ID   G7GA56_9GAMM            Unreviewed;        86 AA.
AC   G7GA56;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   ORFNames=ACT4_006_00260 {ECO:0000313|EMBL:GAB00481.1};
OS   Acinetobacter sp. NBRC 100985.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1071390 {ECO:0000313|EMBL:GAB00481.1, ECO:0000313|Proteomes:UP000012044};
RN   [1] {ECO:0000313|EMBL:GAB00481.1, ECO:0000313|Proteomes:UP000012044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100985 {ECO:0000313|EMBL:GAB00481.1,
RC   ECO:0000313|Proteomes:UP000012044};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins. {ECO:0000256|RuleBase:RU364065}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|RuleBase:RU364065}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB00481.1}.
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DR   EMBL; BAEB01000006; GAB00481.1; -; Genomic_DNA.
DR   RefSeq; WP_004774456.1; NZ_BAEB01000006.1.
DR   AlphaFoldDB; G7GA56; -.
DR   GeneID; 80105965; -.
DR   Proteomes; UP000012044; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0015038; F:glutathione 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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02181; GRX_bact; 1.
DR   PANTHER; PTHR46679; -; 1.
DR   PANTHER; PTHR46679:SF1; GLUTAREDOXIN-2, MITOCHONDRIAL; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU364065};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU364065};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN          4..86
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
SQ   SEQUENCE   86 AA;  9900 MW;  EAF1EB9320705EBE CRC64;
     MTTPNVTIYS TLSCPYCVRA KQLLERKGVA FKEINLSNEA PEVRIELMQR TNHRTVPQIF
     IKDQFIGGFD QLYALEREGK LDQLLA
//