(data stored in SCRATCH zone)

SWISSPROT: Q3KJ53_PSEPF

ID   Q3KJ53_PSEPF            Unreviewed;       221 AA.
AC   Q3KJ53;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 114.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000256|HAMAP-Rule:MF_01401,
GN   ECO:0000313|EMBL:ABA72203.1};
GN   OrderedLocusNames=Pfl01_0459 {ECO:0000313|EMBL:ABA72203.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72203.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72203.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72203.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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. {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine =
CC         [thioredoxin]-dithiol + L-methionine (S)-S-oxide;
CC         Xref=Rhea:RHEA:19993, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58772;
CC         EC=1.8.4.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115769};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:44120, ChEBI:CHEBI:50058; EC=1.8.4.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115765};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00577793}.
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DR   EMBL; CP000094; ABA72203.1; -; Genomic_DNA.
DR   RefSeq; WP_011332125.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0459; -.
DR   PRIDE; Q3KJ53; -.
DR   EnsemblBacteria; ABA72203; ABA72203; Pfl01_0459.
DR   KEGG; pfo:Pfl01_0459; -.
DR   eggNOG; ENOG4107QXP; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263862; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   BioCyc; PFLU205922:G1G4S-464-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ53.
DR   SWISS-2DPAGE; Q3KJ53.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
KW   ECO:0000256|SAAS:SAAS00102831}.
FT   DOMAIN       53    205       PMSR. {ECO:0000259|Pfam:PF01625}.
FT   ACT_SITE     59     59       {ECO:0000256|HAMAP-Rule:MF_01401}.
SQ   SEQUENCE   221 AA;  24362 MW;  CB3E8F8E6752FCE5 CRC64;
     MVLRSEILVN KNVLPTKEQA LPGRETPMAL PEKHFVFTET PLLGPFFQDV DFAIFGLGCF
     WGAERRFWQR EGVVSTVVGY AGGFTPNPTY EEVCSGLTGH AEVVLVVFDK AKVSYEELLA
     MFWELHNPTQ GMRQGNDIGT QYRSVIYATH PEQLDAALKS KAVYQAELSK AGLGEISTEI
     EQAPTVYFAE TYHQQYLAKN PEGYCGIGGT GVCMPPSLAG N
//

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