ID A0A061DWX4_THECC Unreviewed; 225 AA.
AC A0A061DWX4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|RuleBase:RU365044};
DE EC=1.8.4.12 {ECO:0000256|RuleBase:RU365044};
GN ORFNames=TCM_046996 {ECO:0000313|EMBL:EOX97309.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX97309.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX97309.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
CC -!- FUNCTION: Catalyzes the reduction of methionine sulfoxide (MetSO) to
CC methionine in proteins. Plays a protective role against oxidative
CC stress by restoring activity to proteins that have been inactivated by
CC methionine oxidation. MSRB family specifically reduces the MetSO R-
CC enantiomer. {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; CM001880; EOX97309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DWX4; -.
DR STRING; 3641.A0A061DWX4; -.
DR EnsemblPlants; EOX97309; EOX97309; TCM_046996.
DR Gramene; EOX97309; EOX97309; TCM_046996.
DR eggNOG; KOG0856; Eukaryota.
DR HOGENOM; CLU_031040_8_1_1; -.
DR InParanoid; A0A061DWX4; -.
DR OMA; FVPANSW; -.
DR Proteomes; UP000026915; Chromosome 2.
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; PTHR46081; PEPTIDE METHIONINE SULFOXIDE REDUCTASE 2; 1.
DR PANTHER; PTHR46081:SF10; PEPTIDE-METHIONINE (R)-S-OXIDE REDUCTASE; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Metal-binding {ECO:0000256|RuleBase:RU365044};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365044};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|RuleBase:RU365044}.
FT DOMAIN 102..223
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 225 AA; 24400 MW; 99D518791F69B1D5 CRC64;
MGLHILKTTP FSSSSSKALL FTTATAAKPA IFSRFLNSYW RTASNPVLPS NSRLRFPSSS
PRAVTCSISS SGSGRFLHQS KRRFRGSAVV AMAASGSVQK SEEEWRAILS PEQFRILRQK
GTEYPGTGEY DKLFEEGVYN CAGCGTPLYK STTKFNSGCG WPAFYEGLPG AINRNPDPDG
MRIEITCAAC GGHLGHVFKG EGFPTPTNER HCVNSISLKF VPANS
//
