ID A0A240C463_SERFI Unreviewed; 137 AA.
AC A0A240C463;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ECO:0000313|EMBL:SNW02412.1};
GN ORFNames=SAMEA4384070_02771 {ECO:0000313|EMBL:SNW02412.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNW02412.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNW02412.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNW02412.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01400};
CC Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC structural integrity of the protein. {ECO:0000256|HAMAP-Rule:MF_01400};
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR EMBL; LT906479; SNW02412.1; -; Genomic_DNA.
DR RefSeq; WP_061794509.1; NZ_QTUE01000001.1.
DR AlphaFoldDB; A0A240C463; -.
DR STRING; 1411141.GCA_001590885_00041; -.
DR GeneID; 75027919; -.
DR KEGG; sfj:SAMEA4384070_2771; -.
DR OrthoDB; 9785497at2; -.
DR Proteomes; UP000215134; Chromosome 1.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 2.170.150.20; Peptide methionine sulfoxide reductase; 1.
DR HAMAP; MF_01400; MsrB; 1.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR10173; METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR10173:SF52; METHIONINE-R-SULFOXIDE REDUCTASE B3; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01400};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01400}; Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01400}.
FT DOMAIN 7..129
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ SEQUENCE 137 AA; 15359 MW; 875FD08082DEFBE6 CRC64;
MAKETTPGQP VTELNEIQRY VTQERGTEAP YSGKLLHNKR EGVYHCLCCN QPLFYSETKY
DSGCGWPSFY EPVSDDAIRY LDDNSHNMHR VEIRCGHCDA HLGHVFPDGP QPTGERFCVN
SASLSFTDGE NGDKTVG
//
