ID A0A1D8S642_9EURY Unreviewed; 177 AA.
AC A0A1D8S642;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ECO:0000313|EMBL:AOW80821.1};
GN ORFNames=HTSR_1650 {ECO:0000313|EMBL:AOW80821.1};
OS Halodesulfurarchaeum formicicum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halodesulfurarchaeum.
OX NCBI_TaxID=1873524 {ECO:0000313|EMBL:AOW80821.1, ECO:0000313|Proteomes:UP000185608};
RN [1] {ECO:0000313|EMBL:AOW80821.1, ECO:0000313|Proteomes:UP000185608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTSR1 {ECO:0000313|EMBL:AOW80821.1,
RC ECO:0000313|Proteomes:UP000185608};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Smedile F.,
RA Messina E., La Cono V., Yakimov M.M.;
RT "Discovery of anaerobic lithoheterotrophic haloarchaeon capable of sulfur
RT respiration by hydrogen and formate.";
RL Submitted (JUN-2016) 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; CP016070; AOW80821.1; -; Genomic_DNA.
DR RefSeq; WP_070365487.1; NZ_CP016070.1.
DR AlphaFoldDB; A0A1D8S642; -.
DR STRING; 1873524.HSR6_1719; -.
DR GeneID; 29829638; -.
DR KEGG; halh:HTSR_1650; -.
DR PATRIC; fig|1855411.3.peg.1655; -.
DR Proteomes; UP000185608; 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 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}.
FT DOMAIN 8..159
FT /note="Peptide methionine sulphoxide reductase MsrA"
FT /evidence="ECO:0000259|Pfam:PF01625"
FT ACT_SITE 14
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ SEQUENCE 177 AA; 19821 MW; B17684C942AB057E CRC64;
MPTDPELATF AGGCFWCTEA AFKEVPGVQS VTAGYAGGDV PDPSYEEVST GETGHVECVQ
IEYDPDTVSY VDLLGVFFRV HDPTQLNRQG PDVGSQYRSA IFAHDTTQRE TAAEFIEILL
AEDAYDEEIV TEIEDLDAFY PAEAYHQDYY EENPEDRYCT LYVEPKVKKV QAAFSEE
//
