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P0A3G2

- DHAA_RHORH

UniProt

P0A3G2 - DHAA_RHORH

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Protein
Haloalkane dehalogenase
Gene
dhaA
Organism
Rhodococcus rhodochrous
Status
Reviewed - 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. Expresses halogenase activity against 1-chloroalkanes of chain length C3 to C10, and also shows a very weak activity with 1,2-dichloroethane.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Nucleophile By similarity
Active sitei130 – 1301Proton donor By similarity
Active sitei272 – 2721Proton acceptor By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

SABIO-RKP0A3G2.
UniPathwayiUPA00007.

Names & Taxonomyi

Protein namesi
Recommended name:
Haloalkane dehalogenase (EC:3.8.1.5)
Gene namesi
Name:dhaA
Encoded oniPlasmid pRTL10 Publication
OrganismiRhodococcus rhodochrous
Taxonomic identifieri1829 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Haloalkane dehalogenaseUniRule annotation
PRO_0000216775Add
BLAST

Expressioni

Inductioni

By 1-haloalkanes.UniRule annotation

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 175
Beta strandi20 – 289
Beta strandi30 – 323
Beta strandi35 – 384
Helixi45 – 484
Turni49 – 513
Helixi52 – 554
Turni56 – 583
Beta strandi61 – 644
Helixi81 – 9414
Beta strandi99 – 1057
Helixi106 – 11813
Helixi120 – 1223
Beta strandi123 – 1308
Beta strandi135 – 1373
Helixi138 – 1403
Helixi143 – 1453
Helixi146 – 1527
Beta strandi154 – 1563
Helixi157 – 1626
Helixi167 – 1704
Helixi172 – 1754
Beta strandi177 – 1793
Helixi183 – 1908
Helixi191 – 1933
Helixi196 – 1994
Helixi200 – 2089
Helixi216 – 23116
Beta strandi236 – 2438
Beta strandi245 – 2473
Helixi249 – 25810
Beta strandi262 – 27211
Helixi274 – 2774
Helixi279 – 28911
Helixi291 – 2933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V9ZX-ray3.00A1-11[»]
A142-293[»]
3FBWX-ray1.23A1-293[»]
3RK4X-ray1.31A1-293[»]
3SK0X-ray1.78A1-293[»]
4E46X-ray1.26A1-293[»]
4F5ZX-ray1.20A1-293[»]
4F60X-ray1.45A1-293[»]
4FWBX-ray1.26A4-293[»]
ProteinModelPortaliP0A3G2.
SMRiP0A3G2. Positions 4-293.

Miscellaneous databases

EvolutionaryTraceiP0A3G2.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P0A3G2-1 [UniParc]FASTAAdd to Basket

« Hide

MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN    50
IIPHVAPSHR CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV 100
VLVIHDWGSA LGFHWAKRNP ERVKGIACME FIRPIPTWDE WPEFARETFQ 150
AFRTADVGRE LIIDQNAFIE GALPKCVVRP LTEVEMDHYR EPFLKPVDRE 200
PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW GTPGVLIPPA 250
EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PAL 293
Length:293
Mass (Da):33,246
Last modified:March 15, 2005 - v1
Checksum:i2B637C53E36BE9F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060871 Genomic DNA. Translation: AAC15838.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF060871 Genomic DNA. Translation: AAC15838.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V9Z X-ray 3.00 A 1-11 [» ]
A 142-293 [» ]
3FBW X-ray 1.23 A 1-293 [» ]
3RK4 X-ray 1.31 A 1-293 [» ]
3SK0 X-ray 1.78 A 1-293 [» ]
4E46 X-ray 1.26 A 1-293 [» ]
4F5Z X-ray 1.20 A 1-293 [» ]
4F60 X-ray 1.45 A 1-293 [» ]
4FWB X-ray 1.26 A 4-293 [» ]
ProteinModelPortali P0A3G2.
SMRi P0A3G2. Positions 4-293.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00007 .
SABIO-RK P0A3G2.

Miscellaneous databases

EvolutionaryTracei P0A3G2.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
HAMAPi MF_01231. Haloalk_dehal_type2.
InterProi IPR029058. AB_hydrolase.
IPR000639. Epox_hydrolase-like.
IPR023594. Haloalkane_dehalogenase_2.
[Graphical view ]
PRINTSi PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064."
    Kulakova A.N., Larkin M.J., Kulakov L.A.
    Microbiology 143:109-115(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCIMB 13064.

Entry informationi

Entry nameiDHAA_RHORH
AccessioniPrimary (citable) accession number: P0A3G2
Secondary accession number(s): Q53042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: July 9, 2014
This is version 41 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, Plasmid

Documents

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

External Data

Dasty 3

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