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Conserved domains on  [gi|2440762425|ref|WP_272496384|]
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MULTISPECIES: enolase C-terminal domain-like protein, partial [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14017 super family cl32947
galactonate dehydratase; Provisional
 23-194 6.47e-123

galactonate dehydratase; Provisional


The actual alignment was detected with superfamily member PRK14017:

Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 351.89  E-value: 6.47e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:PRK14017  211 PVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGP 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEIDEARVIELSKNAPDWRNP 182
Cdd:PRK14017  291 IALAACLQVDAVSPNAFIQEQSLGIHYNQGADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNP 370

                         170
                  ....*....|..
gi 2440762425 183 LWRYEDGSVAEW 194
Cdd:PRK14017  371 VWRHADGSVAEW 382
 
Name Accession Description Interval E-value
PRK14017 PRK14017
galactonate dehydratase; Provisional
 23-194 6.47e-123

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 351.89  E-value: 6.47e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:PRK14017  211 PVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGP 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEIDEARVIELSKNAPDWRNP 182
Cdd:PRK14017  291 IALAACLQVDAVSPNAFIQEQSLGIHYNQGADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNP 370

                         170
                  ....*....|..
gi 2440762425 183 LWRYEDGSVAEW 194
Cdd:PRK14017  371 VWRHADGSVAEW 382
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 15-165 4.05e-81

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: 244.93  E-value: 4.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  15 EEMTCLFA--PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDV 92
Cdd:cd03325   200 EPYRLLFIeePVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2440762425  93 GLAPHCPLGPIALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEID 165
Cdd:cd03325   280 ALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 23-168 6.01e-48

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: 155.80  E-value: 6.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:pfam13378  78 PVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYnkgaelLDFVKNKEDFNMEGGFFKPLMKPGLGVEIDEAR 168
Cdd:pfam13378 158 IGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 23-169 1.18e-41

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: 143.42  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPL-G 101
Cdd:COG4948   216 PLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeS 295

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2440762425 102 PIALAACLHVDFVSHNAVFQEQSMGIHYNKgaellDFVknKEDFNMEGGFFKPLMKPGLGVEIDEARV 169
Cdd:COG4948   296 GIGLAAALHLAAALPNFDIVELDGPLLLAD-----DLV--EDPLRIEDGYLTVPDGPGLGVELDEDAL 356
 
Name Accession Description Interval E-value
PRK14017 PRK14017
galactonate dehydratase; Provisional
 23-194 6.47e-123

galactonate dehydratase; Provisional


Pssm-ID: 184455 [Multi-domain]  Cd Length: 382  Bit Score: 351.89  E-value: 6.47e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:PRK14017  211 PVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGP 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEIDEARVIELSKNAPDWRNP 182
Cdd:PRK14017  291 IALAACLQVDAVSPNAFIQEQSLGIHYNQGADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNP 370

                         170
                  ....*....|..
gi 2440762425 183 LWRYEDGSVAEW 194
Cdd:PRK14017  371 VWRHADGSVAEW 382
D-galactonate_dehydratase cd03325
D-galactonate dehydratase catalyses the dehydration of galactonate to ...
 15-165 4.05e-81

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: 244.93  E-value: 4.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  15 EEMTCLFA--PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDV 92
Cdd:cd03325   200 EPYRLLFIeePVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDV 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2440762425  93 GLAPHCPLGPIALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEID 165
Cdd:cd03325   280 ALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGDDLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
MR_MLE_C pfam13378
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ...
 23-168 6.01e-48

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: 155.80  E-value: 6.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:pfam13378  78 PVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYnkgaelLDFVKNKEDFNMEGGFFKPLMKPGLGVEIDEAR 168
Cdd:pfam13378 158 IGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDEDA 217
MR_like cd03316
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ...
 23-163 2.15e-45

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: 153.15  E-value: 2.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGP 102
Cdd:cd03316   223 PVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGP 302

