ID W0JYU9_9EURY Unreviewed; 175 AA.
AC W0JYU9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN Name=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN ORFNames=HALLA_19990 {ECO:0000313|EMBL:AHG02183.1};
OS Halostagnicola larsenii XH-48.
OG Plasmid unnamed {ECO:0000313|EMBL:AHG02183.1}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG02183.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHG02183.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHG02183.1,
RC ECO:0000313|Proteomes:UP000019024};
RC PLASMID=4 {ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-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:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_01401};
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_01401}.
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DR EMBL; CP007058; AHG02183.1; -; Genomic_DNA.
DR RefSeq; WP_049954997.1; NZ_CP007058.1.
DR AlphaFoldDB; W0JYU9; -.
DR GeneID; 25147522; -.
DR KEGG; hlr:HALLA_19990; -.
DR PATRIC; fig|797299.3.peg.3864; -.
DR eggNOG; arCOG02816; Archaea.
DR HOGENOM; CLU_031040_10_0_2; -.
DR OrthoDB; 7150at2157; -.
DR Proteomes; UP000019024; Plasmid 4.
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 GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR NCBIfam; TIGR00401; msrA; 1.
DR PANTHER; PTHR43774; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR43774:SF1; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2; 1.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01401}; Plasmid {ECO:0000313|EMBL:AHG02183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 3..155
FT /note="Peptide methionine sulphoxide reductase MsrA"
FT /evidence="ECO:0000259|Pfam:PF01625"
FT ACT_SITE 10
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ SEQUENCE 175 AA; 19524 MW; 75A5AEBAA287961D CRC64;
MAKATFGGGC FWCVEAAFEQ LEGVESATSG YAGGDTEDPT YRAVCSGTTG HAEVVQLEYD
PETVGYEKLL EVFFTIHNPT TRDREGPDVG SQYRSAIYAH DDEQLEQAHS FVEALEAEGG
YDDPIVTEIE LLDTFYEAEP KHQNYFEKNP NDAYCSMHAA PKMEKVRERF AKQNA
//