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P59336

- DHAA_RHOSD

UniProt

P59336 - DHAA_RHOSD

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Protein
Haloalkane dehalogenase
Gene
dhaA
Organism
Rhodococcus sp. (strain TDTM0003)
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. Has a broad substrate specificity, which includes primary, secondary and cyclic haloalkanes (chain length > C4).UniRule annotation

Catalytic activityi

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

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...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    MEROPSiS33.990.

    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 dehalogenaseUniRule annotation
    PRO_0000216777Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer By similarity.UniRule annotation

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 175
    Beta strandi20 – 289
    Beta strandi30 – 334
    Beta strandi35 – 384
    Helixi45 – 484
    Turni49 – 513
    Helixi52 – 554
    Turni56 – 583
    Beta strandi61 – 644
    Helixi81 – 9414
    Beta strandi99 – 1057
    Helixi107 – 11812
    Helixi120 – 1223
    Beta strandi123 – 1308
    Helixi138 – 1403
    Helixi143 – 15210
    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 – 2763
    Helixi279 – 28911
    Helixi290 – 2934

    3D structure databases

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

    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.
    IPR000639. Epox_hydrolase-like.
    IPR023594. Haloalkane_dehalogenase_2.
    [Graphical view]
    PRINTSiPR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P59336-1 [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 GVLPKCVVRP LTEVEMDHYR EPFLKPVDRE 200
    PLWRFPNEIP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW GTPGVLIPPA 250
    EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PGLA 294
    Length:294
    Mass (Da):33,331
    Last modified:February 22, 2003 - v1
    Checksum:i190E6B9944E5DBEF
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BN6 X-ray 1.50 A 1-293 [» ]
    1BN7 X-ray 1.50 A 1-293 [» ]
    1CQW X-ray 1.50 A 4-293 [» ]
    ProteinModelPortali P59336.
    SMRi P59336. Positions 4-294.
    ModBasei Search...

    Protein family/group databases

    MEROPSi S33.990.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P59336.

    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. 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: July 9, 2014
    This is version 52 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

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