GenomeNet

Database: UniProt/TrEMBL
Entry: C6X9S4_METSD
LinkDB: C6X9S4_METSD
Original site: C6X9S4_METSD 
ID   C6X9S4_METSD            Unreviewed;       180 AA.
AC   C6X9S4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   29-MAY-2013, entry version 30.
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;
GN   Name=msrA; OrderedLocusNames=Msip34_0646;
OS   Methylovorus sp. (strain SIP3-4) (Methylotenera sp. (strain SIP3-4)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales;
OC   Methylophilaceae; Methylovorus.
OX   NCBI_TaxID=582744;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M.,
RA   Chistoserdova L.;
RT   "Complete sequence of chromosome of Methylovorus sp. SIP3-4.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin.
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-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; CP001674; ACT49894.1; -; Genomic_DNA.
DR   RefSeq; YP_003050421.1; NC_012969.1.
DR   ProteinModelPortal; C6X9S4; -.
DR   STRING; 582744.Msip34_0646; -.
DR   EnsemblBacteria; ACT49894; ACT49894; Msip34_0646.
DR   GeneID; 8172540; -.
DR   KEGG; mei:Msip34_0646; -.
DR   PATRIC; 22616298; VBIMetSp110381_0653.
DR   eggNOG; COG0225; -.
DR   KO; K07304; -.
DR   OMA; YCLAVIP; -.
DR   ProtClustDB; CLSK2529646; -.
DR   BioCyc; MGLU582744:GHXQ-666-MONOMER; -.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:HAMAP.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:HAMAP.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1; -.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; MsrA; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase.
FT   ACT_SITE     14     14       By similarity.
SQ   SEQUENCE   180 AA;  20281 MW;  2960C96C0DA11CCB CRC64;
     MVKELDVAVL AGGCFWCLEP VFSQLDGVEK VVSGYTGGHT LQPDYKQVCR GDTGHAEAIR
     ISFDPARISF YELLEIFFLS HDPTTPNRQG NDIGTQYRSA IFCQNAAQRS TAEQMIAELN
     QLHVFASPIV TEVNDAAVFY AAEDYHQQYY EQHQEQPYCM LVAAPKVAKI RAKFPEKIRN
//
DBGET integrated database retrieval system