ID A0A099LDU6_9GAMM Unreviewed; 207 AA.
AC A0A099LDU6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=ND16A_3326 {ECO:0000313|EMBL:KGK00566.1};
OS Thalassotalea sp. ND16A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGK00566.1, ECO:0000313|Proteomes:UP000029848};
RN [1] {ECO:0000313|EMBL:KGK00566.1, ECO:0000313|Proteomes:UP000029848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND16A {ECO:0000313|EMBL:KGK00566.1,
RC ECO:0000313|Proteomes:UP000029848};
RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA Hazen T.C.;
RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT Eastern Mediterranean Deep Water.";
RL Submitted (AUG-2014) 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:KGK00566.1}.
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DR EMBL; JQDZ01000012; KGK00566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099LDU6; -.
DR STRING; 1535422.ND16A_3326; -.
DR PATRIC; fig|1535422.3.peg.445; -.
DR eggNOG; COG0386; Bacteria.
DR Proteomes; UP000029848; 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:SF44; GLUTATHIONE PEROXIDASE; 1.
DR Pfam; PF00255; GSHPx; 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:UP000029848};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..207
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001949625"
FT DOMAIN 36..198
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 207 AA; 23267 MW; 7A405A0E7FB0C1A7 CRC64;
MKFIFTVLLA LITSFSVNAE EQLQHSVVPM PVPVVLADAE QCPDFLQHTV RKLNSKQSLD
LCKEFAGKTF LIVNTASNCG FTPQFKALEA LYQEYKDHGL VVLGFPSDNF FQEEDEEQDT
AKVCFVNYGV TFPMFATIEV RGSDAHPIFA HLGEQTASPY WNFYKYLVSA DGKTIQRFNS
RTKPQSEQLT KAIEQQLNIT ALPGISI
//
