKDGWTRFKVKVGA-D 211
Cdd:COG4948    96 KAAVDMAL-WDLLgkALGVpvyqlLGGKVRDR------VPVY----ATLGIdTPEEMAEEAREAVARGFRALKLKVGGpD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 212 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISK-----------CHN 280
Cdd:COG4948   165 PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAELRRatpvpiaadesLTS 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 281 RVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPH---AGGVGLCELVQhliifdyisVSASLEN-RVC 356
Cdd:COG4948   245 RADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcmlESGIGLAAALH---------LAAALPNfDIV 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1227523100 357 EYVDHL---HEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKH 397
Cdd:COG4948   316 ELDGPLllaDDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 158-388 2.71e-44

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: 157.39  E-value: 2.71e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 158 IGKKEREKqmlaqgYPAYTTSCAWlGYSDDTLKQLCAQALKDGWTRFKVKVGA------DLQDDMRRCQIIRDMIGPEKT 231
Cdd:cd03316   119 LGGKVRDR------VRVYASGGGY-DDSPEELAEEAKRAVAEGFTAVKLKVGGpdsggeDLREDLARVRAVREAVGPDVD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 232 LMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKC-----------HNRVIFKQLLQAKALQFLQIDS 300
Cdd:cd03316   192 LMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQAtsvpiaagenlYTRWEFRDLLEAGAVDIIQPDV 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 301 CRLGSVNENLSVLLMAKKFEIPVCPHAGGVGLC-ELVQHLiifdyisvSASLEN-RVCEYVDHLHEH----FKYPVMIQR 374
Cdd:cd03316   272 TKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGlAASLHL--------AAALPNfGILEYHLDDLPLredlFKNPPEIED 343

                         250
                  ....*....|....
gi 1227523100 375 ASYMPPKDPGYSTE 388
Cdd:cd03316   344 GYVTVPDRPGLGVE 357
MR_MLE smart00922
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ...
 186-277 7.72e-27

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: 102.74  E-value: 7.72e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  186 DDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTS 265
Cdd:smart00922   2 EELAEAARRAVAEAGFRAVKVKVGGGPLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81

                           90
                   ....*....|..
gi 1227523100  266 PDDILGHATISK 277
Cdd:smart00922  82 PDDLEGLAELRR 93
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
 158-390 1.40e-25

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: 106.26  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 158 IGKKEREKqmlaqgYPAYTTScawLGYSD-DTLKQLCAQALKDGWTRFKVKVG-------ADLQDDMRRCQIIRDMIGPE 229
Cdd:cd03327   101 LGGRTRDK------IPAYASG---LYPTDlDELPDEAKEYLKEGYRGMKMRFGygpsdghAGLRKNVELVRAIREAVGYD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 230 KTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKC-----------HNRVIFKQLLQAKALQFLQI 298
Cdd:cd03327   172 VDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKAtgipistgeheYTVYGFKRLLEGRAVDILQP 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 299 DSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVglceLVQHLIIFDYIS-VSASLEN-RVCEYVDHLHEHFKYPVMIQRAS 376
Cdd:cd03327   252 DVNWVGGITELKKIAALAEAYGVPVVPHASQI----YNYHFIMSEPNSpFAEYLPNsPDEVGNPLFYYIFLNEPVPVNGY 327

                         250
                  ....*....|....
gi 1227523100 377 YMPPKDPGYSTEMK 390
Cdd:cd03327   328 FDLSDKPGFGLELN 341
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 192-339 1.22e-21

Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.


Pssm-ID: 238188 [Multi-domain]  Cd Length: 229  Bit Score: 92.78  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 192 LCAQALK-------DGWTRFKVKVGADLqddmRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPT 264
Cdd:cd00308    54 LAAKALGvplaellGGGSRDRVPAYGSI----ERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 265 SPDDILGHATISK-----------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGVG-- 331
Cdd:cd00308   130 APDDLEGYAALRRrtgipiaadesVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESsi 209


                  ....*...
gi 1227523100 332 LCELVQHL 339
Cdd:cd00308   210 GTAAALHL 217
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
 173-326 6.52e-17

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: 81.30  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 173 PAYTtSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKL 252
Cdd:cd03328   127 PVYG-SGGFTSYDDDRLREQLSGWVAQGIPRVKMKIGRDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAF 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 253 AKFKPLWIEEPTSPDDILGHATISK-------------CHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKF 319
Cdd:cd03328   206 ADEGVTWFEEPVSSDDLAGLRLVRErgpagmdiaageyAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAH 285


