ID B1WRC9_CROS5 Unreviewed; 178 AA. AC B1WRC9; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 04-NOV-2026, entry version 98. 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=msrA2 {ECO:0000313|EMBL:ACB51778.1}; GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401}; GN OrderedLocusNames=cce_2430 {ECO:0000313|EMBL:ACB51778.1}; OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain OS ATCC 51142)). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae; OC Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica. OX NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB51778.1, ECO:0000313|Proteomes:UP000001203}; RN [1] {ECO:0000313|EMBL:ACB51778.1, ECO:0000313|Proteomes:UP000001203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203}; RX PubMed=18812508; DOI=10.1073/pnas.0805418105; RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.; RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium RT important in the marine nitrogen cycle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008). 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=L-methionyl-[protein] + [thioredoxin]-disulfide + H2O = L- CC methionyl-(S)-S-oxide-[protein] + [thioredoxin]-dithiol; 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:ARBA00047806, ECO:0000256|HAMAP- CC Rule:MF_01401}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + L-methionine + H2O = L-methionine CC (S)-S-oxide + [thioredoxin]-dithiol; 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:ARBA00048782, 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}. 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; CP000806; ACB51778.1; -; Genomic_DNA. DR RefSeq; WP_009544873.1; NC_010546.1. DR AlphaFoldDB; B1WRC9; -. DR STRING; 43989.cce_2430; -. DR KEGG; cyt:cce_2430; -. DR eggNOG; COG0225; Bacteria. DR HOGENOM; CLU_031040_10_0_3; -. DR OMA; ACREWPA; -. DR OrthoDB; 4174719at2; -. DR Proteomes; UP000001203; Chromosome circular. DR GO; GO:0033744; F:L-methionine (S)-S-oxide reductase activity; IEA:RHEA. DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; 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:UP000001203}. FT DOMAIN 3..174 FT /note="Peptide methionine sulphoxide reductase MsrA" FT /evidence="ECO:0000259|Pfam:PF01625" FT ACT_SITE 11 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401" SQ SEQUENCE 178 AA; 20240 MW; C64CB4C3431A93BB CRC64; MSETIVLGGG CFWCVESVYQ NVEGVESVES GYAGGETKNP TYDQVCSGRT GHAEVVKVTF NPQTISLIEI LQIFFTVSHD PTTLNRQGND VGTQYRSIIL WNSQEQLETA KQVIEKLNGE DVFNGKIVTE LKELTDYYPA EEYHQNYFKK HPNQPYCLFS IPPKLDKLKK YFPEKMLA //