ID A0A371HFN6_MUCPR Unreviewed; 298 AA.
AC A0A371HFN6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
DE Flags: Fragment;
GN Name=PRXIIF {ECO:0000313|EMBL:RDY01606.1};
GN ORFNames=CR513_15042 {ECO:0000313|EMBL:RDY01606.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY01606.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDY01606.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDY01606.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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: 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:RDY01606.1}.
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DR EMBL; QJKJ01002726; RDY01606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371HFN6; -.
DR STRING; 157652.A0A371HFN6; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
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:SF34; PEROXIREDOXIN-2F, MITOCHONDRIAL; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|RuleBase:RU366011};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW Peroxidase {ECO:0000256|RuleBase:RU366011};
KW Redox-active center {ECO:0000256|RuleBase:RU366011}.
FT DOMAIN 33..174
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 85
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:RDY01606.1"
SQ SEQUENCE 298 AA; 32621 MW; 4EC4D0D2A046CAFE CRC64;
MASAMVNRGG SSIFKSVSAA LGTRFYAKVA TGTDIVSAAP NVSLQKARTW DEGVASKFST
TPLKDIFKDK KVVIFGLPGA YTGVCSNKHV PTYKENIDKF KAKGIDSVIC VAINDPYTMN
AWAEKLQAQN SIEFYGDFDG SFHKSLELST DLSRALLGTR SQRWSAYVVD GKIKSLNVEK
APTEVKYWTS SSRPWMQGMA PALVRRLSKS LSATLGLRSS PSLAKVTIGT DILSIAPNVS
LQKARTWDQG LSSNFSTTPL IHIFKVQFQS LLSFASLTFL NVLSHHVSGQ ETRHLWNT
//
