MSRA2_NOSS1
ID MSRA2_NOSS1 Reviewed; 222 AA.
AC Q8YWD8;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=alr1675;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(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 (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; BA000019; BAB78041.1; -; Genomic_DNA.
DR PIR; AE2015; AE2015.
DR RefSeq; WP_010995844.1; NZ_RSCN01000013.1.
DR AlphaFoldDB; Q8YWD8; -.
DR SMR; Q8YWD8; -.
DR STRING; 103690.17135495; -.
DR EnsemblBacteria; BAB78041; BAB78041; BAB78041.
DR KEGG; ana:alr1675; -.
DR eggNOG; COG0225; Bacteria.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1554384at2; -.
DR Proteomes; UP000002483; 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..222
FT /note="Peptide methionine sulfoxide reductase MsrA 2"
FT /id="PRO_0000138528"
FT ACT_SITE 56
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24358 MW; 145350789FDAA98A CRC64;
MALFGFGKKL ALPTPEKALP GRAQIMPVPA NHYVNKNPLK PPFPDGFEKA LFGLGCFWGA
ERKFWQQQGV YSTAVGYAAG FTPNPTYDEV CTGLTGHNEV VLVVFDPKVI SYTQLLKVFW
ESHNPTQGMR QGNDVGTQYR SGIYVYSEAQ KQLAEASRDA YQQALSSAGY EKITTEILDA
PEFYYAEAYH QQYLAKNPNG YCGLGGTNVA CPVGVFESSA NG
