(data stored in ACNUC5340 zone)

SWISSPROT: Q6F802_ACIAD

ID   Q6F802_ACIAD            Unreviewed;        85 AA.
AC   Q6F802;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   Name=grx {ECO:0000313|EMBL:CAG69813.1};
GN   OrderedLocusNames=ACIAD3121 {ECO:0000313|EMBL:CAG69813.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69813.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG69813.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG69813.1; -; Genomic_DNA.
DR   RefSeq; WP_004924352.1; NC_005966.1.
DR   STRING; 62977.ACIAD3121; -.
DR   EnsemblBacteria; CAG69813; CAG69813; ACIAD3121.
DR   KEGG; aci:ACIAD3121; -.
DR   eggNOG; ENOG4105VW4; Bacteria.
DR   eggNOG; COG0695; LUCA.
DR   HOGENOM; HOG000095203; -.
DR   KO; K03676; -.
DR   OMA; GRTTFPQ; -.
DR   OrthoDB; 2045232at2; -.
DR   BioCyc; ASP62977:ACIAD_RS14100-MONOMER; -.
DR   Proteomes; UP000000430; 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; Q6F802.
DR   SWISS-2DPAGE; Q6F802.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000430};
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:UP000000430};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN        1     85       Glutaredoxin. {ECO:0000259|PROSITE:
FT                                PS51354}.
SQ   SEQUENCE   85 AA;  9826 MW;  1EEAA7C426A37AA6 CRC64;
     MAANITIYST TVCPYCIRAK QLLERKGVKY KEINLSNEAP EVRVELMQRT HHRTVPQIFI
     NDQFIGGFDQ LYALERDGKL DELLA
//

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