ID   GSPRX_MARGR             Reviewed;         247 AA.
AC   B3EWI1;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Glutathione amide-dependent peroxidase {ECO:0000303|PubMed:11399772};
DE            Short=Prx/Grx {ECO:0000303|PubMed:11399772};
DE            EC=1.11.1.17 {ECO:0000269|PubMed:11399772};
GN   Name=garA {ECO:0000303|PubMed:11399772};
OS   Marichromatium gracile (Chromatium gracile).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=1048;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   STRAIN=DSM 1712 / HOL-1 {ECO:0000269|PubMed:11399772};
RX   PubMed=11399772; DOI=10.1074/jbc.m102026200;
RA   Vergauwen B., Pauwels F., Jacquemotte F., Meyer T.E., Cusanovich M.A.,
RA   Bartsch R.G., Van Beeumen J.J.;
RT   "Characterization of glutathione amide reductase from Chromatium gracile.
RT   Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione
RT   amide redox cycling.";
RL   J. Biol. Chem. 276:20890-20897(2001).
CC   -!- FUNCTION: Catalyzes the oxidation of glutathione amide (GASH) to
CC       produce glutathione amide disulfide (GASSAG). May play a role in GASH
CC       metabolism under anaerobic conditions as a sulfide carrier necessary
CC       for cytoplasmic sulfide oxidation. {ECO:0000269|PubMed:11399772}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione amide + H2O2 = glutathione amide disulfide + 2
CC         H2O; Xref=Rhea:RHEA:27437, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:59895, ChEBI:CHEBI:59896; EC=1.11.1.17;
CC         Evidence={ECO:0000269|PubMed:11399772};
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DR   AlphaFoldDB; B3EWI1; -.
DR   SMR; B3EWI1; -.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03013; PRX5_like; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PTHR10430; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 2.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Peroxidase.
FT   CHAIN           1..247
FT                   /note="Glutathione amide-dependent peroxidase"
FT                   /id="PRO_0000417372"
FT   DOMAIN          4..170
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          163..247
FT                   /note="Glutaredoxin"
SQ   SEQUENCE   247 AA;  27340 MW;  202FDF439ABE2599 CRC64;
     MLQDRTGSRV PQVTFHTRSG HEWVDLTTDE IFAGKTVVVF SLPGAFTPTC SSSHVPRYNQ
     LVPMFKEHGV DTVACVSVSV NDTFVMNEWQ KTQHADDLLF IPDGNGEFTE GMGMLVEKDD
     LGFGKRSWRY SMLVRDGVVE KMFIEPEVEG DPYEVSDADT MLAHLAPNAP KPMDVSVFTR
     DGCPFCVMAK EALRNAGIDF EELVLNEDYT EQTLRAVANA VPQVEVNGEL IGGSEAVEGW
     LKERASA