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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)DescriptionActionsGraphical viewLength
    Active sitei110Nucleophile1 Publication1
    Binding sitei111Substrate1
    Binding sitei114Substrate1
    Sitei134Important for enzyme activity1
    Binding sitei155Substrate1
    Binding sitei156Substrate1
    Binding sitei219Substrate1
    Active sitei280Proton acceptor1 Publication1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciRPAL258594:G13CN-1175-MONOMER.

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi40F → A: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication1
    Mutagenesisi110D → N: Loss of enzyme activity. 1 Publication1
    Mutagenesisi155H → N: Reduced catalytic rate with fluoroacetate, but increased catalytic rate with chloroacetate. Minor effect on substrate affinity. 1 Publication1
    Mutagenesisi156W → H: Reduced catalytic rate. Reduced substrate affinity. 1 Publication1
    Mutagenesisi185W → F: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication1
    Mutagenesisi219Y → F: Reduced catalytic rate. Minor effect on substrate affinity. 1 Publication1
    Mutagenesisi280H → N: Abolishes hydrolysis of covalent reaction intermediate. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003985841 – 302Fluoroacetate dehalogenaseAdd BLAST302

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi258594.RPA1163.

    Structurei

    Secondary structure

    1302
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi12 – 16Combined sources5
    Beta strandi23 – 29Combined sources7
    Beta strandi31 – 37Combined sources7
    Helixi44 – 49Combined sources6
    Helixi51 – 55Combined sources5
    Beta strandi58 – 63Combined sources6
    Helixi81 – 83Combined sources3
    Helixi85 – 98Combined sources14
    Beta strandi102 – 109Combined sources8
    Helixi111 – 122Combined sources12
    Helixi124 – 126Combined sources3
    Beta strandi127 – 134Combined sources8
    Helixi138 – 144Combined sources7
    Helixi147 – 152Combined sources6
    Helixi155 – 159Combined sources5
    Helixi165 – 170Combined sources6
    Helixi174 – 184Combined sources11
    Beta strandi186 – 191Combined sources6
    Helixi196 – 206Combined sources11
    Helixi209 – 223Combined sources15
    Helixi225 – 236Combined sources12
    Beta strandi244 – 249Combined sources6
    Turni254 – 257Combined sources4
    Helixi261 – 267Combined sources7
    Beta strandi268 – 278Combined sources11
    Helixi282 – 285Combined sources4
    Helixi287 – 299Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ6NAM1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6NAM1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini32 – 270AB hydrolase-1Sequence analysisAdd BLAST239

    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
    PDB 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.
    SMRiQ6NAM1.
    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.

    Enzyme and pathway databases

    BioCyciRPAL258594:G13CN-1175-MONOMER.

    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: November 2, 2016
    This is version 74 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.