MSRAB_TREPA
ID MSRAB_TREPA Reviewed; 291 AA.
AC O83641;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB/MsrA;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB;
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE Short=Protein-methionine-S-oxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
GN Name=msrAB; Synonyms=msrA; OrderedLocusNames=TP_0633;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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}.
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 -!- 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 -!- 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 -!- SIMILARITY: In the N-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrA Met
CC sulfoxide reductase family. {ECO:0000305}.
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DR EMBL; AE000520; AAC65608.1; -; Genomic_DNA.
DR PIR; G71300; G71300.
DR RefSeq; WP_010882079.1; NC_000919.1.
DR AlphaFoldDB; O83641; -.
DR SMR; O83641; -.
DR STRING; 243276.TPANIC_0633; -.
DR EnsemblBacteria; AAC65608; AAC65608; TP_0633.
DR KEGG; tpa:TP_0633; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_7_1_12; -.
DR OMA; FWGVEYH; -.
DR Proteomes; UP000000811; Chromosome.
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; 2.
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 3: Inferred from homology;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome.
FT CHAIN 1..291
FT /note="Peptide methionine sulfoxide reductase MsrB/MsrA"
FT /id="PRO_0000138525"
FT DOMAIN 1..124
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 127..284
FT /note="Peptide methionine sulfoxide reductase A"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT ACT_SITE 135
FT /evidence="ECO:0000250"
SQ SEQUENCE 291 AA; 32802 MW; 3FF46CC8D37E8C15 CRC64;
MLANLQHLSD IQYRVTQQSA TETPFKNEFW NSYQPGFYLD VVSGELLFLS EDKFDSGCGW
PSFSAPAYAR AVIEKEDRTH NMLRTEVRSR NANSHLGHVF KDGPPERGGL RYCINSAALR
FVAREEGTAL FAAGCFWSTE AYFRRVKGVL RVRVGYTGGT TKSPTYRNVC TGTTGHAEAV
EILFDPQVIS YEDLLKHFFR MHDPTSLNKQ GGDVGTQYRS AIFYLSGTQK QQAETLMGRY
AGAGKFTRPL VTTLEEARDF YPAEEYHQDY LTKNPGGYCH VSLHLASEPL E
