ID A0A0W0YK62_9GAMM Unreviewed; 84 AA.
AC A0A0W0YK62;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN Name=grx {ECO:0000313|EMBL:KTD57250.1};
GN ORFNames=Lsha_2632 {ECO:0000313|EMBL:KTD57250.1};
OS Legionella shakespearei DSM 23087.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD57250.1, ECO:0000313|Proteomes:UP000054600};
RN [1] {ECO:0000313|EMBL:KTD57250.1, ECO:0000313|Proteomes:UP000054600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD57250.1,
RC ECO:0000313|Proteomes:UP000054600};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {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:KTD57250.1}.
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DR EMBL; LNYW01000069; KTD57250.1; -; Genomic_DNA.
DR RefSeq; WP_018577213.1; NZ_LNYW01000069.1.
DR AlphaFoldDB; A0A0W0YK62; -.
DR STRING; 1122169.Lsha_2632; -.
DR PATRIC; fig|1122169.6.peg.3035; -.
DR eggNOG; COG0695; Bacteria.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000054600; 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; PTHR46679; -; 1.
DR PANTHER; PTHR46679:SF1; GLUTAREDOXIN-2, MITOCHONDRIAL; 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|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU364065};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364065};
KW Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 4..63
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 84 AA; 9391 MW; 43B7EBA23DF7115C CRC64;
MAEVIMYSTG SCPYCIRAKD LLHSKNISFT DIRVDLQPEL REEMMVKSGR RTVPQIFING
QAIGGCDDLY ALEAQGKLNQ LLKG
//