ID A0A0R3MS79_9BRAD Unreviewed; 90 AA.
AC A0A0R3MS79;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN ORFNames=CQ14_27245 {ECO:0000313|EMBL:KRR20435.1};
OS Bradyrhizobium lablabi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR20435.1, ECO:0000313|Proteomes:UP000051660};
RN [1] {ECO:0000313|EMBL:KRR20435.1, ECO:0000313|Proteomes:UP000051660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR20435.1,
RC ECO:0000313|Proteomes:UP000051660};
RA Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT Spain.";
RL Submitted (MAR-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:KRR20435.1}.
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DR EMBL; LLYB01000087; KRR20435.1; -; Genomic_DNA.
DR RefSeq; WP_057860604.1; NZ_LLYB01000087.1.
DR AlphaFoldDB; A0A0R3MS79; -.
DR STRING; 722472.SAMN05444321_1996; -.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000051660; 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; 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; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW Electron transport {ECO:0000256|RuleBase:RU364065};
KW Redox-active center {ECO:0000256|RuleBase:RU364065};
KW Transport {ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 4..64
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 90 AA; 9723 MW; AFFD2A4D96D221A9 CRC64;
MTAIEIYTRP GCGYCTAAKS LLTRKNAAFT ELNVATDPAY REQMYDRAGH GSTFPQIFIG
TTHVGGCDEL YALDRAGKLD SLLNGEKASS
//
