MSRB_BURP1
ID MSRB_BURP1 Reviewed; 143 AA.
AC Q3JRF0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000255|HAMAP-Rule:MF_01400};
DE EC=1.8.4.12 {ECO:0000255|HAMAP-Rule:MF_01400};
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000255|HAMAP-Rule:MF_01400};
GN Name=msrB {ECO:0000255|HAMAP-Rule:MF_01400};
GN OrderedLocusNames=BURPS1710b_2458;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Methionine-R-sulfoxide reductase from Burkholderia pseudomallei.";
RL Submitted (MAR-2008) to the PDB data bank.
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:0000255|HAMAP-
CC Rule:MF_01400};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit. The zinc ion is important for the
CC structural integrity of the protein.;
CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01400}.
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DR EMBL; CP000124; ABA49928.1; -; Genomic_DNA.
DR RefSeq; WP_004527204.1; NC_007434.1.
DR PDB; 3CEZ; X-ray; 2.10 A; A/B=1-143.
DR PDB; 3CXK; X-ray; 1.70 A; A/B=1-143.
DR PDBsum; 3CEZ; -.
DR PDBsum; 3CXK; -.
DR AlphaFoldDB; Q3JRF0; -.
DR SMR; Q3JRF0; -.
DR EnsemblBacteria; ABA49928; ABA49928; BURPS1710b_2458.
DR GeneID; 56529144; -.
DR KEGG; bpm:BURPS1710b_2458; -.
DR HOGENOM; CLU_031040_8_5_4; -.
DR OMA; DEQWRAE; -.
DR OrthoDB; 1650261at2; -.
DR EvolutionaryTrace; Q3JRF0; -.
DR Proteomes; UP000002700; Chromosome I.
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 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 PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Oxidoreductase; Zinc.
FT CHAIN 1..143
FT /note="Peptide methionine sulfoxide reductase MsrB"
FT /id="PRO_0000338617"
FT DOMAIN 16..139
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:3CXK"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3CXK"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3CXK"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3CXK"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:3CXK"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3CXK"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3CXK"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:3CXK"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3CXK"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3CXK"
SQ SEQUENCE 143 AA; 16187 MW; F964A5CC23725C61 CRC64;
MSGDRDDPRY PYPKDDAELR RRLTPMQYEV TQHAATEPPF TGEYTDTEDA GIYHCVVCGT
ALFESGAKYH SGCGWPSYFK PIDGEVIDEK MDYTHGMTRV EVRCNQCGAH LGHVFEDGPR
DKTGLRYCIN SAALNFEAKP ERK
