ID A0A1Q8TG60_9GAMM Unreviewed; 164 AA.
AC A0A1Q8TG60;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=BTW10_04195 {ECO:0000313|EMBL:OLO12664.1};
OS Chromohalobacter japonicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=223900 {ECO:0000313|EMBL:OLO12664.1, ECO:0000313|Proteomes:UP000186806};
RN [1] {ECO:0000313|EMBL:OLO12664.1, ECO:0000313|Proteomes:UP000186806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB17 {ECO:0000313|EMBL:OLO12664.1,
RC ECO:0000313|Proteomes:UP000186806};
RA Mavrodi D.V., Olsson B.E., Korsakova E.S., Pyankova A., Mavrodi O.V.,
RA Plotnikova E.G.;
RT "Draft genome sequences of strains Salinicola socius SMB35, Salinicola sp.
RT MH3R3-1 and Chromohalobacter sp. SMB17 from the Verkhnekamsk potash mining
RT region of Russia.";
RL Submitted (DEC-2016) 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:OLO12664.1}.
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DR EMBL; MSDQ01000006; OLO12664.1; -; Genomic_DNA.
DR RefSeq; WP_075368303.1; NZ_MSDQ01000006.1.
DR AlphaFoldDB; A0A1Q8TG60; -.
DR STRING; 223900.GCA_000821045_01980; -.
DR Proteomes; UP000186806; 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; IPR029760; GPX_CS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 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}.
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 164 AA; 18861 MW; 9BEF0FE77975BCFA CRC64;
MTLYSQDCHT NRMEPFNLRA LRGQVLLIVN VASRCGYTPQ LKELEWLYRR YHDQGFTVLA
FPCNQFGRQT PESAEGFGAF CMREYRVSFP VMEKVHVNGR DAHPLFVLLR RQAPGVLGST
PIKWNFTKFL VGRDGHVIRR FAPRVSPRSM AADIERALDI PFSA
//
