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Protein

Haloalkane dehalogenase

Gene

dhaA

Organism
Rhodococcus sp. (strain TDTM0003)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).

Catalytic activityi

1-haloalkane + H2O = a primary alcohol + halide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411Halide
Active sitei106 – 1061Nucleophile
Binding sitei107 – 1071Halide
Active sitei130 – 1301Proton donor
Active sitei272 – 2721Proton acceptor

GO - Molecular functioni

  1. haloalkane dehalogenase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Haloalkane dehalogenase (EC:3.8.1.5)
Gene namesi
Name:dhaA
OrganismiRhodococcus sp. (strain TDTM0003)
Taxonomic identifieri269091 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Haloalkane dehalogenasePRO_0000216777Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 175Combined sources
Beta strandi20 – 289Combined sources
Beta strandi30 – 334Combined sources
Beta strandi35 – 384Combined sources
Helixi45 – 484Combined sources
Turni49 – 513Combined sources
Helixi52 – 554Combined sources
Turni56 – 583Combined sources
Beta strandi61 – 644Combined sources
Helixi81 – 9414Combined sources
Beta strandi99 – 1057Combined sources
Helixi107 – 11812Combined sources
Helixi120 – 1223Combined sources
Beta strandi123 – 1308Combined sources
Helixi138 – 1403Combined sources
Helixi143 – 15210Combined sources
Helixi157 – 1626Combined sources
Helixi167 – 1704Combined sources
Helixi172 – 1754Combined sources
Beta strandi177 – 1793Combined sources
Helixi183 – 1908Combined sources
Helixi191 – 1933Combined sources
Helixi196 – 1994Combined sources
Helixi200 – 2089Combined sources
Helixi216 – 23116Combined sources
Beta strandi236 – 2438Combined sources
Beta strandi245 – 2473Combined sources
Helixi249 – 25810Combined sources
Beta strandi262 – 27211Combined sources
Helixi274 – 2763Combined sources
Helixi279 – 28911Combined sources
Helixi290 – 2934Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BN6X-ray1.50A1-293[»]
1BN7X-ray1.50A1-293[»]
1CQWX-ray1.50A4-293[»]
ProteinModelPortaliP59336.
SMRiP59336. Positions 4-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59336.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01231. Haloalk_dehal_type2.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P59336-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN
60 70 80 90 100
IIPHVAPSHR CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV
110 120 130 140 150
VLVIHDWGSA LGFHWAKRNP ERVKGIACME FIRPIPTWDE WPEFARETFQ
160 170 180 190 200
AFRTADVGRE LIIDQNAFIE GVLPKCVVRP LTEVEMDHYR EPFLKPVDRE
210 220 230 240 250
PLWRFPNEIP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW GTPGVLIPPA
260 270 280 290
EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PGLA
Length:294
Mass (Da):33,331
Last modified:February 22, 2003 - v1
Checksum:i190E6B9944E5DBEF
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BN6X-ray1.50A1-293[»]
1BN7X-ray1.50A1-293[»]
1CQWX-ray1.50A4-293[»]
ProteinModelPortaliP59336.
SMRiP59336. Positions 4-294.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP59336.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01231. Haloalk_dehal_type2.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiDHAA_RHOSD
AccessioniPrimary (citable) accession number: P59336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: February 22, 2003
Last modified: April 1, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.