ID Q9I457_PSEAE Unreviewed; 184 AA.
AC Q9I457;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN OrderedLocusNames=PA1287 {ECO:0000313|EMBL:AAG04676.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964 {ECO:0000313|EMBL:AAG04676.1, ECO:0000313|Proteomes:UP000002438};
RN [1] {ECO:0000313|EMBL:AAG04676.1, ECO:0000313|Proteomes:UP000002438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC 1C / PRS 101 / PAO1 {ECO:0000313|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.Q., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R., Smith K.,
RA Spencer D., Wong G.K., Wu Z., Paulsen I.T., Reizer J., Saier M.H.,
RA Hancock R.E., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; AE004091; AAG04676.1; -; Genomic_DNA.
DR PIR; G83484; G83484.
DR RefSeq; NP_249978.1; NC_002516.2.
DR RefSeq; WP_003082631.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I457; -.
DR SMR; Q9I457; -.
DR STRING; 208964.PA1287; -.
DR PaxDb; 208964-PA1287; -.
DR DNASU; 881478; -.
DR GeneID; 881478; -.
DR KEGG; pae:PA1287; -.
DR PATRIC; fig|208964.12.peg.1337; -.
DR PseudoCAP; PA1287; -.
DR HOGENOM; CLU_029507_1_3_6; -.
DR InParanoid; Q9I457; -.
DR OrthoDB; 9785502at2; -.
DR PhylomeDB; Q9I457; -.
DR BioCyc; PAER208964:G1FZ6-1312-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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:SF44; 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:UP000002438};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..184
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004331301"
FT DOMAIN 11..181
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 184 AA; 20217 MW; F146CABB72EF9FC0 CRC64;
MKPRVLLSVL ALAGLPLSGW AADCPELLQG QLTKLRSKES IDLCQRYAGK PLVVVNTASH
CGFTPQFKGL EALYQRYKGQ GLEVLGVPSD DFKQEAADTA ETAKICYGNY GVTFAMTQPQ
HVRGDEAIPL FRQLAEQSGQ APRWNFYKYV VDRQGRVVAQ FSSKTTPDDP QLQAAIEKAI
ASQP
//
