MSRA1_SYNY3
ID MSRA1_SYNY3 Reviewed; 222 AA.
AC P72622;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 1;
DE Short=Protein-methionine-S-oxide reductase 1;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 1;
DE Short=Peptide Met(O) reductase 1;
GN Name=msrA1; OrderedLocusNames=sll1394;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 (By similarity). {ECO:0000250}.
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;
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;
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA16624.1; -; Genomic_DNA.
DR PIR; S74472; S74472.
DR AlphaFoldDB; P72622; -.
DR SMR; P72622; -.
DR IntAct; P72622; 5.
DR STRING; 1148.1651696; -.
DR PaxDb; P72622; -.
DR EnsemblBacteria; BAA16624; BAA16624; BAA16624.
DR KEGG; syn:sll1394; -.
DR eggNOG; COG0225; Bacteria.
DR InParanoid; P72622; -.
DR OMA; AGPFYYA; -.
DR PhylomeDB; P72622; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
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 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..222
FT /note="Peptide methionine sulfoxide reductase MsrA 1"
FT /id="PRO_0000138601"
FT ACT_SITE 57
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24209 MW; 6F4FD8FA00027AA2 CRC64;
MGFFDLFGKK TAMVAPNEAL PGRSATMPVP DKHFVNGNPL KAPFPQGMET ALFGLGCFWG
AERKFWQIPG VYSTAVGYAA GYTPNPTYQE VCTGMTGHNE VVLVAFDPQQ VSYDQLLKVF
WESHNPTQGM RQGNDVGTQY RSGIYTYSEA QQQAALASKQ AYQQALQQAG YGEITTEILP
APDFYYAEDY HQQYLAKNPN GYCGLGGTNV ACPIGTEVSL GA
