ID   A0A080MAY7_9PROT        Unreviewed;        91 AA.
AC   A0A080MAY7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   Name=grxC {ECO:0000313|EMBL:KFB77590.1};
GN   ORFNames=AW06_001284 {ECO:0000313|EMBL:KFB77590.1};
OS   Candidatus Accumulibacter cognatus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77590.1, ECO:0000313|Proteomes:UP000021315};
RN   [1] {ECO:0000313|EMBL:KFB77590.1, ECO:0000313|Proteomes:UP000021315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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|ARBA:ARBA00002549,
CC       ECO:0000256|RuleBase:RU364065}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007787, 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:KFB77590.1}.
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DR   EMBL; JDST02000021; KFB77590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080MAY7; -.
DR   STRING; 1453999.AW06_001284; -.
DR   Proteomes; UP000021315; 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; IPR011900; GRX_bact.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02181; GRX_bact; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   PANTHER; PTHR45694:SF18; GLUTAREDOXIN-1; 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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|RuleBase:RU364065};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU364065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN          7..67
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   91 AA;  10137 MW;  4C2CBB549A4C4DFD CRC64;
     MTAMPRVLMY STAVCPYCIR AEQLLRARGV VDIEKVRIDL DPKRRAEMLE RTARRTVPQI
     YIGETHVGGS DELIALDRAG KLTPLLAGEG I
//