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Database: UniProt
Entry: A0A2T1CXY0_9CYAN
LinkDB: A0A2T1CXY0_9CYAN
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ID   A0A2T1CXY0_9CYAN        Unreviewed;       201 AA.
AC   A0A2T1CXY0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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=C7B76_20905 {ECO:0000313|EMBL:PSB13125.1};
OS   filamentous cyanobacterium CCP2.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB13125.1, ECO:0000313|Proteomes:UP000239512};
RN   [1] {ECO:0000313|EMBL:PSB13125.1, ECO:0000313|Proteomes:UP000239512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP2 {ECO:0000313|EMBL:PSB13125.1,
RC   ECO:0000313|Proteomes:UP000239512};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB13125.1, ECO:0000313|Proteomes:UP000239512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP2 {ECO:0000313|EMBL:PSB13125.1,
RC   ECO:0000313|Proteomes:UP000239512};
RA   Keele B.F.;
RL   Submitted (MAR-2018) 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:PSB13125.1}.
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DR   EMBL; PVWD01000180; PSB13125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1CXY0; -.
DR   OrthoDB; 9801080at2; -.
DR   Proteomes; UP000239512; 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:SF168; 2-CYS PEROXIREDOXIN BAS1, CHLOROPLASTIC; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239512}.
FT   DOMAIN          9..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        54
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   201 AA;  22458 MW;  9F97C79CCD746868 CRC64;
     MTEHAEGCIR VGQSAPDFTA TAVYDQEFKT IKLSDYRGKY VVVFFYPLDF TFVCPTEITA
     FSDRYEEFKA LNTEVLGVSV DSEFSHLAWI QTDRKSGGVG DLNYPLVSDI KKEISTAYNV
     LDPEAGVALR GLFIIDKDGI IQHATINNLA FGRSVDETLR TLQAIQYVQS HPDEVCPANW
     QPGEKTMNPD PVKSKNYFAA V
//
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