(data stored in ACNUC29543 zone)

SWISSPROT: MSRB_SYNR3

ID   MSRB_SYNR3              Reviewed;         136 AA.
AC   A5GQT3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE            EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE   AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400};
GN   OrderedLocusNames=SynRCC307_0339;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:45764, ChEBI:CHEBI:50058; EC=1.8.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01400};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01400};
CC       Note=Binds 1 zinc ion per subunit. The zinc ion is important for
CC       the structural integrity of the protein. {ECO:0000255|HAMAP-
CC       Rule:MF_01400};
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01400}.
DR   EMBL; CT978603; CAK27242.1; -; Genomic_DNA.
DR   RefSeq; WP_011934757.1; NC_009482.1.
DR   SMR; A5GQT3; -.
DR   STRING; 316278.SynRCC307_0339; -.
DR   EnsemblBacteria; CAK27242; CAK27242; SynRCC307_0339.
DR   KEGG; syr:SynRCC307_0339; -.
DR   eggNOG; ENOG4105E0X; Bacteria.
DR   eggNOG; COG0229; LUCA.
DR   HOGENOM; HOG000243424; -.
DR   KO; K07305; -.
DR   OMA; EVGMYHC; -.
DR   OrthoDB; 1650261at2; -.
DR   BioCyc; SSP316278:G1GJL-334-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR028427; Met_Sox_Rdtase.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQT3.
DR   SWISS-2DPAGE; A5GQT3.
KW   Complete proteome; Metal-binding; Oxidoreductase; Reference proteome;
KW   Zinc.
FT   CHAIN         1    136       Peptide methionine sulfoxide reductase
FT                                MsrB.
FT                                /FTId=PRO_1000068299.
FT   DOMAIN       13    135       MsrB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
FT   METAL        52     52       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
FT   METAL        55     55       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
FT   METAL       101    101       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
FT   METAL       104    104       Zinc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01126}.
SQ   SEQUENCE   136 AA;  15458 MW;  3D49EE6FAF273274 CRC64;
     MDRTIDDPVE ASENDWRSKL TPEQFRITRE GGTERAFTGA YWNHKGDGMY RCICCGAELF
     RSDRKFDSGT GWPSFWEGVN PEAIRTIQDV SHGMVRTEIR CAKCDSHLGH VFQDSPTPTG
     LRYCVNSASL DFKDKT
//

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