ID A0A126YZ50_9MICO Unreviewed; 149 AA.
AC A0A126YZ50;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=peptide-methionine (R)-S-oxide reductase {ECO:0000256|ARBA:ARBA00012499};
DE EC=1.8.4.12 {ECO:0000256|ARBA:ARBA00012499};
GN ORFNames=AX769_08930 {ECO:0000313|EMBL:AMM20263.1};
OS Frondihabitans sp. PAMC 28766.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM20263.1, ECO:0000313|Proteomes:UP000070552};
RN [1] {ECO:0000313|EMBL:AMM20263.1, ECO:0000313|Proteomes:UP000070552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA Park H.;
RT "Complete genome of Frondihabitans sp.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001795};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014513; AMM20263.1; -; Genomic_DNA.
DR RefSeq; WP_066278345.1; NZ_CP014513.1.
DR AlphaFoldDB; A0A126YZ50; -.
DR STRING; 1795630.AX769_08930; -.
DR KEGG; frp:AX769_08930; -.
DR OrthoDB; 9785497at2; -.
DR Proteomes; UP000070552; Chromosome.
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:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B3; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070552}.
FT DOMAIN 7..130
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
SQ SEQUENCE 149 AA; 16521 MW; 795A45F88F85F271 CRC64;
MTDYQKTPEA LAKLTREQFH VTQRGGTEPA FRNAYHATKD AGIYVDVVTG EPLFSSLDKY
DSGTGWPSFT RPIDTSRIVE KRQGFMIFAR TEVRSASGDS HLGHVFDDGP WREGGLRYCM
NSAALRFVPL ADLEAEGYGE YAALFTSAA
//