                  ....*..
gi 1227523100 320 EIPVCPH 326
Cdd:cd03328   286 HVDLSAH 292
OSBS cd03320
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ...
 177-272 1.64e-14

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: 73.06  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 177 TSCAWLGYSDDTLKQLCAQALKDGWTRFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKF 255
Cdd:cd03320    74 PVNALLPAGDAAALGEAKAAYGGGYRTVKLKVGAtSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAG 153

                          90
                  ....*....|....*..
gi 1227523100 256 KPLWIEEPTSPDDILGH 272
Cdd:cd03320   154 RIEYIEQPLPPDDLAEL 170
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
 195-398 3.68e-14

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: 73.29  E-value: 3.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 195 QALKDGWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHA 273
Cdd:cd03321   151 TAAEEGFHAVKTKIGyPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 274 TISKCHNRVI-----------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHaggvglcelvqhliIF 342
Cdd:cd03321   231 RIASALRTPVqmgenwlgpeeMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH--------------LF 296

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1227523100 343 DYISV---SASLENRVCEYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQ 398
Cdd:cd03321   297 QEISAhllAVTPTAHWLEYVDWAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKYL 355
MLE_like cd03315
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ...
 195-339 8.91e-13

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: 68.14  E-value: 8.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 195 QALKDGWTRFKVKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHAt 274
Cdd:cd03315    95 RALEAGFRTFKLKVGRDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRA- 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 275 isKCHNRVI--------------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPV---CPHAGGVGLCELVq 337
Cdd:cd03315   174 --ALARATDtpimadesaftphdAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVmvgSMIESGLGTLANA- 250


                  ..
gi 1227523100 338 HL 339
Cdd:cd03315   251 HL 252
MR_like_1 cd03326
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ...
 200-279 7.73e-11

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


Pssm-ID: 239442 [Multi-domain]  Cd Length: 385  Bit Score: 63.18  E-value: 7.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 200 GWTRFKVKVG-ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKC 278
Cdd:cd03326   175 GYTVVKIKIGgAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADH 254


                  .
gi 1227523100 279 H 279
Cdd:cd03326   255 Y 255
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 ...
 194-269 1.13e-09

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: 59.12  E-value: 1.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227523100 194 AQALKDGWTRFKVKVGADLQDDMRRCQIIRDMIgPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDI 269
Cdd:cd03319   143 KKAAKRGFPLLKIKLGGDLEDDIERIRAIREAA-PDARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDD 217
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
 203-276 1.60e-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: 59.25  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227523100 203 RFKVKVGA-DLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATIS 276
Cdd:cd03318   161 RFKLKMGArPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLR 235
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 180-327 2.06e-09

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: 58.49  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 180 AWLG-YSDDTLKQLCAQALKDGWTRFK---------VKVGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWM 249
Cdd:cd03325   117 SWIGgDRPSDVAEAARARREAGFTAVKmnateelqwIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLA 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 250 SKLAKFKPLWIEEPTSPDDILGHATISKCHNRVI-----------FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKK 318
Cdd:cd03325   197 KELEPYRLLFIEEPVLPENVEALAEIAARTTIPIatgerlfsrwdFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEA 276


                  ....*....
gi 1227523100 319 FEIPVCPHA 327
Cdd:cd03325   277 YDVALAPHC 285
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 212-330 2.02e-07

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 52.81  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 212 LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDDILGHATISKC------------- 278
Cdd:PRK15440  191 LRKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNapagmmvtsgehe 270

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1227523100 279 HNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHAGGV 330
Cdd:PRK15440  271 ATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSV 322
PRK02901 PRK02901
O-succinylbenzoate synthase; Provisional
 200-263 2.52e-07

O-succinylbenzoate synthase; Provisional


Pssm-ID: 235084 [Multi-domain]  Cd Length: 327  Bit Score: 52.28  E-value: 2.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227523100 200 GWTRFKVKV---GADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPL-WIEEP 263
Cdd:PRK02901  102 GCRTAKVKVaepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALDADGPLeYVEQP 169
PRK14017 PRK14017
galactonate dehydratase; Provisional
 194-396 4.13e-07

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 51.82  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 194 AQALKD-GWTRFKVKVGADLQ--DDMR-------RCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP 263
Cdd:PRK14017  132 ARARVErGFTAVKMNGTEELQyiDSPRkvdaavaRVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 264 TSPD------DILGHATIS-----KCHNRVIFKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEIPVCPHA--GGV 330
Cdd:PRK14017  212 VLPEnaealpEIAAQTSIPiatgeRLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCplGPI 291

