Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fluoroacetate dehalogenase

Gene

RPA1163

Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic defluorination of fluoroacetate to produce glycolate. Has lower activity towards bromoacetate and chloroacetate.2 Publications

Catalytic activityi

Haloacetate + H2O = glycolate + halide.2 Publications

Kineticsi

  1. KM=3.3 mM for fluoroacetate2 Publications
  2. KM=1.4 mM for chloroacetate2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei110 – 1101Nucleophile1 Publication
    Binding sitei111 – 1111Substrate
    Binding sitei114 – 1141Substrate
    Sitei134 – 1341Important for enzyme activity
    Binding sitei155 – 1551Substrate
    Binding sitei156 – 1561Substrate
    Binding sitei219 – 2191Substrate
    Active sitei280 – 2801Proton acceptor1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    ESTHERirhopa-q6nam1. Haloacetate_dehalogenase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fluoroacetate dehalogenase (EC:3.8.1.3)
    Gene namesi
    Ordered Locus Names:RPA1163
    OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
    Taxonomic identifieri258594 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
    Proteomesi
    • UP000001426 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401F → A: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication
    Mutagenesisi110 – 1101D → N: Loss of enzyme activity. 1 Publication
    Mutagenesisi155 – 1551H → N: Reduced catalytic rate with fluoroacetate, but increased catalytic rate with chloroacetate. Minor effect on substrate affinity. 1 Publication
    Mutagenesisi156 – 1561W → H: Reduced catalytic rate. Reduced substrate affinity. 1 Publication
    Mutagenesisi185 – 1851W → F: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication
    Mutagenesisi219 – 2191Y → F: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication
    Mutagenesisi280 – 2801H → N: Abolishes hydrolysis of covalent reaction intermediate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 302302Fluoroacetate dehalogenasePRO_0000398584Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi258594.RPA1163.

    Structurei

    Secondary structure

    1
    302
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 165Combined sources
    Beta strandi23 – 297Combined sources
    Beta strandi31 – 377Combined sources
    Helixi44 – 496Combined sources
    Helixi51 – 555Combined sources
    Beta strandi58 – 636Combined sources
    Helixi81 – 833Combined sources
    Helixi85 – 9814Combined sources
    Beta strandi102 – 1098Combined sources
    Helixi111 – 12212Combined sources
    Helixi124 – 1263Combined sources
    Beta strandi127 – 1348Combined sources
    Helixi138 – 1447Combined sources
    Helixi147 – 1526Combined sources
    Helixi155 – 1595Combined sources
    Helixi165 – 1706Combined sources
    Helixi174 – 18411Combined sources
    Beta strandi186 – 1916Combined sources
    Helixi196 – 20611Combined sources
    Helixi209 – 22315Combined sources
    Helixi225 – 23612Combined sources
    Beta strandi244 – 2496Combined sources
    Turni254 – 2574Combined sources
    Helixi261 – 2677Combined sources
    Beta strandi268 – 27811Combined sources
    Helixi282 – 2854Combined sources
    Helixi287 – 29913Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3R3UX-ray1.60A/B/C/D1-302[»]
    3R3VX-ray1.50A/B1-302[»]
    3R3WX-ray1.60A/B1-302[»]
    3R3XX-ray1.80A/B1-302[»]
    3R3YX-ray1.15A/B1-302[»]
    3R3ZX-ray1.70A/B/C/D1-302[»]
    3R40X-ray1.05A/B1-302[»]
    3R41X-ray1.05A/B1-302[»]
    ProteinModelPortaliQ6NAM1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6NAM1.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EBM. Bacteria.
    COG0596. LUCA.
    HOGENOMiHOG000028073.
    KOiK01561.
    OMAiHAMWHRL.
    OrthoDBiPOG091H0K3A.
    PhylomeDBiQ6NAM1.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6NAM1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPDLADLFPG FGSEWINTSS GRIFARVGGD GPPLLLLHGF PQTHVMWHRV
    60 70 80 90 100
    APKLAERFKV IVADLPGYGW SDMPESDEQH TPYTKRAMAK QLIEAMEQLG
    110 120 130 140 150
    HVHFALAGHD RGARVSYRLA LDSPGRLSKL AVLDILPTYE YWQRMNRAYA
    160 170 180 190 200
    LKIYHWSFLA QPAPLPENLL GGDPDFYVKA KLASWTRAGD LSAFDPRAVE
    210 220 230 240 250
    HYRIAFADPM RRHVMCEDYR AGAYADFEHD KIDVEAGNKI PVPMLALWGA
    260 270 280 290 300
    SGIAQSAATP LDVWRKWASD VQGAPIESGH FLPEEAPDQT AEALVRFFSA

    AP
    Length:302
    Mass (Da):33,692
    Last modified:July 5, 2004 - v1
    Checksum:i3A1FAE748CF25167
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX572596 Genomic DNA. Translation: CAE26606.1.
    RefSeqiWP_011156727.1. NC_005296.1.

    Genome annotation databases

    EnsemblBacteriaiCAE26606; CAE26606; RPA1163.
    KEGGirpa:RPA1163.
    PATRICi23286549. VBIRhoPal84835_1215.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BX572596 Genomic DNA. Translation: CAE26606.1.
    RefSeqiWP_011156727.1. NC_005296.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3R3UX-ray1.60A/B/C/D1-302[»]
    3R3VX-ray1.50A/B1-302[»]
    3R3WX-ray1.60A/B1-302[»]
    3R3XX-ray1.80A/B1-302[»]
    3R3YX-ray1.15A/B1-302[»]
    3R3ZX-ray1.70A/B/C/D1-302[»]
    3R40X-ray1.05A/B1-302[»]
    3R41X-ray1.05A/B1-302[»]
    ProteinModelPortaliQ6NAM1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi258594.RPA1163.

    Protein family/group databases

    ESTHERirhopa-q6nam1. Haloacetate_dehalogenase.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAE26606; CAE26606; RPA1163.
    KEGGirpa:RPA1163.
    PATRICi23286549. VBIRhoPal84835_1215.

    Phylogenomic databases

    eggNOGiENOG4105EBM. Bacteria.
    COG0596. LUCA.
    HOGENOMiHOG000028073.
    KOiK01561.
    OMAiHAMWHRL.
    OrthoDBiPOG091H0K3A.
    PhylomeDBiQ6NAM1.

    Miscellaneous databases

    EvolutionaryTraceiQ6NAM1.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDEHA_RHOPA
    AccessioniPrimary (citable) accession number: Q6NAM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: July 5, 2004
    Last modified: September 7, 2016
    This is version 73 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, Complete proteome, Reference proteome

    Documents

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

    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 one 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.