MSRA_CORDI
ID MSRA_CORDI Reviewed; 220 AA.
AC Q6NEL2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=DIP2260;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX248360; CAE50784.1; -; Genomic_DNA.
DR RefSeq; WP_010935710.1; NC_002935.2.
DR PDB; 4D7L; X-ray; 1.90 A; A/B/C=1-220.
DR PDBsum; 4D7L; -.
DR AlphaFoldDB; Q6NEL2; -.
DR SMR; Q6NEL2; -.
DR STRING; 257309.DIP2260; -.
DR EnsemblBacteria; CAE50784; CAE50784; DIP2260.
DR GeneID; 47688814; -.
DR KEGG; cdi:DIP2260; -.
DR HOGENOM; CLU_031040_10_3_11; -.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1554384at2; -.
DR Proteomes; UP000002198; Chromosome.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..220
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138541"
FT ACT_SITE 52
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01401"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4D7L"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4D7L"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4D7L"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 146..166
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4D7L"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4D7L"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:4D7L"
SQ SEQUENCE 220 AA; 23950 MW; A8D61CDBBF509BBF CRC64;
MGWLFGAPRL VEEKDALKGG PHPVLPNPQP HAVLGTLRGQ PGTETIYIGI GCYWGAEKLF
WETPGVVYTS VGFAGGITPN PTYRETCTGR TNHTEIVEVV YDPTQVTFDE LVVKAMEAHD
PTQGYRQGND TGTQYRSAIY TAGPNAEQQA QRAREIVEHY APKLAAAGLG RITTEILPLA
STPAGEYYMA EDEHQQYLHK NPLGYCPHHS TGVACGIPEA
