GenomeNet

Database: UniProt
Entry: H0SY84_9BRAD
LinkDB: H0SY84_9BRAD
Original site: H0SY84_9BRAD 
ID   H0SY84_9BRAD            Unreviewed;        91 AA.
AC   H0SY84;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   Name=grxC {ECO:0000313|EMBL:CCD99161.1};
GN   ORFNames=BRAS3809_2480019 {ECO:0000313|EMBL:CCD99161.1};
OS   Bradyrhizobium sp. STM 3809.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551936 {ECO:0000313|EMBL:CCD99161.1, ECO:0000313|Proteomes:UP000004098};
RN   [1] {ECO:0000313|Proteomes:UP000004098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM 3809 {ECO:0000313|Proteomes:UP000004098};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCD99161.1}.
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; CAFJ01000166; CCD99161.1; -; Genomic_DNA.
DR   RefSeq; WP_008961758.1; NZ_CAFJ01000166.1.
DR   AlphaFoldDB; H0SY84; -.
DR   OrthoDB; 9814618at2; -.
DR   Proteomes; UP000004098; 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-RELATED; 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          5..65
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   91 AA;  9878 MW;  E9E73D63FBC127AB CRC64;
     MTAAIEIYTR PGCGYCTAAK SLLTRKNVPF TEYDAGKDPN VRQQMYDRVG PGSTFPQIFI
     GKAHVGGCDD LYALDREGRL DAMLAGDKAT S
//
DBGET integrated database retrieval system