(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJH7_PSEPF

ID   Q3KJH7_PSEPF            Unreviewed;        84 AA.
AC   Q3KJH7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   Name=grxC {ECO:0000313|EMBL:ABA72079.1};
GN   OrderedLocusNames=Pfl01_0335 {ECO:0000313|EMBL:ABA72079.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72079.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72079.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72079.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
CC       the presence of NADPH and glutathione reductase. Reduces low
CC       molecular weight disulfides and proteins.
CC       {ECO:0000256|RuleBase:RU364065}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|RuleBase:RU364065}.
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DR   EMBL; CP000094; ABA72079.1; -; Genomic_DNA.
DR   RefSeq; WP_007952522.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0335; -.
DR   EnsemblBacteria; ABA72079; ABA72079; Pfl01_0335.
DR   KEGG; pfo:Pfl01_0335; -.
DR   eggNOG; ENOG4105VW4; Bacteria.
DR   eggNOG; COG0695; LUCA.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; GRTTFPQ; -.
DR   BioCyc; PFLU205922:G1G4S-339-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   CDD; cd03418; GRX_GRXb_1_3_like; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02181; GRX_bact; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJH7.
DR   SWISS-2DPAGE; Q3KJH7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW   Electron transport {ECO:0000256|RuleBase:RU364065};
KW   Redox-active center {ECO:0000256|RuleBase:RU364065};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN        1     84       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
SQ   SEQUENCE   84 AA;  9139 MW;  A2957CC92097989B CRC64;
     MSDVIVYSSD YCPYCSRAKY LLANKGVAFE EIKVDGKPQV RAAMAQKAGR TSVPQIWIGD
     THVGGCDDLY ALERAGKLDA LLKA
//

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