GPXA_NEIMB
ID GPXA_NEIMB Reviewed; 177 AA.
AC P0A0T5; P52036;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Glutathione peroxidase homolog;
GN Name=gpxA; Synonyms=gph; OrderedLocusNames=NMB1621;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: Important in the cellular metabolism or defense processes
CC particular to this pathogen. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; AE002098; AAF41973.1; -; Genomic_DNA.
DR PIR; C81062; C81062.
DR RefSeq; NP_274627.1; NC_003112.2.
DR RefSeq; WP_002218952.1; NC_003112.2.
DR AlphaFoldDB; P0A0T5; -.
DR SMR; P0A0T5; -.
DR STRING; 122586.NMB1621; -.
DR PaxDb; P0A0T5; -.
DR EnsemblBacteria; AAF41973; AAF41973; NMB1621.
DR GeneID; 61281794; -.
DR KEGG; nme:NMB1621; -.
DR PATRIC; fig|122586.8.peg.2082; -.
DR HOGENOM; CLU_029507_2_2_4; -.
DR OMA; FPMMSKI; -.
DR Proteomes; UP000000425; 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; Reference proteome.
FT CHAIN 1..177
FT /note="Glutathione peroxidase homolog"
FT /id="PRO_0000066659"
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