ID MSRA2_SYNY3 Reviewed; 214 AA. AC P72800; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 2; DE Short=Protein-methionine-S-oxide reductase 2; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 2; DE Short=Peptide Met(O) reductase 2; GN Name=msrA2; OrderedLocusNames=slr1795; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: Has an important function as a repair enzyme for proteins CC that have been inactivated by oxidation. Catalyzes the reversible CC oxidation-reduction of methionine sulfoxide in proteins to methionine CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120, CC ChEBI:CHEBI:50058; EC=1.8.4.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]- CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, 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:58772; EC=1.8.4.11; CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family. CC {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; BA000022; BAA16815.1; -; Genomic_DNA. DR PIR; S74663; S74663. DR AlphaFoldDB; P72800; -. DR SMR; P72800; -. DR IntAct; P72800; 1. DR STRING; 1148.gene:10497672; -. DR PaxDb; 1148-1651888; -. DR EnsemblBacteria; BAA16815; BAA16815; BAA16815. DR KEGG; syn:slr1795; -. DR eggNOG; COG0225; Bacteria. DR InParanoid; P72800; -. DR PhylomeDB; P72800; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom. DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf. DR NCBIfam; TIGR00401; msrA; 1. DR PANTHER; PTHR43774; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1. DR PANTHER; PTHR43774:SF1; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2; 1. DR Pfam; PF01625; PMSR; 1. DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1. PE 3: Inferred from homology; KW Oxidoreductase; Reference proteome. FT CHAIN 1..214 FT /note="Peptide methionine sulfoxide reductase MsrA 2" FT /id="PRO_0000138602" FT ACT_SITE 45 FT /evidence="ECO:0000250" SQ SEQUENCE 214 AA; 23605 MW; 785DEAB941703338 CRC64; MGLAIAVGSF LISPFSKVIP DPVVDINPVS TTARGTEKAV FAGGCFWGLE AMFEEVRGVK DVQTGYSGGT EATANYARVS GGGTDHAESI EIVYDPAQVS YGELLKIFFS VGHDPTQVNR QGVDQGRQYR SAIFATTPEQ KQVAQAYIDQ LEESQAFDQA IATEVNDFDA FYPAEDYHQD FVQRNPAHPY VLVHDLPKLR KFRQQYSDKL KAQS //