ID   MSRA_ARATH              Reviewed;         258 AA.
AC   P54150; Q9SW13;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   05-MAY-2009, entry version 59.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Protein-methionine-S-oxide reductase;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE            Short=Peptide Met(O) reductase;
GN   Name=PMSR; OrderedLocusNames=At4g25130; ORFNames=F13M23.270;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Piffanelli P., Batchedler C., Murphy D.J.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
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.
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   -!- INTERACTION:
CC       Q42403:TRX3; NbExp=1; IntAct=EBI-449349, EBI-449157;
CC   -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
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DR   EMBL; X97326; CAA65991.1; -; Genomic_DNA.
DR   EMBL; AL035523; CAB36755.1; -; Genomic_DNA.
DR   EMBL; AL161562; CAB79422.1; -; Genomic_DNA.
DR   IPI; IPI00543565; -.
DR   PIR; T05534; T05534.
DR   RefSeq; NP_194243.1; -.
DR   UniGene; At.24140; -.
DR   HSSP; P27110; 1FF3.
DR   SMR; P54150; 78-258.
DR   IntAct; P54150; 1.
DR   PRIDE; P54150; -.
DR   GeneID; 828616; -.
DR   GenomeReviews; CT486007_GR; AT4G25130.
DR   KEGG; ath:AT4G25130; -.
DR   NMPDR; fig|3702.1.peg.20418; -.
DR   TAIR; At4g25130; -.
DR   OMA; P54150; QQKLLNR.
DR   BRENDA; 1.8.4.11; 302.
DR   ArrayExpress; P54150; -.
DR   GermOnline; AT4G25130; Arabidopsis thaliana.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Complete proteome; Oxidoreductase.
FT   CHAIN         1    258       Peptide methionine sulfoxide reductase.
FT                                /FTId=PRO_0000138632.
FT   CONFLICT    131    131       Y -> S (in Ref. 1; CAA65991).
SQ   SEQUENCE   258 AA;  28644 MW;  DCB95E4B4CF88EA1 CRC64;
     MQVLVVSPPL IAAASLSKPL NSLSKAALSF SRAKPICPFP QTSRRPISVY KSPMNNLFNR
     LGFGSRPQAQ ADPSSAAIAQ GPDDDVPSSG QQFAQFGAGC FWGVELAYQR VPGVTKTEVG
     YSHGIVHNPS YEDVCTGTTG HNEVVRVQYD PKECSFESLL DVFWNRHDPT TLNRQGGDVG
     TQYRSGIYYY TDEQERIARE AVEKQQKILN KRIVTEILPA TKFYRAENYH QQYLAKGGRM
     GLRQSAEKGC KDPIRCYG
//