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Database: UniProt
Entry: G9ZY15_9PROT
LinkDB: G9ZY15_9PROT
Original site: G9ZY15_9PROT 
ID   G9ZY15_9PROT            Unreviewed;       173 AA.
AC   G9ZY15;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=HMPREF9946_01447 {ECO:0000313|EMBL:EHM02147.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM02147.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHM02147.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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:EHM02147.1}.
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DR   EMBL; AGEZ01000046; EHM02147.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9ZY15; -.
DR   STRING; 1054213.HMPREF9946_01447; -.
DR   PATRIC; fig|1054213.3.peg.1339; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_1_2_5; -.
DR   OrthoDB; 9785502at2; -.
DR   BioCyc; ABAC1054213:G1H32-1345-MONOMER; -.
DR   Proteomes; UP000003292; Unassembled WGS sequence.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..173
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003530334"
FT   DOMAIN          20..173
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   173 AA;  18656 MW;  B77606F75675765E CRC64;
     MAELSRRLLL AGMPLALMAA APAGSAHDFR FPAIEGGEIN LADHRGKPIL VVNTASFCGF
     APQFAALQKL HERFAPEGLL VVGVPSNDFN QEAADNEAVK EFCEAEFGVD FPMAAISHVK
     GAQAHPFFAW AGEPGWNFYK YLIGKDGSLI QSFPSRVTPD SPELLRLIEA SLS
//
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