ID Q5ZT58_LEGPH Unreviewed; 84 AA.
AC Q5ZT58;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN Name=grxC {ECO:0000313|EMBL:AAU28369.1};
GN OrderedLocusNames=lpg2307 {ECO:0000313|EMBL:AAU28369.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU28369.1, ECO:0000313|Proteomes:UP000000609};
RN [1] {ECO:0000313|EMBL:AAU28369.1, ECO:0000313|Proteomes:UP000000609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {ECO:0000313|Proteomes:UP000000609};
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU28369.1; -; Genomic_DNA.
DR RefSeq; WP_010948013.1; NC_002942.5.
DR RefSeq; YP_096316.1; NC_002942.5.
DR AlphaFoldDB; Q5ZT58; -.
DR SMR; Q5ZT58; -.
DR STRING; 272624.lpg2307; -.
DR PaxDb; 272624-lpg2307; -.
DR GeneID; 66491433; -.
DR KEGG; lpn:lpg2307; -.
DR PATRIC; fig|272624.6.peg.2421; -.
DR eggNOG; COG0695; Bacteria.
DR HOGENOM; CLU_026126_7_3_6; -.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000000609; 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:UP000000609};
KW Transport {ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 4..63
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 84 AA; 9651 MW; 06EF616DC70D65BA CRC64;
MNEVILYTTG YCPYCIKAKE LLDRKKVIYT EIRVDLQPEL REEMIQKSGR RTVPQIFING
QAIGGCDDLY ALEAQGTLNE LLKK
//
