Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup enolase

     ⌊ Family enolase

  ⌊ FunctionalDomain enolase 1 (ID 114)

Superfamily Assignment Evidence Code(s) FSM PubMed:8987982
Family Assignment Evidence Code ISS PubMed:7005235
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Saccharomyces cerevisiae YJM1389 Taxon ID: 1294361 766994714 AJS28021.1 (Genbank) URP
Saccharomyces cerevisiae YJM1388 Taxon ID: 1294360 766994217 AJS27526.1 (Genbank) URP
Saccharomyces cerevisiae YJM1326 Taxon ID: 1294347 766955448 AJS21061.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Enolase 1 P00924 4.2.1.11 ENO1_YEAST (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 437 | Length of Functional Domain: 421

1       10        20        30        40        50        60

MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGK
GVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASR
AAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTF
AEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDG
KVKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFA
EDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAA
QDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEEL
GDNAVFAGENFHHGDKL
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
247 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
296 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
321 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
212 Glu (E) side chain acid (promotes elim of OH) proton relay -- reactant IDA PubMed:8634301
247 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
296 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
321 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
346 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant IDA PubMed:8634301
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
40 Ser (S) side chain metal binding ligand (2nd metal) metal ligand -- binding ICS PubMed:11434770
212 Glu (E) side chain acid (promotes elimination of OH) proton relay -- reactant IDA PubMed:8634301
247 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
296 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
321 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:8605183
346 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant IDA PubMed:8634301

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1EBG Chelation Of Ser 39 To Mg2+ Latches A Gate At The Active Site Of Enolase: Structure Of The Bis(Mg2+) Complex Of Yeast Enolase And The Intermediate Analog Phosphonoacetohydroxamate At 2.1 Angstroms Resolution Enolase 64 2.1 Magnesium Ion • Phosphonoacetohydroxamic Acid CSA • PDB • PDBSum
1EBH Octahedral Coordination At The High Affinity Metal Site In Enolase; Crystallographic Analysis Of The Mg++-Enzyme From Yeast At 1.9 Angstroms Resolution Enolase 64 1.9 Chloride Ion • Magnesium Ion CSA • PDB • PDBSum
2AL1 Crystal Structure Analysis Of Enolase Mg Subunit Complex At Ph 8.0 Enolase 1 64 1.5 Magnesium Ion
(4 more ⇓) 		CSA • PDB • PDBSum
2ONE Asymmetric Yeast Enolase Dimer Complexed With Resolved 2'-Phosphoglycerate And Phosphoenolpyruvate Enolase 64 2.0 Magnesium Ion
(3 more ⇓) 		CSA • PDB • PDBSum
1ONE Yeast Enolase Complexed With An Equilibrium Mixture Of 2'-Phosphoglyceate And Phosphoenolpyruvate Enolase 64 1.8 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
1P48 Reverse Protonation Is The Key To General Acid-Base Catalysis In Enolase Enolase 1 64 2.0 Yes Magnesium Ion • Phosphoenolpyruvate CSA • PDB • PDBSum
1P43 Reverse Protonation Is The Key To General Acid-Base Catalysis In Enolase Enolase 1 64 1.8 Yes Magnesium Ion • 2-Phosphoglyceric Acid CSA • PDB • PDBSum
1L8P Mg-Phosphonoacetohydroxamate Complex Of S39A Yeast Enolase 1 Enolase 1 64 2.1 Yes Magnesium Ion • Phosphonoacetohydroxamic Acid CSA • PDB • PDBSum
7ENL Mechanism Of Enolase: The Crystal Structure Of Enolase-Mg2+-Phosphoglycerate(Slash) Phosphoenolpyruvate Complex At 2.2-Angstroms Resolution Enolase 64 2.2 Magnesium Ion • 2-Phosphoglyceric Acid CSA • PDB • PDBSum
3ENL Refined Structure Of Yeast Apo-Enolase At 2.25 Angstroms Resolution Enolase 64 2.25 Sulfate Ion CSA • PDB • PDBSum
4ENL Crystal Structure Of Holoenzyme Refined At 1.9 Angstroms Resolution: Trigonal-Bipyramidal Geometry Of The Cation Binding Site Enolase 64 1.9 Zinc Ion • Sulfate Ion CSA • PDB • PDBSum
5ENL Inhibition Of Enolase: The Crystal Structures Of Enolase-Ca2+-Phosphoglycerate And Enolase-Zn2+-Phosphoglycolate Complexes At 2.2-Angstroms Resolution Enolase 64 2.2 Calcium Ion • 2-Phosphoglyceric Acid CSA • PDB • PDBSum
6ENL Inhibition Of Enolase: The Crystal Structures Of Enolase-Ca2+-Phosphoglycerate And Enolase-Zn2+-Phosphoglycolate Complexes At 2.2-Angstroms Resolution Enolase 64 2.2 2-Phosphoglycolic Acid • Zinc Ion CSA • PDB • PDBSum
1ELS Catalytic Metal Ion Binding In Enolase: The Crystal Structure Of Enolase-Mn2+-Phosphonoacetohydroxamate Complex At 2.4 Angstroms Resolution Enolase 64 2.4 Manganese (Ii) Ion • Phosphonoacetohydroxamic Acid CSA • PDB • PDBSum
1NEL Fluoride Inhibition Of Yeast Enolase: Crystal Structure Of The Enolase-Mg2+-F--Pi Complex At 2.6-Angstroms Resolution Enolase 64 2.6 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
2AL2 Crystal Structure Analysis Of Enolase Mg Subunit Complex At Ph 8.0 Enolase 1 • Enolase 1 64 1.85 Magnesium Ion
(4 more ⇓) 		CSA • PDB • PDBSum
2XH7 Engineering The Enolase Active Site Pocket: Crystal Structure Of The D321A Mutant Of Yeast Enolase 1 Enolase 1 62 1.8 Yes Magnesium Ion • 2-Phosphoglyceric Acid CSA • PDB • PDBSum
2XGZ Engineering The Enolase Active Site Pocket: Crystal Structure Of The S39N D321R Mutant Of Yeast Enolase 1 Enolase 1 61 1.8 Yes Magnesium Ion • Phosphoenolpyruvate CSA • PDB • PDBSum
2XH2 Engineering The Enolase Active Site Pocket: Crystal Structure Of The S39N D321A Mutant Of Yeast Enolase 1 Enolase 1 61 1.8 Yes 2-Phosphoglyceric Acid • Magnesium Ion CSA • PDB • PDBSum
2XH4 Engineering The Enolase Active Site Pocket: Crystal Structure Of The S39A D321A Mutant Of Yeast Enolase 1 Enolase 1 61 1.7 Yes Magnesium Ion • 2-Phosphoglyceric Acid CSA • PDB • PDBSum
2XH0 Engineering The Enolase Active Site Pocket: Crystal Structure Of The S39N Q167K D321R Mutant Of Yeast Enolase 1 Enolase 1 60 1.7 Yes Magnesium Ion • Phosphoenolpyruvate CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.