GLRX2_VACCW
ID GLRX2_VACCW Reviewed; 124 AA.
AC P68460; P21025; Q76ZU1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 23-FEB-2022, entry version 83.
DE RecName: Full=Glutaredoxin-2;
GN OrderedLocusNames=VACWR081; ORFNames=G4L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2024483; DOI=10.1016/0042-6822(91)90585-y;
RA Meis R.J., Condit R.C.;
RT "Genetic and molecular biological characterization of a vaccinia virus gene
RT which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT).";
RL Virology 182:442-454(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=8955061; DOI=10.1006/viro.1996.0669;
RA Gvakharia B.O., Koonin E.K., Mathews C.K.;
RT "Vaccinia virus G4L gene encodes a second glutaredoxin.";
RL Virology 226:408-411(1996).
RN [4]
RP FUNCTION.
RX PubMed=10982364; DOI=10.1128/jvi.74.19.9175-9183.2000;
RA White C.L., Weisberg A.S., Moss B.;
RT "A glutaredoxin, encoded by the G4L gene of vaccinia virus, is essential
RT for virion morphogenesis.";
RL J. Virol. 74:9175-9183(2000).
RN [5]
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-13 AND CYS-16.
RX PubMed=11752136; DOI=10.1128/jvi.76.2.467-472.2002;
RA White C.L., Senkevich T.G., Moss B.;
RT "Vaccinia virus G4L glutaredoxin is an essential intermediate of a
RT cytoplasmic disulfide bond pathway required for virion assembly.";
RL J. Virol. 76:467-472(2002).
RN [6]
RP FUNCTION, INTERACTION WITH A2.5, AND INTERACTION WITH L1.
RX PubMed=11983854; DOI=10.1073/pnas.062163799;
RA Senkevich T.G., White C.L., Koonin E.V., Moss B.;
RT "Complete pathway for protein disulfide bond formation encoded by
RT poxviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=16840349; DOI=10.1128/jvi.00521-06;
RA Su H.P., Lin D.Y., Garboczi D.N.;
RT "The structure of G4, the poxvirus disulfide oxidoreductase essential for
RT virus maturation and infectivity.";
RL J. Virol. 80:7706-7713(2006).
CC -!- FUNCTION: Glutaredoxin necessary for virion morphogenesis and virus
CC replication. Functions as a thiol-disulfide transfer protein between
CC membrane-associated A2.5 and substrates L1 or F9. The complete pathway
CC for formation of disulfide bonds in intracellular virion membrane
CC proteins sequentially involves oxidation of E10, A2.5 and G4. Exhibit
CC thioltransferase and dehydroascorbate reductase activities in vitro.
CC {ECO:0000269|PubMed:10982364, ECO:0000269|PubMed:11752136,
CC ECO:0000269|PubMed:11983854, ECO:0000269|PubMed:8955061}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with A2.5; this interaction
CC involves formation of a transient disulfide-bonded intermediate,
CC allowing disulfide bond transfer. Interacts with L1; this interaction
CC involves formation of a transient disulfide-bonded intermediate,
CC allowing disulfide bond transfer. {ECO:0000269|PubMed:11983854,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; J03399; AAB59814.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89360.1; -; Genomic_DNA.
DR RefSeq; YP_232963.1; NC_006998.1.
DR PDB; 2G2Q; X-ray; 2.50 A; A/B/C=1-124.
DR PDBsum; 2G2Q; -.
DR SMR; P68460; -.
DR DNASU; 3707537; -.
DR GeneID; 3707537; -.
DR KEGG; vg:3707537; -.
DR EvolutionaryTrace; P68460; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR008554; Glutaredoxin-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF05768; Glrx-like; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Host cytoplasm;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..124
FT /note="Glutaredoxin-2"
FT /id="PRO_0000141629"
FT DISULFID 13..16
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:11752136"
FT MUTAGEN 13
FT /note="C->S: Complete loss of substrate oxidation."
FT /evidence="ECO:0000269|PubMed:11752136"
FT MUTAGEN 16
FT /note="C->S: Partial loss of substrate oxidation."
FT /evidence="ECO:0000269|PubMed:11752136"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:2G2Q"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:2G2Q"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:2G2Q"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2G2Q"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:2G2Q"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2G2Q"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:2G2Q"
SQ SEQUENCE 124 AA; 13987 MW; DFBE2D7B3A1A9CA6 CRC64;
MKNVLIIFGK PYCSICENVS DAVEELKSEY DILHVDILSF FLKDGDSSML GDVKRGTLIG
NFAAHLSNYI VSIFKYNPQT KQMAFVDINK SLDFTKTDKS LVNLEILKSE IEKATYGVWP
PVTE
