MSRA2_SYNY3
ID MSRA2_SYNY3 Reviewed; 214 AA.
AC P72800;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 2;
DE Short=Protein-methionine-S-oxide reductase 2;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 2;
DE Short=Peptide Met(O) reductase 2;
GN Name=msrA2; OrderedLocusNames=slr1795;
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; BAA16815.1; -; Genomic_DNA.
DR PIR; S74663; S74663.
DR AlphaFoldDB; P72800; -.
DR SMR; P72800; -.
DR IntAct; P72800; 1.
DR STRING; 1148.1651888; -.
DR PaxDb; P72800; -.
DR PRIDE; P72800; -.
DR EnsemblBacteria; BAA16815; BAA16815; BAA16815.
DR KEGG; syn:slr1795; -.
DR eggNOG; COG0225; Bacteria.
DR InParanoid; P72800; -.
DR OMA; MEAVFEH; -.
DR PhylomeDB; P72800; -.
DR Proteomes; UP000001425; 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 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..214
FT /note="Peptide methionine sulfoxide reductase MsrA 2"
FT /id="PRO_0000138602"
FT ACT_SITE 45
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 23605 MW; 785DEAB941703338 CRC64;
MGLAIAVGSF LISPFSKVIP DPVVDINPVS TTARGTEKAV FAGGCFWGLE AMFEEVRGVK
DVQTGYSGGT EATANYARVS GGGTDHAESI EIVYDPAQVS YGELLKIFFS VGHDPTQVNR
QGVDQGRQYR SAIFATTPEQ KQVAQAYIDQ LEESQAFDQA IATEVNDFDA FYPAEDYHQD
FVQRNPAHPY VLVHDLPKLR KFRQQYSDKL KAQS
