ID A0A2E9CGQ6_9ARCH Unreviewed; 165 AA.
AC A0A2E9CGQ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin Q {ECO:0000256|ARBA:ARBA00042163};
GN ORFNames=CME83_06935 {ECO:0000313|EMBL:MBS86267.1};
OS Candidatus Heimdallarchaeota archaeon.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=2026747 {ECO:0000313|EMBL:MBS86267.1, ECO:0000313|Proteomes:UP000228988};
RN [1] {ECO:0000313|Proteomes:UP000228988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000256|ARBA:ARBA00004456}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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:MBS86267.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PBWW01000074; MBS86267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E9CGQ6; -.
DR Proteomes; UP000228988; Unassembled WGS sequence.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF4; AHPC_TSA FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 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|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:MBS86267.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 12..165
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 165 AA; 19185 MW; B8CC8FF339B14DEE CRC64;
MIYDFILNMT QFKEGDDFPE FSLKNQKDEK ISKSDLDGQK FILFSYPRAL TPGCTKEVCS
IRDNFTLLEN KGFKIFGISN DPHDKNKKFA DKYELQYDLL SDVNAELLEK IGAYGEKQMY
GNTYMGTIRK SYIVDEKHKV RKIFNKVKTA THGDELLNEI NQLDL
//