ID A0A0K9HBA3_9BACI Unreviewed; 318 AA. AC A0A0K9HBA3; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 03-MAY-2023, entry version 38. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401}; DE Includes: 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}; DE Includes: DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400}; DE EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400}; DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400}; GN Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400}; GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401}; GN ORFNames=AC623_19320 {ECO:0000313|EMBL:KMY55822.1}; OS Bacillus sp. FJAT-27231. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY55822.1, ECO:0000313|Proteomes:UP000037077}; RN [1] {ECO:0000313|Proteomes:UP000037077} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H., RA Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (JUL-2015) 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-(R)-S-oxide-[protein]; CC Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764, CC ChEBI:CHEBI:50058; EC=1.8.4.12; CC Evidence={ECO:0000256|ARBA:ARBA00001795, ECO:0000256|HAMAP- CC Rule:MF_01400}; 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 -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. CC {ECO:0000256|HAMAP-Rule:MF_01400}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}. 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:KMY55822.1}. 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; LFZU01000001; KMY55822.1; -; Genomic_DNA. DR RefSeq; WP_049665720.1; NZ_LFZU01000001.1. DR AlphaFoldDB; A0A0K9HBA3; -. DR STRING; 1679168.AC623_19320; -. DR EnsemblBacteria; KMY55822; KMY55822; AC623_19320. DR PATRIC; fig|1679168.3.peg.4142; -. DR OrthoDB; 4174719at2; -. DR Proteomes; UP000037077; Unassembled WGS sequence. DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA. DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule. 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; 2.170.150.20; Peptide methionine sulfoxide reductase; 1. DR Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1. DR HAMAP; MF_01401; MsrA; 1. DR HAMAP; MF_01400; MsrB; 1. DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom. DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf. DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom. DR InterPro; IPR011057; Mss4-like_sf. 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 Pfam; PF01641; SelR; 1. DR SUPFAM; SSF51316; Mss4-like; 1. DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1. DR TIGRFAMs; TIGR00357; methionine-R-sulfoxide reductase; 1. DR TIGRFAMs; TIGR00401; msrA; 1. DR PROSITE; PS51790; MSRB; 1. PE 3: Inferred from homology; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000037077}. FT DOMAIN 180..302 FT /note="MsrB" FT /evidence="ECO:0000259|PROSITE:PS51790" FT ACT_SITE 14 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401" FT ACT_SITE 291 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400" SQ SEQUENCE 318 AA; 36667 MW; C2B060499D7CDF29 CRC64; MAEQWKLATF AGGCFWCMVS PFDEQPGIKE VVSGYTGGHT ENPTYEEVCS DTTGHYEAVQ IKFDPAVFPY KKLVELFWQQ IDPTDAGGQF NDRGLSYKTA IFYHDEEQKE LAEASKTALE ASGRFQKPVV TAILPAGPFY RAEEKHQHYY KKNPFHYNLY REGSGRAKFI RENWKNRKTD EQLRQELTPL QYEVTKHNAT EPPFRNEYWN HIEEGIYVDI ISGEPLFSST DKYDAGCGWP SFTKPLRRIE LEEKLDTSHG MRRIEVRAKT SDSHLGHVFD DGPGPDRARY CINSAALRFV PKDKLDEEGY GEFKSLFE //