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P68460

- GLRX2_VACCW

UniProt

P68460 - GLRX2_VACCW

Protein

Glutaredoxin-2

Gene

VACWR081

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Glutaredoxin necessary for virion morphogenesis and virus replication. Functions as a thiol-disulfide transfer protein between membrane-associated A2.5 and substrates L1 or F9. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of E10, A2.5 and G4. Exhibit thioltransferase and dehydroascorbate reductase activities in vitro.4 Publications

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaredoxin-2
    Gene namesi
    Ordered Locus Names:VACWR081
    ORF Names:G4L
    OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
    Taxonomic identifieri10254 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000000344: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131C → S: Complete loss of substrate oxidation. 1 Publication
    Mutagenesisi16 – 161C → S: Partial loss of substrate oxidation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 124124Glutaredoxin-2PRO_0000141629Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi13 ↔ 16Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer Probable. Interacts with A2.5; this interaction involves formation of a transient disulfide-bonded intermediate, allowing disulfide bond transfer. Interacts with L1; this interaction involves formation of a transient disulfide-bonded intermediate, allowing disulfide bond transfer.1 PublicationCurated

    Structurei

    Secondary structure

    1
    124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Helixi14 – 2411
    Turni25 – 295
    Beta strandi30 – 367
    Helixi46 – 483
    Helixi58 – 658
    Helixi66 – 694
    Beta strandi71 – 777
    Turni78 – 814
    Beta strandi82 – 854
    Helixi89 – 913
    Helixi99 – 1013
    Helixi104 – 11310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G2QX-ray2.50A/B/C1-124[»]
    ProteinModelPortaliP68460.
    SMRiP68460. Positions 1-121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68460.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutaredoxin family.Curated

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR008554. Glutaredoxin-like.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF05768. DUF836. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P68460-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNVLIIFGK PYCSICENVS DAVEELKSEY DILHVDILSF FLKDGDSSML    50
    GDVKRGTLIG NFAAHLSNYI VSIFKYNPQT KQMAFVDINK SLDFTKTDKS 100
    LVNLEILKSE IEKATYGVWP PVTE 124
    Length:124
    Mass (Da):13,987
    Last modified:November 23, 2004 - v1
    Checksum:iDFBE2D7B3A1A9CA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03399 Genomic DNA. Translation: AAB59814.1.
    AY243312 Genomic DNA. Translation: AAO89360.1.
    RefSeqiYP_232963.1. NC_006998.1.

    Genome annotation databases

    GeneIDi3707537.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03399 Genomic DNA. Translation: AAB59814.1 .
    AY243312 Genomic DNA. Translation: AAO89360.1 .
    RefSeqi YP_232963.1. NC_006998.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G2Q X-ray 2.50 A/B/C 1-124 [» ]
    ProteinModelPortali P68460.
    SMRi P68460. Positions 1-121.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3707537.

    Miscellaneous databases

    EvolutionaryTracei P68460.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR008554. Glutaredoxin-like.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF05768. DUF836. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genetic and molecular biological characterization of a vaccinia virus gene which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT)."
      Meis R.J., Condit R.C.
      Virology 182:442-454(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
      Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Vaccinia virus G4L gene encodes a second glutaredoxin."
      Gvakharia B.O., Koonin E.K., Mathews C.K.
      Virology 226:408-411(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "A glutaredoxin, encoded by the G4L gene of vaccinia virus, is essential for virion morphogenesis."
      White C.L., Weisberg A.S., Moss B.
      J. Virol. 74:9175-9183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly."
      White C.L., Senkevich T.G., Moss B.
      J. Virol. 76:467-472(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISULFIDE BOND, MUTAGENESIS OF CYS-13 AND CYS-16.
    6. "Complete pathway for protein disulfide bond formation encoded by poxviruses."
      Senkevich T.G., White C.L., Koonin E.V., Moss B.
      Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH A2.5, INTERACTION WITH L1.
    7. "The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity."
      Su H.P., Lin D.Y., Garboczi D.N.
      J. Virol. 80:7706-7713(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiGLRX2_VACCW
    AccessioniPrimary (citable) accession number: P68460
    Secondary accession number(s): P21025, Q76ZU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral 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

    External Data

    Dasty 3