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 22500)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Xanthobacter autotrophicus Taxon ID: 280 3122178
Xanthobacter autotrophicus Taxon ID: 280 2914421
Xanthobacter autotrophicus Taxon ID: 280 2914420

Uniprot

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

Sequence

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

1       10        20        30        40        50        60

MIKAVVFDAYGTLFDVQSVADATERAYPGRGEYITQVWRQKQLEYSWLRALMGRYADFWG
VTREALAYTLGTLGLEPDESFLADMAQAYNRLTPYPDAAQCLAELAPLKRAILSNGAPDM
LQALVANAGLTDSFDAVISVDAKRVFKPHPDSYALVEEVLGVTPAEVLFVSSNGFDVGGA
KNFGFSVARVARLSQEALARELVSGTIAPLTMFKALRMREETYAEAPDFVVPALGDLPRL
VRGMAGAHLAPAV
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 PubMed:12081483
147 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
8 Asp (D) side chain nucleophile: attacks C2 of substrate to form covalent intermediate covalent catalysis -- reactant IDA PubMed:7629151
12 Thr (T) side chain None -- IDA PubMed:7490277
114 Ser (S) side chain stabilizes COOH of intermediate electrostatic stabiliser -- spectator ICS PubMed:9614112
147 Lys (K) side chain None -- IDA PubMed:7490277
153 Tyr (Y) side chain None -- IDA PubMed:7490277
176 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
1AQ6 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus L-2-Haloacid Dehalogenase 5 1.95 Formic Acid CSA • PDB • PDBSum
1QQ5 Structure Of L-2-Haloacid Dehalogenase From Xanthobacter Autotrophicus Protein (L-2-Haloacid Dehalogenase) 5 1.52 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, 10:11 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.