ID A0A0M4MGR9_9SPHN Unreviewed; 159 AA.
AC A0A0M4MGR9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=AMC99_01324 {ECO:0000313|EMBL:ALE16618.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE16618.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE16618.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE16618.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP012669; ALE16618.1; -; Genomic_DNA.
DR RefSeq; WP_061924357.1; NZ_CP012669.1.
DR AlphaFoldDB; A0A0M4MGR9; -.
DR STRING; 361183.AMC99_01324; -.
DR KEGG; aep:AMC99_01324; -.
DR PATRIC; fig|361183.4.peg.1294; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000057938; Chromosome.
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:UP000057938}.
FT DOMAIN 1..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 159 AA; 17608 MW; F70085F61FE867EE CRC64;
MTTISDFTVT TNRGEELDLS SKQGKVLLVV NTASKCGFTP QYDGLEELYQ KYKDQGFEVL
GFPCNQFGAQ EPGNADEIQE FCKVNFGVTF PLMEKVDVNG PDASPLFDWM KGEAKGIMGT
TAIKWNFTKF LIDRGGNVVK RYGSTDKPAS IAKDIEKLL
//
