ID I0KH78_9BACT Unreviewed; 224 AA.
AC I0KH78;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=FAES_5482 {ECO:0000313|EMBL:CCH03481.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH03481.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCH03481.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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|HAMAP-Rule:MF_01401}.
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DR EMBL; HE796683; CCH03481.1; -; Genomic_DNA.
DR AlphaFoldDB; I0KH78; -.
DR STRING; 1166018.FAES_5482; -.
DR KEGG; fae:FAES_5482; -.
DR PATRIC; fig|1166018.3.peg.2462; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_0_10; -.
DR Proteomes; UP000011058; 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}; Reference proteome {ECO:0000313|Proteomes:UP000011058};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..224
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003631519"
FT DOMAIN 47..199
FT /note="Peptide methionine sulphoxide reductase MsrA"
FT /evidence="ECO:0000259|Pfam:PF01625"
FT ACT_SITE 54
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ SEQUENCE 224 AA; 24738 MW; 88EE92978C3C0917 CRC64;
MTTAPFRFAV TLLAIWFSVG ATAQTLPQST KSKRMTSESA SSATLEKATF GTGCFWCTEA
MFETLDGVKS AVSGYEGGQT KNPSYKDVCS GETGHAECVE VTYDPSKVTY AELLEAFFRS
HDPTSLNRQG ADVGTQYRSV VFYHNDEQKR LAETAKAELD KSGAYSKPIV TEISPATTFY
EAEAYHQNYF ANNPDQGYCA FVIAPKLDKF KKVFKEKLRA DVSH
//
