ID E1F077_GIAIA Unreviewed; 201 AA.
AC E1F077;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=GLP15_440 {ECO:0000313|EMBL:EFO64134.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO64134.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO64134.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO64134.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. {ECO:0000256|PIRNR:PIRNR000239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:EFO64134.1}.
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DR EMBL; ACVC01000104; EFO64134.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F077; -.
DR STRING; 658858.E1F077; -.
DR EnsemblProtists; EFO64134; EFO64134; GLP15_440.
DR VEuPathDB; GiardiaDB:GLP15_440; -.
DR OMA; QHLYGDD; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000008974; Unassembled WGS sequence.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; AT16346P-RELATED; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|PIRNR:PIRNR000239};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR000239}.
FT DOMAIN 4..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 201 AA; 22549 MW; 73F749D896A2D7DF CRC64;
MPVPIPGTPC PDFEVDVVTP ELKFAKRKLA DYKGKYLIVF FYPLDFTFVC PSEIIHFSNL
AEQLKKKCNA EIIIGSTDSV YSHYAWCLQG QNEGGIGTCK CDLFADTNHR MARDFGVLVE
DAGIALRGMF IVSDKGVIRH VTINDLPVGR SVEEAMRLVQ AFQYADKTGG VIPCGWTPEK
NDTIIPDPEK KKEYFSKTFK K
//
