ID A0A075B1R0_ROZAC Unreviewed; 203 AA.
AC A0A075B1R0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=O9G_002037 {ECO:0000313|EMBL:EPZ34906.1}, ROZALSC1DRAFT_27643
GN {ECO:0000313|EMBL:RKP20911.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ34906.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ34906.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ34906.1,
RC ECO:0000313|Proteomes:UP000030755}, and CSF55
RC {ECO:0000313|EMBL:EPZ34906.1};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
RN [2] {ECO:0000313|Proteomes:UP000281549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|Proteomes:UP000281549};
RX PubMed=30297742; DOI=10.1038/s41564-018-0261-0;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N.K., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the fungal tree of life.";
RL Nat. Microbiol. 3:1417-1428(2018).
RN [3] {ECO:0000313|EMBL:RKP20911.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CSF55 {ECO:0000313|EMBL:RKP20911.1};
RG DOE Joint Genome Institute;
RA Ahrendt S.R., Quandt C.A., Ciobanu D., Clum A., Salamov A.,
RA Andreopoulos B., Cheng J.-F., Woyke T., Pelin A., Henrissat B.,
RA Reynolds N., Benny G.L., Smith M.E., James T.Y., Grigoriev I.V.;
RT "Leveraging single-cell genomics to expand the Fungal Tree of Life.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KE560904; EPZ34906.1; -; Genomic_DNA.
DR EMBL; ML005008; RKP20911.1; -; Genomic_DNA.
DR STRING; 988480.A0A075B1R0; -.
DR EnsemblFungi; EPZ34906; EPZ34906; O9G_002037.
DR HOGENOM; CLU_042529_21_1_1; -.
DR OMA; KPAPEWE; -.
DR OrthoDB; 47465at2759; -.
DR Proteomes; UP000030755; Unassembled WGS sequence.
DR Proteomes; UP000281549; 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; IPR024706; Peroxiredoxin_AhpC-typ.
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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000239}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT DOMAIN 11..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 56
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 203 AA; 22501 MW; 3C2F84CFA6AB835E CRC64;
MTVETNNHVP CLIQRPAPTW SLQAVHNGEI KQIASSDYAG KDILLLFYPA DFTFVCPTEI
IAFSDRAAEF SELGCQVIAV SCDSAYSHLN WTMIPREKGG LGEMNIPILA DFNKSLSKKF
GVLLEDEGLP IRGLFIIDKK GILRHATLND LPIGRSVDEA LRTLKAIHFA DEHGEVCPVN
WTPGKKGMKP TLEGVKEYFN SKK
//
