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Q51669

- GFA_PARDE

UniProt

Q51669 - GFA_PARDE

Protein

Glutathione-dependent formaldehyde-activating enzyme

Gene

gfa

Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.1 Publication

    Catalytic activityi

    S-(hydroxymethyl)glutathione = glutathione + formaldehyde.

    Cofactori

    Binds 2 zinc ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi31 – 311Zinc 1; structural
    Metal bindingi33 – 331Zinc 1; structural
    Metal bindingi52 – 521Zinc 2; catalytic
    Metal bindingi54 – 541Zinc 2; catalytic
    Metal bindingi57 – 571Zinc 2; catalytic
    Metal bindingi99 – 991Zinc 1; structural
    Metal bindingi102 – 1021Zinc 1; structural

    GO - Molecular functioni

    1. S-(hydroxymethyl)glutathione synthase activity Source: UniProtKB-HAMAP
    2. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. formaldehyde catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00562; UER00621.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione-dependent formaldehyde-activating enzyme (EC:4.4.1.22)
    Alternative name(s):
    S-(hydroxymethyl)glutathione synthase
    Gene namesi
    Name:gfa
    OrganismiParacoccus denitrificans
    Taxonomic identifieri266 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 194193Glutathione-dependent formaldehyde-activating enzymePRO_0000220321Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 144
    Beta strandi27 – 304
    Beta strandi34 – 363
    Beta strandi39 – 424
    Beta strandi47 – 526
    Beta strandi55 – 573
    Beta strandi64 – 729
    Helixi73 – 753
    Beta strandi76 – 805
    Helixi82 – 843
    Beta strandi85 – 884
    Beta strandi92 – 998
    Turni100 – 1023
    Beta strandi105 – 1106
    Turni116 – 1194
    Beta strandi120 – 1234
    Helixi125 – 1273
    Beta strandi138 – 1414
    Helixi142 – 1487
    Helixi152 – 1543
    Helixi155 – 16410
    Beta strandi171 – 1733
    Helixi175 – 18915
    Beta strandi190 – 1923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X6MX-ray2.35A/B/C/D2-194[»]
    1XA8X-ray2.40A/B/C/D2-194[»]
    ProteinModelPortaliQ51669.
    SMRiQ51669. Positions 1-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ51669.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Gfa family.Curated

    Family and domain databases

    Gene3Di3.90.1590.10. 1 hit.
    HAMAPiMF_00723. Formald_GSH.
    InterProiIPR014185. Formald_GSH.
    IPR006913. GFA/CENP-V.
    IPR011057. Mss4-like.
    [Graphical view]
    PfamiPF04828. GFA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF033318. Formald_GSH. 1 hit.
    SUPFAMiSSF51316. SSF51316. 1 hit.
    TIGRFAMsiTIGR02820. formald_GSH. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q51669-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AVRAQTAHNH    50
    VCGCTKCWKP EGAIFSQVAV VGRDALEVLE GAEKLEIVNA EAPIQRHRCR 100
    DCGVHMYGRI ENRDHPFYGL DFVHTELSDE DGWSAPEFAA FVSSIIESGV 150
    DPSRMEAIRA RLRELGLEPY DALSPPLMDA IATHIAKRSG ALAA 194
    Length:194
    Mass (Da):20,967
    Last modified:January 23, 2007 - v3
    Checksum:i95B6E386B1756619
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34346 Genomic DNA. Translation: AAC44550.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34346 Genomic DNA. Translation: AAC44550.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X6M X-ray 2.35 A/B/C/D 2-194 [» ]
    1XA8 X-ray 2.40 A/B/C/D 2-194 [» ]
    ProteinModelPortali Q51669.
    SMRi Q51669. Positions 1-194.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00562 ; UER00621 .

    Miscellaneous databases

    EvolutionaryTracei Q51669.

    Family and domain databases

    Gene3Di 3.90.1590.10. 1 hit.
    HAMAPi MF_00723. Formald_GSH.
    InterProi IPR014185. Formald_GSH.
    IPR006913. GFA/CENP-V.
    IPR011057. Mss4-like.
    [Graphical view ]
    Pfami PF04828. GFA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF033318. Formald_GSH. 1 hit.
    SUPFAMi SSF51316. SSF51316. 1 hit.
    TIGRFAMsi TIGR02820. formald_GSH. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?"
      Harms N., Ras J., Reijnders W.N.M., van Spanning R.J.M., Stouthamer A.H.
      J. Bacteriol. 178:6296-6299(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy."
      Goenrich M., Bartoschek S., Hagemeier C.H., Griesinger C., Vorholt J.A.
      J. Biol. Chem. 277:3069-3072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

    Entry informationi

    Entry nameiGFA_PARDE
    AccessioniPrimary (citable) accession number: Q51669
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 70 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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