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P0A3G2

- DHAA_RHORH

UniProt

P0A3G2 - DHAA_RHORH

Protein

Haloalkane dehalogenase

Gene

dhaA

Organism
Rhodococcus rhodochrous
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
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    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.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061NucleophileBy similarity
    Active sitei130 – 1301Proton donorBy similarity
    Active sitei272 – 2721Proton acceptorBy similarity

    GO - Molecular functioni

    1. haloalkane dehalogenase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. response to toxic substance Source: UniProtKB-KW

    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 dehalogenasePRO_0000216775Add
    BLAST

    Expressioni

    Inductioni

    By 1-haloalkanes.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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...
    MobiDBi 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: October 1, 2014
    This is version 42 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