Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.4: Enolase-phosphatase Like

     ⌊ Family enolase-phosphatase

  ⌊ FunctionalDomain enolase-phosphatase (ID 125440)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IEA
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Callithrix jacchus Taxon ID: 9483 296196168 XP_002745713.1 (RefSeq) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a F7IAF2 F7IAF2_CALJA (TrEMBL)

Sequence

Length of Enzyme (full-length): 261 | Length of Functional Domain: 261

1       10        20        30        40        50        60

MVVLSVPAEVTVILLDIEGTTTPIAFVKDILFPYIEKNVKEYLQTHWEEEECQQDVSLLR
KQAEEDAHLDGAVPIPAASGSGMDDLQQMIQAVVDNVCWQMSLDRKTTALKQLQGHMWRT
AFTAGLMKAEFFADVVPAVRKWREAGMKVYVYSSGSVEAQKLLFGHSTEGDILELVDGHF
DTKIGRKVESESYRKIADSIGCSTNNILFLTDVTREASAAEEADVHVAVVVRPGNAGLTD
DEKTYYSLITSFSELYLPSST
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 2/2 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
16 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
153 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
16 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15843022
154 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
187 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
212 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15843022
216 Glu (E) side chain Mg2+ ligand (via water) metal ligand -- binding ICS PubMed:15843022
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
16 Asp (D) side chain nucleophile: attacks phosphate moiety of substrate to form covalent intermediate; Mg2+ ligand covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:15843022
20 Thr (T) side chain None -- ISS PubMed:9649311
154 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
187 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
212 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:15843022
216 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
April 30, 2014, 8:10 a.m. update curation agent sbrown setDomainBoundaries.py
update domain end position 257 261
update domain start position 5 1
EC number assigned by UniProtKB accession ID.