ID A0A263NZ02_9PSED Unreviewed; 215 AA. AC A0A263NZ02; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 07-OCT-2020, entry version 11. 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=B7453_03400 {ECO:0000313|EMBL:OZO05846.1}; OS Pseudomonas sp. IB20. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1702250 {ECO:0000313|EMBL:OZO05846.1, ECO:0000313|Proteomes:UP000215734}; RN [1] {ECO:0000313|EMBL:OZO05846.1, ECO:0000313|Proteomes:UP000215734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IB20 {ECO:0000313|EMBL:OZO05846.1, RC ECO:0000313|Proteomes:UP000215734}; RA Lira F., Olivares Pacheco J.A.; RT "Antartic Pseudomonas sp. IB20 genome sequencing and assembly."; RL Submitted (JUL-2017) 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|HAMAP-Rule:MF_01401}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OZO05846.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NMRE01000005; OZO05846.1; -; Genomic_DNA. DR Proteomes; UP000215734; Unassembled WGS sequence. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1060.10; -; 1. DR HAMAP; MF_01401; MsrA; 1. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA. 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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01401}. FT DOMAIN 52..204 FT /note="PMSR" FT /evidence="ECO:0000259|Pfam:PF01625" FT ACT_SITE 58 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401" SQ SEQUENCE 215 AA; 23669 MW; 9F69674F26F952EE CRC64; MVLRSEILVN KNVLPTQEQA LPGRETPMNL PQTHFVNGNP LLGPFVDNVE FAIFGLGCFW GAERKFWQRD GVVSTVVGYA GGYTPNPTYE EVCSGLTGHS EVVLVVFDQD KISYEELLKM FWELHNPTQG MRQGNDIGSQ YRSVIYAVKP EHLEAAKASA EAYQGELTKA GLGTITTEIE EAPTVYFAEA YHQQYLAKNP QGYCGIGGTG VTCPI //