ID   B4FN24_MAIZE            Unreviewed;       162 AA.
AC   B4FN24;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   04-NOV-2026, entry version 115.
DE   RecName: Full=Glutaredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013016, ECO:0000256|RuleBase:RU366011};
DE            EC=1.11.1.25 {ECO:0000256|ARBA:ARBA00013016, ECO:0000256|RuleBase:RU366011};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF83517.1};
RN   [1] {ECO:0000313|EMBL:ACG27262.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [2] {ECO:0000313|EMBL:ACF83517.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF83517.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000256|RuleBase:RU366011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutaredoxin]-dithiol + a hydroperoxide = [glutaredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62624, Rhea:RHEA-
CC         COMP:10729, Rhea:RHEA-COMP:10730, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00001711};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00691}.
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DR   EMBL; BT038512; ACF83517.1; -; mRNA.
DR   EMBL; EU955144; ACG27262.1; -; mRNA.
DR   EMBL; EU964599; ACG36717.1; -; mRNA.
DR   RefSeq; NP_001232829.1; NM_001245900.1.
DR   AlphaFoldDB; B4FN24; -.
DR   SMR; B4FN24; -.
DR   IntAct; B4FN24; 8.
DR   STRING; 4577.B4FN24; -.
DR   PaxDb; 4577-B4FN24; -.
DR   GeneID; 100283392; -.
DR   KEGG; zma:100283392; -.
DR   eggNOG; KOG0541; Eukaryota.
DR   HOGENOM; CLU_072440_1_2_1; -.
DR   OrthoDB; 1882547at2759; -.
DR   GO; GO:0005737; C:cytoplasm; 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:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   CDD; cd03013; PRX5_like; 1.
DR   FunFam; 3.40.30.10:FF:000020; Peroxiredoxin; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF8; PEROXIREDOXIN-2A-RELATED; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|RuleBase:RU366011};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366011};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU366011};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU366011}.
FT   DOMAIN          4..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        51
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ   SEQUENCE   162 AA;  17323 MW;  F0552B51FE01DB2C CRC64;
     MAPIAVGDAL PDGQLGWFDE NDQLQQVSVH ALAAGKKVIL FGVPGAFTPT CSNQHVPGFI
     TQAEQLKAKG VDEILLISVN DPFVMKAWAK TYPENKHVKF LADGSGAYTK ALDLELDLTD
     KGLGVRSKRF ALLADDLTVT VANIEEGGQF TISGAEEILK AL
//