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Database: UniProt
Entry: A0A0J7XR60_9SPHN
LinkDB: A0A0J7XR60_9SPHN
Original site: A0A0J7XR60_9SPHN 
ID   A0A0J7XR60_9SPHN        Unreviewed;       134 AA.
AC   A0A0J7XR60;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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   ORFNames=V473_18205 {ECO:0000313|EMBL:KMS54129.1};
OS   Sphingobium cupriresistens LL01.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS54129.1, ECO:0000313|Proteomes:UP000052232};
RN   [1] {ECO:0000313|EMBL:KMS54129.1, ECO:0000313|Proteomes:UP000052232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL01 {ECO:0000313|EMBL:KMS54129.1,
RC   ECO:0000313|Proteomes:UP000052232};
RX   PubMed=25850427; DOI=10.1534/g3.114.015933;
RA   Pearce S.L., Oakeshott J.G., Pandey G.;
RT   "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT   Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL   G3 (Bethesda) 5:1081-1094(2015).
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; Evidence={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}.
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:KMS54129.1}.
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DR   EMBL; JACT01000004; KMS54129.1; -; Genomic_DNA.
DR   RefSeq; WP_066607291.1; NZ_KQ130435.1.
DR   AlphaFoldDB; A0A0J7XR60; -.
DR   STRING; 1420583.V473_18205; -.
DR   PATRIC; fig|1420583.3.peg.3452; -.
DR   Proteomes; UP000052232; Unassembled WGS sequence.
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:SF57; PEPTIDE-METHIONINE (R)-S-OXIDE REDUCTASE; 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:UP000052232};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01400}.
FT   DOMAIN          8..130
FT                   /note="MsrB"
FT                   /evidence="ECO:0000259|PROSITE:PS51790"
FT   ACT_SITE        119
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01400"
SQ   SEQUENCE   134 AA;  14739 MW;  9B8AA9DDD16500D1 CRC64;
     MDKLNLSEAE WRARLSPEQY HVLREAGTER AFTGPYNGNK ADGVYYCAGC GAELFDAEEK
     YDSGSGWPSF TAPVDIDAVE EIRDASHGMV RTEVRCATCE GHLGHVFPDG PGVNGLRYCM
     NSASLDFKPR DEEA
//
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