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Database: UniProt
Entry: A0A1C7NDD3_9FUNG
LinkDB: A0A1C7NDD3_9FUNG
Original site: A0A1C7NDD3_9FUNG 
ID   A0A1C7NDD3_9FUNG        Unreviewed;       245 AA.
AC   A0A1C7NDD3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   Name=PRDX2 {ECO:0000313|EMBL:OBZ87058.1};
GN   ORFNames=A0J61_04885 {ECO:0000313|EMBL:OBZ87058.1};
OS   Choanephora cucurbitarum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC   Choanephora.
OX   NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ87058.1, ECO:0000313|Proteomes:UP000093000};
RN   [1] {ECO:0000313|EMBL:OBZ87058.1, ECO:0000313|Proteomes:UP000093000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ87058.1,
RC   ECO:0000313|Proteomes:UP000093000};
RA   Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT   "Choanephora cucurbitarum.";
RL   Submitted (MAR-2016) 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:OBZ87058.1}.
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DR   EMBL; LUGH01000250; OBZ87058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7NDD3; -.
DR   STRING; 101091.A0A1C7NDD3; -.
DR   InParanoid; A0A1C7NDD3; -.
DR   OrthoDB; 47465at2759; -.
DR   Proteomes; UP000093000; Unassembled WGS sequence.
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:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 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:UP000093000}.
FT   DOMAIN          49..206
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   245 AA;  27026 MW;  F66466D66749FCBD CRC64;
     MFAARRIAAS LAPRVAFSAS IRPAVSVAQK SVIRPTAVRF LNTIEPKRAT VQHPAPEWTA
     NALVDGEFKE LSLSDFKGFK VLVFYPADFT FVCPTELLAF SDRIDEFKKL GADVIGISVD
     NVFSHLAWTN VPRKQGGLGD IKIPLVSDIK KEISTNYNVL IPEEGLALRG LFIIDPKGIL
     RTATVHDLPI GRSVDETLRV IEAIKYTDEH GEVCPANWTK GEKTIKPDPK GSQEYFNAVD
     LTGYN
//
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