(data stored in SCRATCH zone)

SWISSPROT: Q3IIE2_PSEHT

ID   Q3IIE2_PSEHT            Unreviewed;        89 AA.
AC   Q3IIE2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 83.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   OrderedLocusNames=PSHAa0368 {ECO:0000313|EMBL:CAI85466.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85466.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85466.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85466.1; -; Genomic_DNA.
DR   RefSeq; WP_011327079.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIE2; -.
DR   STRING; 326442.PSHAa0368; -.
DR   EnsemblBacteria; CAI85466; CAI85466; PSHAa0368.
DR   KEGG; pha:PSHAa0368; -.
DR   PATRIC; fig|326442.8.peg.352; -.
DR   eggNOG; ENOG4108UEK; Bacteria.
DR   eggNOG; ENOG4111EWG; LUCA.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; GRTTFPQ; -.
DR   OrthoDB; POG091H0GMC; -.
DR   BioCyc; PHAL326442:GJIU-373-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier 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; IPR012336; Thioredoxin-like_fold.
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; Q3IIE2.
DR   SWISS-2DPAGE; Q3IIE2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
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:UP000006843};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN        1     89       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
SQ   SEQUENCE   89 AA;  9725 MW;  8041AEF02B5F3C0D CRC64;
     MSNVVLYTKA YCPFCQRARA LLDSKGVQYT NFDIGVQPEL RDEMIAKAGG ASTVPQIFIN
     DEHIGGCDDM MAIEAQGQLD KKLNATLNA
//

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