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2440762425 103 IALAACLHVDFVSHNAVFQEQSMGIHYnkgaelLDFVKNKEDFNMEGGFFKPLMKPGLGVE 163
Cdd:cd03316   303 IGLAASLHLAAALPNFGILEYHLDDLP------LREDLFKNPPEIEDGYVTVPDRPGLGVE 357
RspA COG4948
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ...
 23-169 1.18e-41

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: 143.42  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPL-G 101
Cdd:COG4948   216 PLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeS 295

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2440762425 102 PIALAACLHVDFVSHNAVFQEQSMGIHYNKgaellDFVknKEDFNMEGGFFKPLMKPGLGVEIDEARV 169
Cdd:COG4948   296 GIGLAAALHLAAALPNFDIVELDGPLLLAD-----DLV--EDPLRIEDGYLTVPDGPGLGVELDEDAL 356
MR_like_2 cd03327
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ...
 14-165 3.14e-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: 99.71  E-value: 3.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  14 WEEmtclfaPSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVG 93
Cdd:cd03327   202 IEE------PLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVP 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2440762425  94 LAPHCplgpiALAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMeGGFFKPLMKPGLGVEID 165
Cdd:cd03327   276 VVPHA-----SQIYNYHFIMSEPNSPFAEYLPNSPDEVGNPLFYYIFLNEPVPV-NGYFDLSDKPGFGLELN 341
enolase_like cd00308
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ...
 23-122 4.59e-24

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: 94.32  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAgERMFSRFEFK-RVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLG 101
Cdd:cd00308   128 PCAPDDLEGYAALRRRTGIPIAA-DESVTTVDDAlEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE 206

                          90       100
                  ....*....|....*....|..
gi 2440762425 102 -PIALAACLHVDFVSHNAVFQE 122
Cdd:cd00308   207 sSIGTAAALHLAAALPNDRAIE 228
RspA cd03322
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ...
 23-194 1.13e-23

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: 95.97  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCP--L 100
Cdd:cd03322   197 PTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdL 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425 101 GPIALAACLHVDFVSHNAVFQEQsMGiHYNKGAELLdfvknKEDFNMEGGFFKPLMKPGLGVEIDEarviELSKNAPDWR 180
Cdd:cd03322   277 SPVGMAAALHLDLWVPNFGIQEY-MR-HAEETLEVF-----PHSVRFEDGYLHPGEEPGLGVEIDE----KAAAKFPYVP 345

                         170
                  ....*....|....*.
gi 2440762425 181 NPL--WRYEDGSVAEW 194
Cdd:cd03322   346 RYLpvARLEDGTVHNW 361
PRK15072 PRK15072
D-galactonate dehydratase family protein;
23-194 8.45e-17

D-galactonate dehydratase family protein;


Pssm-ID: 237901 [Multi-domain]  Cd Length: 404  Bit Score: 77.26  E-value: 8.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYpRLAAQ-THIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCP-- 99
Cdd:PRK15072  240 PTPAENQEAF-RLIRQhTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPtd 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425 100 LGPIALAACLHVDFVSHNAVFQEqsmgihYNKGAELLDFVkNKEDFNMEGGFFKPLMKPGLGVEIDEarviELSKNAPDW 179
Cdd:PRK15072  319 LSPVCMAAALHFDLWVPNFGIQE------YMGHSEETLEV-FPHSYTFEDGYLHPGDAPGLGVDFDE----KLAAKYPYE 387

                         170
                  ....*....|....*..
gi 2440762425 180 RN--PLWRYEDGSVAEW 194
Cdd:PRK15072  388 PAylPVARLEDGTMWNW 404
MR_like_3 cd03328
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ...
 34-167 5.08e-10

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: 57.42  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  34 RLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLGPIALAACLhVDF 113
Cdd:cd03328   229 RERGPAGMDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVACA-VPR 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2440762425 114 VSHNAVFQEqsmgiHYNKGAELLDFVKNKedfnmEGGFFKP-LMKPGLGVEIDEA 167
Cdd:cd03328   308 LRHLEWFHD-----HVRIERMLFDGAPDP-----SGGALRPdLSRPGLGLELRAR 352
PRK15440 PRK15440
L-rhamnonate dehydratase; Provisional
 43-97 2.72e-08

