ID A0A098S522_9BACT Unreviewed; 157 AA.
AC A0A098S522;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=IX84_17620 {ECO:0000313|EMBL:KGE86878.1};
OS Phaeodactylibacter xiamenensis.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Phaeodactylibacter.
OX NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE86878.1, ECO:0000313|Proteomes:UP000029736};
RN [1] {ECO:0000313|EMBL:KGE86878.1, ECO:0000313|Proteomes:UP000029736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD52 {ECO:0000313|EMBL:KGE86878.1,
RC ECO:0000313|Proteomes:UP000029736};
RX PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014).
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:KGE86878.1}.
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DR EMBL; JPOS01000039; KGE86878.1; -; Genomic_DNA.
DR RefSeq; WP_044223398.1; NZ_JPOS01000039.1.
DR AlphaFoldDB; A0A098S522; -.
DR STRING; 1524460.IX84_17620; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000029736; 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 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; PS00763; GLUTATHIONE_PEROXID_2; 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:UP000029736}.
FT DOMAIN 1..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 157 AA; 18081 MW; BF6D3C88ED9622B1 CRC64;
MEFYNFEAEQ LNGKKVKMEE YKGKTVVVVN TASKCGLTPQ YEGLEKLYQK YRDEGLVVLG
FPCNQFANQE PGDAEDIKEF CEINYGVSFP MFTKVEVNGE GTHPIFRYLK DELNGLFGKK
IKWNFTKFVI DKNGKPVKRF APVTKPEKME STIKKLL
//
