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Q60099 (HAD_XANAU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(S)-2-haloacid dehalogenase

EC=3.8.1.2
Alternative name(s):
2-haloalkanoic acid dehalogenase
Halocarboxylic acid halidohydrolase
L-2-haloacid dehalogenase
Gene names
Name:dhlB
OrganismXanthobacter autotrophicus
Taxonomic identifier280 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Active with 2-halogenated carboxylic acids and converts only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate.

Catalytic activity

(S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. S-2-haloalkanoic acid dehalogenase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.5.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_function(S)-2-haloacid dehalogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 253253(S)-2-haloacid dehalogenase
PRO_0000079159

Sites

Active site81Nucleophile

Experimental info

Sequence conflict841D → G Ref.1
Sequence conflict841D → G Ref.2

Secondary structure

............................................. 253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60099 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: E2AB8DEED37A5716

FASTA25327,469
        10         20         30         40         50         60 
MIKAVVFDAY GTLFDVQSVA DATERAYPGR GEYITQVWRQ KQLEYSWLRA LMGRYADFWG 

        70         80         90        100        110        120 
VTREALAYTL GTLGLEPDES FLADMAQAYN RLTPYPDAAQ CLAELAPLKR AILSNGAPDM 

       130        140        150        160        170        180 
LQALVANAGL TDSFDAVISV DAKRVFKPHP DSYALVEEVL GVTPAEVLFV SSNGFDVGGA 

       190        200        210        220        230        240 
KNFGFSVARV ARLSQEALAR ELVSGTIAPL TMFKALRMRE ETYAEAPDFV VPALGDLPRL 

       250 
VRGMAGAHLA PAV 

« Hide

References

[1]"Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene."
van der Ploeg J., van Hall G., Janssen D.B.
J. Bacteriol. 173:7925-7933(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18.
Strain: GJ10.
[2]"Sequence analysis of the upstream region of dhlB, the gene encoding haloalkanoic acid dehalogenase of Xanthobacter autotrophicus GJ10."
van der Ploeg J., Janssen D.B.
Biodegradation 6:257-263(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
Strain: GJ10.
[3]"Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate."
Ridder I.S., Rozeboom H.J., Kalk K.H., Janssen D.B., Dijkstra B.W.
J. Biol. Chem. 272:33015-33022(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SEQUENCE REVISION TO 84.
Strain: GJ10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81691 Genomic DNA. Translation: AAA27590.1.
X86084 Genomic DNA. Translation: CAA60039.1.
PIRS52840.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ6X-ray1.95A/B1-253[»]
1QQ5X-ray1.52A/B1-253[»]
1QQ6X-ray2.10A/B1-253[»]
1QQ7X-ray1.70A/B1-253[»]
ProteinModelPortalQ60099.
SMRQ60099. Positions 1-245.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR006328. HAD_II.
IPR023198. PGP_dom2.
[Graphical view]
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00413. HADHALOGNASE.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01493. HAD-SF-IA-v2. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01428. HAD_type_II. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ60099.

Entry information

Entry nameHAD_XANAU
AccessionPrimary (citable) accession number: Q60099
Secondary accession number(s): Q56757
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 16, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references