ID A0A073CF05_PLAAG Unreviewed; 111 AA.
AC A0A073CF05;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN Name=grxC {ECO:0000313|EMBL:KEI66706.1};
GN ORFNames=A19Y_1697 {ECO:0000313|EMBL:KEI66706.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI66706.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI66706.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI66706.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
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}.
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DR EMBL; CM002803; KEI66706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073CF05; -.
DR STRING; 388467.A19Y_1697; -.
DR PATRIC; fig|388467.6.peg.1640; -.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_026126_7_3_3; -.
DR Proteomes; UP000027395; Chromosome.
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; 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:UP000027395};
KW Transport {ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 28..88
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 111 AA; 12833 MW; 62C586B920DDE965 CRC64;
MLISRNFIML DALNNLLGRH PERNQANVEI YTWQTCPFCI RAKLLLWWKG VDFTEYKIDG
DDVARNQMAE RANGRRTVPQ IFINNQHIGG CDDLYQLDGE GKLEPRLAEP A
//
