ID   GPXA_NEIMF              Reviewed;         177 AA.
AC   A1KV41; P0A0T6; P52036;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Glutathione peroxidase homolog;
GN   Name=gpxA; Synonyms=gph; OrderedLocusNames=NMC1547;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8746463; DOI=10.3109/10425179509074701;
RA   Aho E.L., Kelly L.P.;
RT   "Identification of a glutathione peroxidase homolog in Neisseria
RT   meningitidis.";
RL   DNA Seq. 6:55-60(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
CC   -!- FUNCTION: Important in the cellular metabolism or defense processes
CC       particular to this pathogen.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; U16141; AAB41264.1; -; Genomic_DNA.
DR   EMBL; AM421808; CAM10742.1; -; Genomic_DNA.
DR   RefSeq; WP_002218952.1; NC_008767.1.
DR   AlphaFoldDB; A1KV41; -.
DR   SMR; A1KV41; -.
DR   EnsemblBacteria; CAM10742; CAM10742; NMC1547.
DR   GeneID; 61281794; -.
DR   KEGG; nmc:NMC1547; -.
DR   HOGENOM; CLU_029507_2_2_4; -.
DR   OMA; FPMMSKI; -.
DR   OrthoDB; 1635499at2; -.
DR   Proteomes; UP000002286; 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   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..177
FT                   /note="Glutathione peroxidase homolog"
FT                   /id="PRO_0000285027"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  19929 MW;  89E50641FCAED5B5 CRC64;
     MGIYDFQMKD AEGNAVDLSG YRGKVLLIVN TATRCGLTPQ YEALQKLYAQ YTAEGLEILD
     FPCNQFREQA PESSGEIAQV CMMKFGTKFK IFDKIEVNGA NTAPLYAYLK SVKPQDKGNH
     LFKDFVLKLA ALGEKRDEGD IKWNFTKFLV NRDGEVVERF APSVTPEEIE ADIRALL