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Database: UniProt
Entry: A0A0F4R8D9_9GAMM
LinkDB: A0A0F4R8D9_9GAMM
Original site: A0A0F4R8D9_9GAMM 
ID   A0A0F4R8D9_9GAMM        Unreviewed;        84 AA.
AC   A0A0F4R8D9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN   ORFNames=TW85_03055 {ECO:0000313|EMBL:KJZ15879.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ15879.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ15879.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ15879.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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|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:KJZ15879.1}.
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DR   EMBL; JXYC01000004; KJZ15879.1; -; Genomic_DNA.
DR   RefSeq; WP_046015591.1; NZ_JXYC01000004.1.
DR   AlphaFoldDB; A0A0F4R8D9; -.
DR   PATRIC; fig|579484.3.peg.631; -.
DR   OrthoDB; 9814618at2; -.
DR   Proteomes; UP000033747; 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-RELATED; 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:UP000033747};
KW   Transport {ECO:0000256|RuleBase:RU364065}.
FT   DOMAIN          4..63
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   84 AA;  9618 MW;  7A8022543DC07069 CRC64;
     MSQVTIYSSD YCPFCIRAKQ LLKMKQVEFN EINVDGQSAL RREMTEKSGR TSVPQIWIQE
     HHVGGCDELF ALERNGKLDA LLSQ
//
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