ID A0A3N6MLI2_9BURK Unreviewed; 87 AA.
AC A0A3N6MLI2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN Name=grxC {ECO:0000313|EMBL:RQH04644.1};
GN ORFNames=D1Y85_17270 {ECO:0000313|EMBL:RQH04644.1};
OS Paraburkholderia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH04644.1, ECO:0000313|Proteomes:UP000272778};
RN [1] {ECO:0000313|EMBL:RQH04644.1, ECO:0000313|Proteomes:UP000272778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOA04 {ECO:0000313|EMBL:RQH04644.1,
RC ECO:0000313|Proteomes:UP000272778};
RA Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT "Paraburkholderia sp. DHOA04, isolated from soil.";
RL Submitted (NOV-2018) 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:RQH04644.1}.
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DR EMBL; RQIS01000012; RQH04644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6MLI2; -.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000272778; 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:UP000272778};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 4..64
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 87 AA; 9840 MW; BBD14409841705C4 CRC64;
MSKVVMYSTQ VCPYCQMAER LLKSRGVEHI EKVLIDRDPT RREEMMTRTG RRTVPQVFIG
ETHVGGYDDL SALDRAGGLM PLLEKAA
//