(data stored in SCRATCH zone)

SWISSPROT: Q5LWM3_RUEPO

ID   Q5LWM3_RUEPO            Unreviewed;        86 AA.
AC   Q5LWM3;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   OrderedLocusNames=SPO0070 {ECO:0000313|EMBL:AAV93401.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93401.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93401.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93401.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93401.1; -; Genomic_DNA.
DR   RefSeq; WP_011045843.1; NC_003911.12.
DR   STRING; 246200.SPO0070; -.
DR   EnsemblBacteria; AAV93401; AAV93401; SPO0070.
DR   KEGG; sil:SPO0070; -.
DR   eggNOG; ENOG4105VW4; Bacteria.
DR   eggNOG; COG0695; LUCA.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; GRTTFPQ; -.
DR   OrthoDB; 2045232at2; -.
DR   BioCyc; RPOM246200:G1G48-71-MONOMER; -.
DR   Proteomes; UP000001023; 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; 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; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWM3.
DR   SWISS-2DPAGE; Q5LWM3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW   Electron transport {ECO:0000256|RuleBase:RU364065};
KW   Redox-active center {ECO:0000256|RuleBase:RU364065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN        1     86       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
SQ   SEQUENCE   86 AA;  9587 MW;  248C16EA1F6DF09B CRC64;
     MKPVEIYTSP LCGYCHAAKR LLDQKGIAFT EIDVLTNPKR KPEMIQRAGG RRTVPQIFID
     GQHVGGCDDL YALEQDGKLD PMLASR
//

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