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227523100 331 GLCELVQhliiFDYISVSASLE--------NRVCEYVDHL--HEHFKYpvmiqRASYM-PPKDPGYSTEMKEESVKK 396
Cdd:PRK14017  292 ALAACLQ----VDAVSPNAFIQeqslgihyNQGADLLDYVknKEVFAY-----EDGFVaIPTGPGLGIEIDEAKVRE 359
NAAAR cd03317
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ...
 186-396 2.55e-06

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: 49.16  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 186 DDTLKQLcAQALKDGWTRFKVKVGAdlQDDMRRCQIIRDMIgPEKTLMMDAN---QRWDVPEavewMSKLAKFKPLWIEE 262
Cdd:cd03317   139 EQLLKQI-ERYLEEGYKRIKLKIKP--GWDVEPLKAVRERF-PDIPLMADANsayTLADIPL----LKRLDEYGLLMIEQ 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 263 PTSPDDILGHATISK------CHNRVI--FKQLLQAKALQFLQ---IDSCRLGSVNENLSVLLMAKKFEIPVCpHAG--- 328
Cdd:cd03317   211 PLAADDLIDHAELQKllktpiCLDESIqsAEDARKAIELGACKiinIKPGRVGGLTEALKIHDLCQEHGIPVW-CGGmle 289

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1227523100 329 -GVGLCELVQ--HLIIFDY-ISVSASleNRvceyvdHLHEHF-KYPVMIQRASYMPPKDPGYSTEMKEESVKK 396
Cdd:cd03317   290 sGIGRAHNVAlaSLPNFTYpGDISAS--SR------YFEEDIiTPPFELENGIISVPTGPGIGVTVDREALKK 354
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 192-270 3.49e-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: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100  192 LCAQALKDGWTRFKVKVG--ADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEP-TSPDD 268
Cdd:PLN02980  1097 VARKLVEEGFSAIKLKVGrrVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPvQDEDD 1176


                   ..
gi 1227523100  269 IL 270
Cdd:PLN02980  1177 LI 1178
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
 173-277 1.85e-04

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: 43.15  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 173 PAY-TTSCAWLGYSDDTLKQLC--AQALKD-GWTRFKVK--VGADLQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAV 246
Cdd:cd03329   127 PAYaSTMVGDDLEGLESPEAYAdfAEECKAlGYRAIKLHpwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADAL 206

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1227523100 247 EWMSKLAKFKPLWIEEPTSPDDILGHATISK 277
Cdd:cd03329   207 RLGRALEELGFFWYEDPLREASISSYRWLAE 237
PRK02714 PRK02714
o-succinylbenzoate synthase;
176-267 1.89e-04

o-succinylbenzoate synthase;


Pssm-ID: 235061 [Multi-domain]  Cd Length: 320  Bit Score: 43.08  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 176 TTSCAWLGYSDDTLKQLcAQALKDGWTRFKVKVGAD-LQDDMRRCQIIRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAK 254
Cdd:PRK02714  110 LSYSALLPAGEAALQQW-QTLWQQGYRTFKWKIGVDpLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDR 188

                          90
                  ....*....|....*.
gi 1227523100 255 FKPL---WIEEPTSPD 267
Cdd:PRK02714  189 RLSGkieFIEQPLPPD 204
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
 218-406 5.49e-04

The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.


Pssm-ID: 239438 [Multi-domain]  Cd Length: 361  Bit Score: 41.66  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 218 RCQI------IRDMIGPEKTLMMDANQRWDVPEAVEWMSKLAKFKPLWIEEPTSPDD------ILGHAT----ISKCHNR 281
Cdd:cd03322   146 RVQLpklfeaVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENqeafrlIRQHTAtplaVGEVFNS 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227523100 282 VI-FKQLLQAKALQFLQIDSCRLGSVNENLSVLLMAKKFEI-----------PVCpHAGGVGLCELVQHLIIFDYISvsa 349
Cdd:cd03322   226 IWdWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVrtgwhgptdlsPVG-MAAALHLDLWVPNFGIQEYMR--- 301

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227523100 350 slenrvceYVDHLHEHFKYPVMIQRASYMPPKDPGYSTEMKEESVKKHQY----------PDGEVWK 406
Cdd:cd03322   302 --------HAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYvprylpvarlEDGTVHN 360
 
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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