ID MSRB1_RHIME Reviewed; 135 AA. AC Q92RA4; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 28-JAN-2026, entry version 127. DE RecName: Full=Peptide methionine sulfoxide reductase MsrB 1; DE EC=1.8.4.12; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase 1; GN Name=msrB1; OrderedLocusNames=R00991; ORFNames=SMc00117; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481430; DOI=10.1073/pnas.161294398; RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., RA Thebault P., Vandenbol M., Weidner S., Galibert F.; RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium RT meliloti strain 1021."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11474104; DOI=10.1126/science.1060966; RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., RA Wong K., Yeh K.-C., Batut J.; RT "The composite genome of the legume symbiont Sinorhizobium meliloti."; RL Science 293:668-672(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L- CC methionyl-(R)-S-oxide-[protein] + [thioredoxin]-dithiol; 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. The zinc ion is important for the CC structural integrity of the protein. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC45563.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AL591688; CAC45563.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_010968974.1; NC_003047.1. DR AlphaFoldDB; Q92RA4; -. DR SMR; Q92RA4; -. DR EnsemblBacteria; CAC45563; CAC45563; SMc00117. DR KEGG; sme:SMc00117; -. DR PATRIC; fig|266834.11.peg.2392; -. DR eggNOG; COG0229; Bacteria. DR OrthoDB; 9785497at2; -. DR Proteomes; UP000001976; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030091; P:protein repair; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR FunFam; 2.170.150.20:FF:000001; Peptide methionine sulfoxide reductase MsrB; 1. DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1. DR HAMAP; MF_01400; MsrB; 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 B1; 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; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..135 FT /note="Peptide methionine sulfoxide reductase MsrB 1" FT /id="PRO_0000140290" FT DOMAIN 13..135 FT /note="MsrB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT ACT_SITE 124 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126" SQ SEQUENCE 135 AA; 15364 MW; F22222B102456B35 CRC64; MSENRMPKIT KTNEEWRAAL TPEQYRVTRE HGTERPFTGP FLDNKRHGTY KCVCCGRALF RSDTKFDSGC GWPSYFAPVD PDAIAEYVDR SHLMVRTEIR CADCDAHLGH VFPDGPPPTG LRYCLNGTAM TFEED //