L-rhamnonate dehydratase; Provisional


Pssm-ID: 185337 [Multi-domain]  Cd Length: 394  Bit Score: 52.42  E-value: 2.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2440762425  43 IAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPH 97
Cdd:PRK15440  264 VTSGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH 318
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 ...
 26-114 2.26e-06

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: 46.80  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  26 AEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCPLG---- 101
Cdd:cd03319   214 AGDDDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVEssls 293

                          90
                  ....*....|....*
gi 2440762425 102 --PIALAACLHVDFV 114
Cdd:cd03319   294 iaAAAHLAAAKADFV 308
MR_like_4 cd03329
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ...
 25-165 2.55e-06

Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.


Pssm-ID: 239445 [Multi-domain]  Cd Length: 368  Bit Score: 46.62  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  25 LAEQAEY-YPRLAAQTHIPIAAGE----RMFSRFEFKRvleAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCP 99
Cdd:cd03329   224 LREASISsYRWLAEKLDIPILGTEhsrgALESRADWVL---AGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGN 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2440762425 100 lgpiaLAACLHVDFVSHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFFKPLMKPGLGVEID 165
Cdd:cd03329   301 -----GAANLHVIAAIRNTRYYERGLLHPSQKYDVYAGYLSVLDDPVDSDGFVHVPKGPGLGVEID 361
MLE cd03318
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ...
 13-169 3.62e-06

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: 46.16  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  13 AWEEMTCL--------FAPSLAEQA------EYYPRLAAQTHIPIAAGERMFSR---FEFKRVLEAGGVAIlqpDLSHAG 75
Cdd:cd03318   198 AWDESTAIralprleaAGVELIEQPvprenlDGLARLRSRNRVPIMADESVSGPadaFELARRGAADVFSL---KIAKSG 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  76 GITECYKIAGMAEAYdvGLAPH---CPLGPIALAACLHvdfvsHNAVFQEQSMGIHYNKGAELLDFVKNKEDFNMEGGFF 152
Cdd:cd03318   275 GLRRAQKVAAIAEAA--GIALYggtMLESSIGTAASAH-----LFATLPSLPFGCELFGPLLLAEDLLEEPLAYRDGELH 347

                         170
                  ....*....|....*..
gi 2440762425 153 KPlMKPGLGVEIDEARV 169
Cdd:cd03318   348 VP-TGPGLGVRLDEDKV 363
mandelate_racemase cd03321
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ...
 23-169 5.28e-06

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: 45.94  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  23 PSLAEQAEYYPRLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHcplgp 102
Cdd:cd03321   220 PTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH----- 294

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2440762425 103 ialaaclhvdfvshnaVFQEQSMGI-------HYNKGAELLDFVKnKEDFNMEGGFFKPLMKPGLGVEIDEARV 169
Cdd:cd03321   295 ----------------LFQEISAHLlavtptaHWLEYVDWAGAIL-EPPLKFEDGNAVIPDEPGNGIIWREKAV 351
rTSbeta_L-fuconate_dehydratase cd03324
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ...
 37-97 3.49e-05

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: 43.49  E-value: 3.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2440762425  37 AQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPH 97
Cdd:cd03324   291 APLPIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVCPH 351
D-glucarate_dehydratase cd03323
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ...
 34-175 7.96e-05

D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD 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 that is stabilized by coordination to the essential Mg2+ ion.


Pssm-ID: 239439 [Multi-domain]  Cd Length: 395  Bit Score: 42.31  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2440762425  34 RLAAQTHIPIAAGERMFSRFEFKRVLEAGGVAILQPDLSHAGGITECYKIAGMAEAYDVGLAPHCP--LGpIALAACLHV 111
Cdd:cd03323   255 EFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNnhLG-ISLAMMTHV 333

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2440762425 112 DFVSHNAVFqeqSMGIHYNKGAEllDFVKnKEDFNMEGGFFKPLMKPGLGVEIDEARVIELSKN 175
Cdd:cd03323   334 AAAAPGLIT---ACDTHWIWQDG--QVIT-GEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHEL 391
 
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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