ID M5C9G4_THACB Unreviewed; 178 AA.
AC M5C9G4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Alkyl hydroperoxide reductase/thiol specific antioxidant/Mal allergen {ECO:0000313|EMBL:CCO32487.1};
DE EC=1.11.1.- {ECO:0000313|EMBL:CCO32487.1};
GN Name=LbPrx1 {ECO:0000313|EMBL:CCO32487.1};
GN ORFNames=BN14_06547 {ECO:0000313|EMBL:CCO32487.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO32487.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO32487.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
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 -!- 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:CCO32487.1}.
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DR EMBL; CAOJ01009913; CCO32487.1; -; Genomic_DNA.
DR AlphaFoldDB; M5C9G4; -.
DR HOGENOM; CLU_072440_1_1_1; -.
DR Proteomes; UP000012065; 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; 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:SF16; PEROXIREDOXIN-5, 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 ECO:0000313|EMBL:CCO32487.1};
KW Peroxidase {ECO:0000256|RuleBase:RU366011, ECO:0000313|EMBL:CCO32487.1};
KW Redox-active center {ECO:0000256|RuleBase:RU366011}.
FT DOMAIN 11..178
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 66
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 178 AA; 18988 MW; 07E75ED39D08EE7D CRC64;
MSDTTKPVEV IKVGATIPEA EFPTVYWSEE LENGAACGVP SKLSTKSWAG KKVVVVAVPG
AFTPTCHVNH IPAYVKNYQA FKDKGVDQIV VIAANDPFVM SGWGRINGAK DHVLFVSDTY
AGWSKELGLD IDLTGHGLGV RTGRYALVLN DNKVEKINVE PNPGAVSNTG AEHILAAL
//
