ID A7T568_NEMVE Unreviewed; 179 AA.
AC A7T568;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=NEMVEDRAFT_v1g222475 {ECO:0000313|EMBL:EDO28895.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO28895.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO28895.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS471064; EDO28895.1; -; Genomic_DNA.
DR RefSeq; XP_001620995.1; XM_001620945.1.
DR AlphaFoldDB; A7T568; -.
DR STRING; 45351.A7T568; -.
DR EnsemblMetazoa; EDO28895; EDO28895; NEMVEDRAFT_v1g222475.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_1505232_0_0_1; -.
DR InParanoid; A7T568; -.
DR PhylomeDB; A7T568; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR10681:SF173; PEROXIREDOXIN-4; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..179
FT /note="thioredoxin-dependent peroxiredoxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002714893"
FT DOMAIN 137..172
FT /note="Peroxiredoxin C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10417"
SQ SEQUENCE 179 AA; 20207 MW; 067B88648AC2C308 CRC64;
MATGALFVFC FALFAFCSSA NKVEDQDQCR VYAGGQVYPE RTKISEHAVH WSKAQSSKFP
YKVCIKQVMS NSHKINSPRK EGGLGNLKYP LLSDINHQVS KDYGVLLENE GHTLSYQECT
LKLVGRSVDE TLRLVQAFQY TDKHGEVCPA GWKPGKDTII PDPTQKKKYF EKQAQKQDL
//
