ID   MSRA1_RHILO             Reviewed;         172 AA.
AC   Q98JV5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrA 1;
DE            Short=Protein-methionine-S-oxide reductase 1;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE            Short=Peptide Met(O) reductase 1;
GN   Name=msrA1; OrderedLocusNames=mll1760;
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF303099;
RX   MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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.
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DR   EMBL; BA000012; BAB49060.1; -; Genomic_DNA.
DR   RefSeq; NP_103274.1; -.
DR   HSSP; P96814; 1NWA.
DR   SMR; Q98JV5; 3-167.
DR   GeneID; 1225935; -.
DR   GenomeReviews; BA000012_GR; mll1760.
DR   KEGG; mlo:mll1760; -.
DR   NMPDR; fig|266835.1.peg.1378; -.
DR   HOGENOM; Q98JV5; -.
DR   OMA; Q98JV5; VPNATYR.
DR   BRENDA; 1.8.4.11; 3315.
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    172       Peptide methionine sulfoxide reductase
FT                                msrA 1.
FT                                /FTId=PRO_0000138571.
FT   ACT_SITE     14     14       By similarity.
SQ   SEQUENCE   172 AA;  19280 MW;  0B2C31E29596AA40 CRC64;
     MATSTERAVL AGGCFWGMQD LIRRYPGVIS TRVGYSGGDV ANATYRNHGT HAEAIEINFD
     PAVISYRTLL ERFFQIHDPT TRNRQGNDVG MSYRSAIYYT SDEQKRVAED TIADVDASGL
     WPGKVVTEVA PAGAFWEAEP EHQDYLEKYP NGYTCHFVRP GWKLPVREKA VS
//