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 2239)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES
This entry was last updated onJune 3, 2017

References to Other Databases

Genbank

SpeciesGIAccessionModel
Xanthobacter autotrophicus 6435583 MB
Xanthobacter autotrophicus 6435582 MB

Uniprot

Protein NameAccessionEC Number IdentifierModel
(S)-2-haloacid dehalogenase Q60099 3.8.1.2 HAD_XANAU (Swiss-Prot) MB

Sequence

Length of Enzyme (full-length): 253 | Length of Functional Domain: 247

1       10        20        30        40        50        60

MIKAVVFDAYGTLFDVQSVADATERAYPGRGEYITQVWRQKQLEYSWLRALMGRYADFWS
VTREALAYTLGTLGLEPDESFLADMAQAYNRLTPYPDAAQCLAELAPLKRAILSNGAPDM
LQALVANAGLTDSFDAVISVDAKRVFKPHPDSYALVEEVLGVTPAEVLFVSSNGFDVGGA
KNFGFSVARVARLSQEALARELVSGTIAPLTMFKALRMREETYAEAPDFVVPALGDLPRL
VRGMAGA
HLAPAV

FASTA | BLAST | HMM

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
8 Asp (D) side chain nucleophile: forms covalent intermediate covalent catalysis -- reactant ISS
114 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
8 Asp (D) side chain Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
ICS
147 Lys (K) side chain None -- ICS
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Asp (D) side chain nucleophile: attacks C2 of substrate to form covalent intermediate covalent catalysis -- reactant IDA
12 Thr (T) side chain None -- IDA
114 Ser (S) side chain stabilizes COOH of intermediate electrostatic stabiliser -- spectator ICS
147 Lys (K) side chain None -- IDA
153 Tyr (Y) side chain None -- IDA
176 Asp (D) side chain hydrolysis of ester intermediate proton relay -- reactant IDA

Catalyzed Reaction

(S)-2-haloacid dehalogenase (configuration-inverting)

+ +
(S)-2-haloacid
15791
water
15377
(2R)-2-hydroxy monocarboxylic acid
17893
halide anion
16042

EC: 3.8.1.2 | IntEnz: 3.8.1.2 | Kegg: 3.8.1.2 | BioCyc: 3.8.1.2 | BRENDA: 3.8.1.2

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
1QQ5 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus Protein (L-2-Haloacid Dehalogenase) 5 1.52 Formic Acid CSA • PDB • PDBSum
1AQ6 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus L-2-Haloacid Dehalogenase 5 1.95 Formic Acid CSA • PDB • PDBSum
1QQ7 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus With Chloropropionic Acid Covalently Bound Protein (L-2-Haloacid Dehalogenase) 5 1.7 Aspartic Acid-4-Carboxymethyl Ester • Chloride Ion CSA • PDB • PDBSum
1QQ6 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus With Chloroacetic Acid Covalently Bound Protein (L-2-Haloacid Dehalogenase) 5 2.1 Aspartic Acid-4-Carboxymethyl Ester • Chloride 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
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.