ID A0A173H907_9PSED Unreviewed; 84 AA. AC A0A173H907; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 03-MAY-2023, entry version 24. DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065}; GN ORFNames=AA098_01710 {ECO:0000313|EMBL:ANI32286.1}; OS Pseudomonas sp. JY-Q. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1338689 {ECO:0000313|EMBL:ANI32286.1, ECO:0000313|Proteomes:UP000078361}; RN [1] {ECO:0000313|EMBL:ANI32286.1, ECO:0000313|Proteomes:UP000078361} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JY-Q {ECO:0000313|EMBL:ANI32286.1, RC ECO:0000313|Proteomes:UP000078361}; RA Zhong W.; RT "Pseudomonas sp. JY-Q genome sequencing and assembly."; RL Submitted (MAY-2015) 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 -!- SIMILARITY: Belongs to the glutaredoxin family. CC {ECO:0000256|RuleBase:RU364065}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011525; ANI32286.1; -; Genomic_DNA. DR RefSeq; WP_003249204.1; NZ_CP011525.1. DR AlphaFoldDB; A0A173H907; -. DR EnsemblBacteria; ANI32286; ANI32286; AA098_01710. DR GeneID; 75200168; -. DR PATRIC; fig|1338689.3.peg.358; -. DR Proteomes; UP000078361; Chromosome. 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 PANTHER; PTHR45694; GLUTAREDOXIN 2; 1. DR PANTHER; PTHR45694:SF18; GLUTAREDOXIN-1-RELATED; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR PRINTS; PR00160; GLUTAREDOXIN. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR TIGRFAMs; TIGR02181; GRX_bact; 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}; Transport {ECO:0000256|RuleBase:RU364065}. FT DOMAIN 4..63 FT /note="Glutaredoxin" FT /evidence="ECO:0000259|Pfam:PF00462" SQ SEQUENCE 84 AA; 9226 MW; D2FED7B84CEED9A0 CRC64; MKPVIVYSSD YCPYCMRAKY LLESKGVAFE EIKVDGKPQV RAEMSQKAGR TSVPQIWIGS THVGGCDDLY ALERAGKLDA LLAA //