ID MSRA_COREF Reviewed; 217 AA. AC Q8FLU6; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 20-JAN-2009, entry version 35. DE RecName: Full=Peptide methionine sulfoxide reductase msrA; DE Short=Protein-methionine-S-oxide reductase; DE EC=1.8.4.11; DE AltName: Full=Peptide-methionine (S)-S-oxide reductase; DE Short=Peptide Met(O) reductase; GN Name=msrA; OrderedLocusNames=CE2764; OS Corynebacterium efficiens. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=152794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX MEDLINE=22723752; PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., RA Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., RA Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: Has an important function as a repair enzyme for CC proteins that have been inactivated by oxidation. Catalyzes the CC reversible oxidation-reduction of methionine sulfoxide in proteins CC to methionine (By similarity). CC -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + CC H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. CC -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O = CC L-methionine (S)-S-oxide + thioredoxin. CC -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000035; BAC19574.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_739374.1; -. DR HSSP; P54149; 1FVG. DR GeneID; 1032113; -. DR GenomeReviews; BA000035_GR; CE2764. DR KEGG; cef:CE2764; -. DR NMPDR; fig|196164.1.peg.2764; -. DR HOGENOM; Q8FLU6; -. DR BioCyc; CEFF196164:CE2764-MON; -. DR BRENDA; 1.8.4.11; 277326. DR GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006464; P:protein modification process; IEA:HAMAP. DR HAMAP; MF_01401; -; 1. DR InterPro; IPR002569; MsrA. DR Gene3D; G3DSA:3.30.1060.10; MsrA; 1. DR Pfam; PF01625; PMSR; 1. DR ProDom; PD003489; PMSR; 1. DR TIGRFAMs; TIGR00401; msrA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase. FT CHAIN 1 217 Peptide methionine sulfoxide reductase FT msrA. FT /FTId=PRO_0000138542. FT ACT_SITE 56 56 By similarity. SQ SEQUENCE 217 AA; 24191 MW; 0E642BD96745EFD2 CRC64; MAFFFRPEPK MVTPEEALKG GRHPVLESPQ PHTVLGTPIT GPWKEGQKRV WIGLGCFWGV EQMYWKMDGV ESTSVGYAGG YTPNPTYREV CSGRTGHTEI VEVVYDPEKI TLAELVARGL EAHDPTQGYR QGNDVGTQYR SAFYVETGEE AETVRQIVST YGETLKSHGF GEITTEVDVI TPADYYLAED YHQQYLHKNP DGYCPHHSTG IPCGVEA //