ID A0A2D0PWA4_ICTPU Unreviewed; 179 AA.
AC A0A2D0PWA4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
GN Name=msrb2 {ECO:0000313|RefSeq:XP_017309410.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017309410.1};
RN [1] {ECO:0000313|RefSeq:XP_017309410.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017309410.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58773; EC=1.8.4.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000502};
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 RefSeq; XP_017309410.1; XM_017453921.3.
DR AlphaFoldDB; A0A2D0PWA4; -.
DR STRING; 7998.ENSIPUP00000010198; -.
DR Ensembl; ENSIPUT00000010643; ENSIPUP00000010198; ENSIPUG00000006982.
DR GeneID; 108256746; -.
DR KEGG; ipu:108256746; -.
DR CTD; 22921; -.
DR OMA; CDVPLFS; -.
DR OrthoDB; 1074224at2759; -.
DR Proteomes; UP000221080; Chromosome 23.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
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}; Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 48..177
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 179 AA; 19973 MW; 1E0B412FD541409B CRC64;
MARLLVRLSS ALHNGASTQS VLSRSWSALI RPLSTTTDLL SLTRYDERVD WKKKLTPEQY
VVTREKGTEV PFSGIYLNCN DVGMYHCVCC DTPLFSSESK YDSGTGWPSF FEAHGTWERD
ESHANIIRRP DNSLGSPGTE VICKQCDGHL GHVFDDGPDP TGQRFCINSA ALNFKPREA
//
