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P59336 (DHAA_RHOSD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. 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:
Haloalkane dehalogenase

EC=3.8.1.5
Gene names
Name:dhaA
OrganismRhodococcus sp. (strain TDTM0003)
Taxonomic identifier269091 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes primary, secondary and cyclic haloalkanes (chain length > C4). HAMAP-Rule MF_01231

Catalytic activity

1-haloalkane + H2O = a primary alcohol + halide. HAMAP-Rule MF_01231

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01231

Sequence similarities

Belongs to the haloalkane dehalogenase family. Type 2 subfamily.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functionhaloalkane dehalogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Haloalkane dehalogenase HAMAP-Rule MF_01231
PRO_0000216777

Sites

Active site1061Nucleophile
Active site1301Proton donor
Active site2721Proton acceptor
Binding site411Halide
Binding site1071Halide

Secondary structure

.......................................................... 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59336 [UniParc].

Last modified February 22, 2003. Version 1.
Checksum: 190E6B9944E5DBEF

FASTA29433,331
        10         20         30         40         50         60 
MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR 

        70         80         90        100        110        120 
CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP 

       130        140        150        160        170        180 
ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GVLPKCVVRP 

       190        200        210        220        230        240 
LTEVEMDHYR EPFLKPVDRE PLWRFPNEIP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW 

       250        260        270        280        290 
GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PGLA 

« Hide

References

[1]"Haloalkane dehalogenases: structure of a Rhodococcus enzyme."
Newman J., Peat T.S., Richard R., Kan L., Swanson P.E., Affholter J.A., Holmes I.H., Schindler J.F., Unkefer C.J., Terwilliger T.C.
Biochemistry 38:16105-16114(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BN6X-ray1.50A1-293[»]
1BN7X-ray1.50A1-293[»]
1CQWX-ray1.50A4-293[»]
ProteinModelPortalP59336.
SMRP59336. Positions 4-294.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS33.990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
HAMAPMF_01231. Haloalk_dehal_type2.
InterProIPR029058. AB_hydrolase.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]
PRINTSPR00412. EPOXHYDRLASE.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP59336.

Entry information

Entry nameDHAA_RHOSD
AccessionPrimary (citable) accession number: P59336
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: February 22, 2003
Last modified: July 9, 2014
This is version 52 of the entry and version 1 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