ID G1XWX9_9PROT Unreviewed; 189 AA.
AC G1XWX9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=AZA_51791 {ECO:0000313|EMBL:EGY02228.1};
OS Nitrospirillum amazonense Y2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY02228.1, ECO:0000313|Proteomes:UP000018435};
RN [1] {ECO:0000313|EMBL:EGY02228.1, ECO:0000313|Proteomes:UP000018435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT "Genomic insights into the versatility of the plant growth-promoting
RT bacterium Azospirillum amazonense.";
RL BMC Genomics 12:409-409(2011).
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:EGY02228.1}.
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DR EMBL; AFBX01000123; EGY02228.1; -; Genomic_DNA.
DR RefSeq; WP_004271873.1; NZ_AFBX01000123.1.
DR AlphaFoldDB; G1XWX9; -.
DR PATRIC; fig|1003237.3.peg.841; -.
DR Proteomes; UP000018435; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018435}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 189 AA; 20438 MW; FD6B0CD31E91B6F7 CRC64;
MLTPTVKASV HQTTGQEPTP MLPQSQTAAT ASAHAFSFQR LGGKGAVPLA AYAGQPVLVV
NTASNCRFTN QYEDLQALHA KYGPRGLVVL GVPSNDFGKQ EPGSASEIGA FCQRNYGVEF
TMADKEVVIG AEAHPFFNWL VDVAGEDAAP RWNFHKYLLG KDGRLVRYWS SVFRPSNEAI
IQAVEAQLA
//
