Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  ⌊ C1.5.4: Enolase-phosphatase Like

  ⌊ FunctionalDomain C1.5.4: Enolase-phosphatase Like (ID 309380)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onFeb. 13, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Macaca fascicularis Taxon ID: 9541 355760742 EHH61711.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a G8F347 G8F347_MACFA (TrEMBL)

Sequence

Length of Enzyme (full-length): 223 | Length of Functional Domain: 220

1       10        20        30        40        50        60

MYNNVDILFPYIEENVKEYLQTHWEEEECQQDVSLLRKQAEEDAHLDGAVPIPAASGNGV
DDLQQMIQAVVDNVCWQMSLDRKTTALKQLQGHMWRAAFTAGRMKAEFFADVVPAVRKWR
EAGMKVYIYSSGSVEAQKLLFGHSTEGDILELVDGHFDTKIGRKVESESYRKIADSIGCS
TNNILFLTDVTREASAAEEADVHVAVVVRPGNAGLTDDDPCSV
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 1/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
130 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 4/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
131 Ser (S) side chain binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:15843022
164 Lys (K) side chain Forms salt bridge with nucleophilic Asp; binds phosphate moiety of substrate to increase elecrophilicity and facilitate nucleophilic attack -- ICS PubMed:15843022
189 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15843022
193 Glu (E) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15843022

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1YNS Crystal Structure Of Human Enolase-Phosphatase E1 And Its Complex With A Substrate Analog E-1 Enzyme 14 1.7 Magnesium Ion • 2-Oxoheptylphosphonic Acid CSA • PDB • PDBSum
1ZS9 Crystal Structure Of Human Enolase-Phosphatase E1 E-1 Enzyme 12 1.7 Selenomethionine • Magnesium Ion 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
Aug. 1, 2014, 2:07 p.m. update curation agent sbrown setDomainBoundaries.py
Feb. 11, 2017, 4 a.m. update domain end position 222 223
EC number assigned by UniProtKB accession ID.