ID H3B406_LATCH Unreviewed; 254 AA.
AC H3B406;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial {ECO:0000256|ARBA:ARBA00040356};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 3 {ECO:0000256|ARBA:ARBA00042158};
GN Name=PRDX3 {ECO:0000313|Ensembl:ENSLACP00000016627.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016627.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000016627.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01100004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01100005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005999276.1; XM_005999214.2.
DR AlphaFoldDB; H3B406; -.
DR STRING; 7897.ENSLACP00000016627; -.
DR Ensembl; ENSLACT00000016741.1; ENSLACP00000016627.1; ENSLACG00000014651.1.
DR GeneID; 102345673; -.
DR KEGG; lcm:102345673; -.
DR CTD; 10935; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; H3B406; -.
DR OMA; NNFGVMR; -.
DR OrthoDB; 47465at2759; -.
DR TreeFam; TF105181; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000014651; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
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 Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 61..219
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 254 AA; 28015 MW; 4431DF1225FB5B34 CRC64;
MAALLGRVLR AFVCHAYSCS GRISAAVRTP VALHTLNTSR VLPGYCNQRL AFSTSSAKLT
PAVTQLAPYF KGTAVVNGDF KEISLNDFKG KYLVLFFYPL DFTFVCPTEI TSFSDKAKEF
HDVNCDVVGV SVDSHFSHLA WTNIPRKNGG LGHMKIPLLS DITKQISRDY GVLLEGAGIA
LRGLFIMDTN GVLRHMSVND LPVGRKVDEV LRLVKAFQFV ETHGEVCPAD WTPDSPTIKP
TPTDSKEYFL KVNE
//
