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 2322)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code ISS PubMed:1512562
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Delftia acidovorans Taxon ID: 80866 34500480 NP_904251.1 (RefSeq) URP
Delftia acidovorans Taxon ID: 80866 695208401 YP_009077274.1 (RefSeq) URP
Delftia acidovorans Taxon ID: 80866 695208397 YP_009077271.1 (RefSeq) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Haloacetate dehalogenase H-2 Q01399 3.8.1.3 DEH2_MORSB (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MKKIEAIAFDMYGTLYDVHSVVDACEKQYPGKGKDISVLWRQKQLEYAWLRCLMGQYIKF
EEATANALTYTCNQMKLDCDEGSAMRLTEEYLRLKPFPEVRGALRALRQRGMRLAILSNG
STETIHDVVHNSGVEGEFEHLISVDSARAYKPHPLAYELGEEAFGISRESILFVSSNPWD
VSGAKAFGYQVCWINRYGFAFDELGQTPDFTVPVMDAIVHLIAV
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

haloacetate dehalogenase

+ + +
haloacetate
16277		 water
15377		 glycolate
29805		 halide
37578		 hydron
15378

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

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.