MSRAB_ENTFL
ID MSRAB_ENTFL Reviewed; 343 AA.
AC P86890;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Peptide methionine sulfoxide reductase msrA/msrB {ECO:0000250|UniProtKB:Q9ZMK8};
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase msrA {ECO:0000250|UniProtKB:P0A744};
DE Short=Protein-methionine-S-oxide reductase {ECO:0000250|UniProtKB:P0A744};
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000250|UniProtKB:P0A744};
DE Short=Peptide Met(O) reductase {ECO:0000250|UniProtKB:P0A744};
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase msrB {ECO:0000250|UniProtKB:P0A746};
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000250|UniProtKB:P0A746};
GN Name=msrAB {ECO:0000250|UniProtKB:Q9ZMK8};
OS Enterococcus faecalis (Streptococcus faecalis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1351;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RA Chouchani C., Marrakchi R., Aboulkacem N., Ferchichi L., El Salabi A.;
RT "Involvement of TEM-1 type beta-lactamase and efflux pumps in the defense
RT mechanisms of Enterococcus faecalis.";
RL Submitted (JAN-2011) to UniProtKB.
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 (By similarity). {ECO:0000250|UniProtKB:P0A744}.
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:0000250|UniProtKB:P0A744};
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:0000250|UniProtKB:P0A744};
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:0000250|UniProtKB:P0A746};
CC -!- SIMILARITY: In the N-terminal section; belongs to the MsrA Met
CC sulfoxide reductase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000305}.
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DR AlphaFoldDB; P86890; -.
DR SMR; P86890; -.
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-EC.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; 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; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
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; PF01625; PMSR; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Multifunctional enzyme; Oxidoreductase.
FT CHAIN 1..343
FT /note="Peptide methionine sulfoxide reductase msrA/msrB"
FT /id="PRO_0000406599"
FT DOMAIN 191..314
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 21..174
FT /note="Peptide methionine sulfoxide reductase A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZMK8"
FT ACT_SITE 29
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
SQ SEQUENCE 343 AA; 39277 MW; 3921D78C7E11A102 CRC64;
MGAIMQANEN MGSKLPKTDG KVIYLAGGCF WGLEAYMERI YGVVDASSGY ANGKTQSTNY
QKLHESDHAE SVKVVYDPKK ISLDKLLRYY FKVVDPVSVN KQGNDVGRQY RTGIYYVDNA
DKKVIDNALK ELQKSVKGKI AIEVEPLKNY VRAEIYHQDY LKKNPNGYCH IDLKKADEVI
VDSDKYTKPS DEVLKKKLTQ LQYEVTQNKR TEKPFENEYY NKEEEGIYVD ITTGEPLFSM
ADKYDSGCGW PSFSKPISKD VVKYEDDESL NMRRTEVLSR IGKAHLGHVF NDGPKELGGL
RYCINSASLR FIPLKDMEKE GYGEFIPYIK KGELKKYIHD KTH
