Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C2.B: Phosphomannomutase and Phosphatase Like

  ⌊ C2.B.4: PGP Like

     ⌊ Family phosphoglycolate phosphatase 3

  ⌊ FunctionalDomain phosphoglycolate phosphatase 3 (ID 275445)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermoplasma acidophilum Taxon ID: 2303 499203062 WP_010900602.1 (RefSeq)
Thermoplasma acidophilum DSM 1728 Taxon ID: 273075 46396657 URP
Thermoplasma acidophilum Taxon ID: 2303 10639319

Uniprot

Protein NameAccessionEC Number Identifier
Phosphoglycolate phosphatase Q9HLQ2 3.1.3.18 PGP_THEAC (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 224 | Length of Functional Domain: 224

1       10        20        30        40        50        60

MIRLAAIDVDGTLTDRDRLISTKAIESIRSAEKKGLTVSLLSGNVIPVVYALKIFLGING
PVFGENGGIMFDNDGSIKKFFSNEGTNKFLEEMSKRTSMRSILTNRWREASTGFDIDPED
VDYVRKEAESRGFVIFYSGYSWHLMNRGEDKAFAVNKLKEMYSLEYDEILVIGDSNNDMP
MFQLPVRKACPANATDNIKAVSDFVSDYSYGEEIGQIFKHFELM
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
8 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:14555659
10 Asp (D) side chain general acid, sometimes general base, Mg2+ ligand metal ligand -- binding,
proton relay -- reactant 		ISS
151 Lys (K) side chain Binds phosphate, increasing electrophilicity of phosphorous for nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:14555659
174 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659
178 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of substrate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:14555659
10 Asp (D) side chain None -- ISS
18 Arg (R) side chain Stabilizes closed conformation of enzyme electrostatic stabiliser -- spectator ICS PubMed:14555659
138 Ser (S) side chain Binds phosphate, increasing electrophilicity of phosphorous for nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:14555659
151 Lys (K) side chain Binds phosphate, increasing electrophilicity of phosphorous for nucleophilic attack increase electrophilicity -- spectator,
substrate binding -- binding 		ICS PubMed:14555659
174 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659
175 Ser (S) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659
178 Asp (D) side chain Mg2+ ligand metal ligand -- binding ICS PubMed:14555659

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1L6R Crystal Structure Of Thermoplasma Acidophilum 0175 (Apc0014) Hypothetical Protein Ta0175 1 1.4 Calcium Ion • Formic Acid CSA • PDB • PDBSum
1KYT Crystal Structure Of Thermoplasma Acidophilum 0175 (Apc014) Hypothetical Protein Ta0175 1 1.7 Yes Selenomethionine • Calcium 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, 12:50 p.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.