ID   GLRX_BPT4               Reviewed;          87 AA.
AC   P00276;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Glutaredoxin;
DE   AltName: Full=Thioredoxin;
GN   Name=NRDC;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4565673; DOI=10.1016/s0021-9258(20)81809-2;
RA   Sjoeberg B.-M., Holmgren A.;
RT   "Studies on the structure of T4 thioredoxin. II. Amino acid sequence of the
RT   protein and comparison with thioredoxin from Escherichia coli.";
RL   J. Biol. Chem. 247:8063-8068(1972).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3735493; DOI=10.1128/jvi.59.3.759-760.1986;
RA   Lemaster D.M.;
RT   "Nucleotide sequence and protein overproduction of bacteriophage T4
RT   thioredoxin.";
RL   J. Virol. 59:759-760(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3575111; DOI=10.1093/nar/15.8.3632;
RA   Tomaschewski J., Rueger W.;
RT   "Nucleotide sequence and primary structures of gene products coded for by
RT   the T4 genome between map positions 48.266 kb and 39.166 kb.";
RL   Nucleic Acids Res. 15:3632-3633(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [5]
RP   MUTAGENESIS OF HIS-12; LYS-13; VAL-15; TYR-16; LYS-21; PRO-66 AND ASP-80,
RP   AND FUNCTION.
RX   PubMed=8440680; DOI=10.1016/s0021-9258(18)53550-x;
RA   Nikkola M., Gleason F.K., Eklund H.;
RT   "Reduction of mutant phage T4 glutaredoxins by Escherichia coli thioredoxin
RT   reductase.";
RL   J. Biol. Chem. 268:3845-3849(1993).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX   PubMed=366603; DOI=10.1073/pnas.75.12.5827;
RA   Soederberg B.-O., Sjoeberg B.-M., Sonnerstam U., Braenden C.-I.;
RT   "Three-dimensional structure of thioredoxin induced by bacteriophage T4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:5827-5830(1978).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=15017142; DOI=10.1023/b:jnmr.0000019506.30351.ca;
RA   Wang Y., Amegbey G., Wishart D.S.;
RT   "Solution structures of reduced and oxidized bacteriophage T4
RT   glutaredoxin.";
RL   J. Biomol. NMR 29:85-90(2004).
CC   -!- FUNCTION: Serves as a reducing agent for the phage-induced
CC       ribonucleotide reductase, but not for the bacterial ones. This
CC       specificity may be the result of sequence differences around the redox-
CC       active disulfide bond. The oxidized form accepts electrons from
CC       bacterial glutathione and will, in turn, reduce other small disulfides.
CC       Can also be reduced by NADPH and by bacterial thioredoxin reductase.
CC       {ECO:0000269|PubMed:8440680}.
CC   -!- MISCELLANEOUS: The disulfide bond functions as an electron carrier in
CC       the synthesis of deoxyribonucleotides from the corresponding
CC       ribonucleotide.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC   -!- CAUTION: As it can also be reduced by thioredoxin reductase, it is also
CC       known as thioredoxin. {ECO:0000305}.
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DR   EMBL; M13894; AAA32529.1; -; Genomic_DNA.
DR   EMBL; Y00122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF158101; AAD42626.1; -; Genomic_DNA.
DR   PIR; A00282; TXBPT4.
DR   RefSeq; NP_049698.1; NC_000866.4.
DR   PDB; 1AAZ; X-ray; 2.00 A; A/B=1-87.
DR   PDB; 1ABA; X-ray; 1.45 A; A=1-87.
DR   PDB; 1DE1; NMR; -; A=1-87.
DR   PDB; 1DE2; NMR; -; A=1-87.
DR   PDBsum; 1AAZ; -.
DR   PDBsum; 1ABA; -.
DR   PDBsum; 1DE1; -.
DR   PDBsum; 1DE2; -.
DR   BMRB; P00276; -.
DR   SMR; P00276; -.
DR   GeneID; 1258540; -.
DR   KEGG; vg:1258540; -.
DR   EvolutionaryTrace; P00276; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Deoxyribonucleotide synthesis; Direct protein sequencing;
KW   Disulfide bond; Electron transport; NADP; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..87
FT                   /note="Glutaredoxin"
FT                   /id="PRO_0000141649"
FT   DOMAIN          1..87
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        14..17
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:4565673"
FT   MUTAGEN         12
FT                   /note="H->S: 70% loss of ability to be reduced by
FT                   thioredoxin reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         13
FT                   /note="K->S: 85% loss of ability to be reduced by
FT                   thioredoxin reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         15
FT                   /note="V->G: Almost no effect."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         15
FT                   /note="V->P: Almost no effect. 55% loss of ability to be
FT                   reduced by thioredoxin reductase; when associated with P-
FT                   16."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         16
FT                   /note="Y->A: 20% loss of ability to be reduced by
FT                   thioredoxin reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         21
FT                   /note="K->Q: Complete loss of ability to be reduced by
FT                   thioredoxin reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         66
FT                   /note="P->A: 30% loss of ability to be reduced by
FT                   thioredoxin reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   MUTAGEN         80
FT                   /note="D->S: Increased ability to be reduced by thioredoxin
FT                   reductase."
FT                   /evidence="ECO:0000269|PubMed:8440680"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   STRAND          31..36
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:1DE1"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:1DE1"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:1ABA"
FT   HELIX           79..85
FT                   /evidence="ECO:0007829|PDB:1ABA"
SQ   SEQUENCE   87 AA;  10050 MW;  7CBB775323D1B4CE CRC64;
     MFKVYGYDSN IHKCVYCDNA KRLLTVKKQP FEFINIMPEK GVFDDEKIAE LLTKLGRDTQ
     IGLTMPQVFA PDGSHIGGFD QLREYFK