(data stored in SCRATCH9089 zone)

SWISSPROT: MSRA_PASMU

ID   MSRA_PASMU              Reviewed;         174 AA.
AC   Q9CN40;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000255|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000255|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000255|HAMAP-Rule:MF_01401}; OrderedLocusNames=PM0605;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC       that have been inactivated by oxidation. Catalyzes the reversible
CC       oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01401}.
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-COMP:10700,
CC         Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC         ChEBI:CHEBI:50058; EC=1.8.4.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC         dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58772; EC=1.8.4.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01401}.
DR   EMBL; AE004439; AAK02689.1; -; Genomic_DNA.
DR   RefSeq; WP_005722174.1; NC_002663.1.
DR   SMR; Q9CN40; -.
DR   EnsemblBacteria; AAK02689; AAK02689; PM0605.
DR   KEGG; pmu:PM0605; -.
DR   PATRIC; fig|272843.6.peg.613; -.
DR   eggNOG; ENOG4108HW8; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263863; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   BioCyc; PMUL272843:G1FZ8-638-MONOMER; -.
DR   Proteomes; UP000000809; 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; Q9CN40.
DR   SWISS-2DPAGE; Q9CN40.
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..174
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /id="PRO_0000138563"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   174 AA;  19755 MW;  FB49FB4CCB1238C1 CRC64;
     MTQQAIFAGG CFWCVEAVFN QIKGVEKATS GYINGTTENP TYKEVCTGET GHAEAVKVEF
     DATVISYEKL LDIFFSIHNP TQLNHQGEDV GTQYRTGIYY LNDEQEQLAN KKIAELQPHF
     AEKIVTEVLP AQTFYPAEDY HQGYLLQNPQ NSYCNLVATP KFLKAKVKFE EIWK
//

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