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Database: UniProt
Entry: A0A2A9MMW8_9APIC
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ID   A0A2A9MMW8_9APIC        Unreviewed;       268 AA.
AC   A0A2A9MMW8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   ORFNames=BESB_010760 {ECO:0000313|EMBL:PFH38734.1};
OS   Besnoitia besnoiti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX   NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH38734.1, ECO:0000313|Proteomes:UP000224006};
RN   [1] {ECO:0000313|EMBL:PFH38734.1, ECO:0000313|Proteomes:UP000224006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH38734.1,
RC   ECO:0000313|Proteomes:UP000224006};
RA   Schares G., Venepally P., Lorenzi H.A.;
RT   "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PFH38734.1}.
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DR   EMBL; NWUJ01000001; PFH38734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9MMW8; -.
DR   STRING; 94643.A0A2A9MMW8; -.
DR   VEuPathDB; ToxoDB:BESB_010760; -.
DR   OrthoDB; 205987at2759; -.
DR   Proteomes; UP000224006; Chromosome i.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   PANTHER; PTHR10681:SF164; THIOREDOXIN PEROXIDASE 1; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224006}.
FT   DOMAIN          65..225
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   268 AA;  28960 MW;  F4A5AA3D7E332739 CRC64;
     MATFCLRATS IFSSLALRAV RTPSAAPLAK LNAASSLRAA AAPLSFCMET RAFASEAPER
     LANLSLVARP APDFTADAAM PGGEIAKLTL SELCGNGSGV VLLFYPLDFT FVCPSEILAF
     NAAVADFEKL GFKVVGVSVD SVFTHQAWMR VPLAEGGIGK LDFPLVSDLD KTISSRYHSL
     LNNSVALRTL VIIDGAKNVR HMTVNDLPLG RNVEEALRVC EMIREVEKNG GKQVCPANWR
     RGEKMMEASF HGVKDYLGGL REKIEKQI
//
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