ID A0A1H4BCU2_9BACT Unreviewed; 556 AA.
AC A0A1H4BCU2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN04487851_106138 {ECO:0000313|EMBL:SEA45874.1};
OS Prevotella sp. tc2-28.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761888 {ECO:0000313|EMBL:SEA45874.1, ECO:0000313|Proteomes:UP000199625};
RN [1] {ECO:0000313|EMBL:SEA45874.1, ECO:0000313|Proteomes:UP000199625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC2-28 {ECO:0000313|EMBL:SEA45874.1,
RC ECO:0000313|Proteomes:UP000199625};
RA de Groot N.N.;
RL Submitted (OCT-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;
CC Evidence={ECO:0000256|ARBA:ARBA00001063, 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001497, ECO:0000256|HAMAP-
CC Rule:MF_01401};
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000256|ARBA:ARBA00005591, ECO:0000256|HAMAP-Rule:MF_01401}.
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DR EMBL; FNRE01000006; SEA45874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4BCU2; -.
DR STRING; 1761888.SAMN04487851_106138; -.
DR OrthoDB; 9803578at2; -.
DR Proteomes; UP000199625; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR CDD; cd11294; E_set_Esterase_like_N; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR NCBIfam; TIGR00401; msrA; 1.
DR PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF00756; Esterase; 1.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF81296; E set domains; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199625}.
FT DOMAIN 3..153
FT /note="Peptide methionine sulphoxide reductase MsrA"
FT /evidence="ECO:0000259|Pfam:PF01625"
FT DOMAIN 200..258
FT /note="Glycoside hydrolase family 13 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02922"
FT ACT_SITE 10
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ SEQUENCE 556 AA; 63334 MW; 6412E5D417EABFFC CRC64;
MREIYLAGGC FWGTEHYFKQ IQGVLNTEVG FANGNTENPT YKEVYTDQTG YAETVHVVYD
ETVVSLEFLL NMFFKAIDPI SLNKQGHDEG TRYRTGVYYV TEDQLPIINK VFNEQQALLT
EPIAVERLPL KNFYTAEEYH QDYLDKNPDG YCHLPTALFE FARQAKEKLT VCFLLMLMTA
GSWAQQAIFD VNNLTSPQVN ADGSVTFQLY APKAITASVT GDFGVIDMKE GKGGIWSGTT
PVLEPEMYSY KYKVDGMDQL DPSNVYRCRD IASFTNIFIV TKTQGDKGWL YSVNKVRHGN
VSKVWYPSPT LKTTRRMTIY TPAGYEDGRR YPVLYLLHGA GGDEEAWTTL GRAAQILDNL
IAEGKVKPMI VVMPNGNANS DAAPGEWEKG MYKPSFMGHA TSKPVASTEE AFKDIVSYVD
KHYRTLANKK NRAICGLSMG GGHSFAISRL YPDWFNYVGL FSAYVHLDVK DSADLQAKGC
CFTPDSERML QTQFKKKLAL YWIAIGKDDF LYDNNKMYRE YLDQKGYPYE YVETDGGHIW
RNWRIYLTRF SQRLFK
//
