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 2689)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:1588303
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pseudomonas putida Taxon ID: 303 151246 AAA25832.1 (Genbank) URP
Pseudomonas putida Taxon ID: 303 3122191 URP

Uniprot

Protein NameAccessionEC Number Identifier
(S)-2-haloacid dehalogenase Q52087 3.8.1.2 HADL_PSEPU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 227 | Length of Functional Domain: 227

1       10        20        30        40        50        60

MKNIQGIVFDLYGTLYDVHSVVQACEEVYPGQGDAISRLWRQKQLEYTWLRSLMGRYVNF
EKATEDALRFTCTHLGLSLDDETHQRLSDAYLHLTPYADTADAVRRLKAAGLPLGIISNG
SHCSIEQVVTNSEMNWAFDQLISVEDVQVFKPDSRVYSLAEKRMGFPKENILFVSSNAWD
ASAASNFGFPVCWINRQNGAFDELDAKPTHVVRNLAEMSNWLVNSLD
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

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

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:28 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.