ID A0A3P6HDV1_ENTVE Unreviewed; 148 AA.
AC A0A3P6HDV1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499, ECO:0000256|RuleBase:RU365044};
DE EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499, ECO:0000256|RuleBase:RU365044};
GN ORFNames=EVEC_LOCUS5086 {ECO:0000313|EMBL:VDD90335.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|EMBL:VDD90335.1, ECO:0000313|Proteomes:UP000274131};
RN [1] {ECO:0000313|EMBL:VDD90335.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methionine-sulfoxide reductase that specifically reduces
CC methionine (R)-sulfoxide back to methionine. While in many cases
CC methionine oxidation is the result of random oxidation following
CC oxidative stress, methionine oxidation is also a post-translational
CC modification that takes place on specific residues.
CC {ECO:0000256|RuleBase:RU365044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU365044};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU365044};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|ARBA:ARBA00007174, ECO:0000256|RuleBase:RU365044}.
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DR EMBL; UXUI01008049; VDD90335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6HDV1; -.
DR STRING; 51028.A0A3P6HDV1; -.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR10173:SF37; METHIONINE-R-SULFOXIDE REDUCTASE B2, MITOCHONDRIAL; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU365044};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365044};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 24..147
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 148 AA; 16674 MW; FAAC57FD08D49654 CRC64;
MLSDICKGAF SKLNINKTPK EVTDEEWKKV LTPEQYEITR ESGTEKPFSG KYDKFFENGI
YHCVCCGAQL FKSDAKYNSG CGWPAFSKSV DNDLNITRIK DFSNGMERTE VRCKQCNAHL
GHVFGDGPKE TGERYCINSG SIDFAKES
//