Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

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

  ⌊ C1.5.6: HAD, Beta-PGM, Phosphatase Like

     ⌊ Family 2-haloacid dehalogenase

  ⌊ FunctionalDomain 2-haloacid dehalogenase (ID 2238)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pseudomonas sp. YL Taxon ID: 66693 157834412
Pseudomonas sp. YL Taxon ID: 66693 157834411

Uniprot

Protein NameAccessionEC Number Identifier
(S)-2-haloacid dehalogenase Q53464 3.8.1.2 HAD_PSEUY (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 232 | Length of Functional Domain: 228

1       10        20        30        40        50        60

MDYIKGIAFDLYGTLFDVHSVVGRCDEAFPGRGREISALWRQKQLEYTWLRSLMNRYVNF
QQATEDALRFTCRHLGLDLDARTRSTLCDAYLRLAPFSEVPDSLRELKRRGLKLAILSNG
SPQSIDAVVSHAGLRDGFDHLLSVDPVQVYKPDNRVYELAEQALGLDRSAILFVASNAWD
ATGARYFGFPTCWINRTGNVFEEMGQTPDWEVTSLRAVVELFETAAGKAEKG
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
10 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
118 Ser (S) side chain interacts with substrate/intermediate substrate binding -- binding ISS
Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
10 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding 		ICS PubMed:12081483
151 Lys (K) side chain None -- ICS PubMed:10956028 PubMed:12081483
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
10 Asp (D) side chain nucleophile: attacks C2 of substrate to form covalent intermediate covalent catalysis -- reactant IDA PubMed:7629151
14 Thr (T) side chain None -- IDA PubMed:7490277
118 Ser (S) side chain stabilizes COOH of intermediate electrostatic stabiliser -- spectator ICS PubMed:9614112
151 Lys (K) side chain None -- IDA PubMed:7490277
157 Tyr (Y) side chain None -- IDA PubMed:7490277
180 Asp (D) side chain hydrolysis of ester intermediate proton relay -- reactant IDA PubMed:7490277

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1ZRN Intermediate Structure Of L-2-Haloacid Dehalogenase With Monochloroacetate L-2-Haloacid Dehalogenase 2 1.83 Yes Acetic Acid CSA • PDB • PDBSum
1ZRM Crystal Structure Of The Reaction Intermediate Of L-2-Haloacid Dehalogenase With 2-Chloro-N-Butyrate L-2-Haloacid Dehalogenase 2 2.0 Yes Butanoic Acid CSA • PDB • PDBSum
1JUD L-2-Haloacid Dehalogenase L-2-Haloacid Dehalogenase 2 2.5 CSA • PDB • PDBSum
1QH9 Enzyme-Product Complex Of L-2-Haloacid Dehalogenase 2-Haloacid Dehalogenase 2 2.5 Lactic Acid 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.
EC number assigned by UniProtKB accession ID.