ID   MSRB_METBF              Reviewed;         142 AA.
AC   Q46EH1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Peptide methionine sulfoxide reductase msrB;
DE            EC=1.8.4.12;
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN   Name=msrB; OrderedLocusNames=Mbar_A0743;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. The zinc ion is important
CC       for the structural integrity of the protein (By similarity).
CC   -!- SIMILARITY: Belongs to the msrB 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; CP000099; AAZ69721.1; -; Genomic_DNA.
DR   RefSeq; YP_304301.1; -.
DR   GeneID; 3624444; -.
DR   GenomeReviews; CP000099_GR; Mbar_A0743.
DR   KEGG; mba:Mbar_A0743; -.
DR   NMPDR; fig|269797.3.peg.129; -.
DR   HOGENOM; Q46EH1; -.
DR   OMA; Q46EH1; ARVLLHH.
DR   BioCyc; MBAR269797:MBAR_A0743-MON; -.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase ac...; IEA:EC.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01400; -; 1.
DR   InterPro; IPR002579; Methionine_sulphoxide_MsrB.
DR   Gene3D; G3DSA:2.170.150.20; MsrB; 1.
DR   Pfam; PF01641; SelR; 1.
DR   ProDom; PD004057; DUF25; 1.
DR   TIGRFAMs; TIGR00357; MsrB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN         1    142       Peptide methionine sulfoxide reductase
FT                                msrB.
FT                                /FTId=PRO_1000068278.
FT   ACT_SITE    121    121       Nucleophile (By similarity).
FT   METAL        49     49       Zinc (By similarity).
FT   METAL        52     52       Zinc (By similarity).
FT   METAL        98     98       Zinc (By similarity).
FT   METAL       101    101       Zinc (By similarity).
SQ   SEQUENCE   142 AA;  16242 MW;  F1089EBB012CFD73 CRC64;
     MAQKAVEKSE EEWKKVLTPE QYHVLRQKGT ERPFSGNLYY NKEKGVYTCA ACGQELFSSD
     TKFESGTGWP SFYDVISSDR VRLKEDTSYF MNRIEVVCSR CGSHLGHVFE DGPAPTGKRY
     CINSVSLNFK TEEEGKQGEE RM
//