(data stored in ACNUC1104 zone)

SWISSPROT: D3UYW2_XENBS

ID   D3UYW2_XENBS            Unreviewed;       215 AA.
AC   D3UYW2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE            Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
GN   Name=msrA {ECO:0000256|HAMAP-Rule:MF_01401,
GN   ECO:0000313|EMBL:CBJ79490.1};
GN   OrderedLocusNames=XBJ1_0340 {ECO:0000313|EMBL:CBJ79490.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79490.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79490.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79490.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine. {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine =
CC         [thioredoxin]-dithiol + L-methionine (S)-S-oxide;
CC         Xref=Rhea:RHEA:19993, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58772;
CC         EC=1.8.4.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115769};
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-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:44120, ChEBI:CHEBI:50058; EC=1.8.4.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115765};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00577793}.
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DR   EMBL; FN667741; CBJ79490.1; -; Genomic_DNA.
DR   RefSeq; WP_012986950.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0340; -.
DR   EnsemblBacteria; CBJ79490; CBJ79490; XBJ1_0340.
DR   GeneID; 8829965; -.
DR   KEGG; xbo:XBJ1_0340; -.
DR   PATRIC; fig|406818.4.peg.312; -.
DR   eggNOG; ENOG4107QXP; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263862; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   BioCyc; XBOV406818:XBJ1_RS01480-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYW2.
DR   SWISS-2DPAGE; D3UYW2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
KW   ECO:0000256|SAAS:SAAS00102831, ECO:0000313|EMBL:CBJ79490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       47    200       PMSR. {ECO:0000259|Pfam:PF01625}.
FT   ACT_SITE     53     53       {ECO:0000256|HAMAP-Rule:MF_01401}.
SQ   SEQUENCE   215 AA;  24160 MW;  AAA8D17A7EC1A556 CRC64;
     MPNSANESQH VSTQDALLGR AIPLTVSPYH VITQHSINDI PENMEIAYIG MGCFWGVERL
     FWQQEGIYTT SVGYSGGTTP NPTYEEVCTG LTGHAEVVRI VFDPTKITYG QLLTLFWENH
     DPAQGMRQHG DIGTQYRSAI YTISSQQYEQ ALATREQFQQ AMNENGDQRT ITTEIHAAKP
     FYFAEDYHQQ YLFKNPEGYC GLGGIGVCLL PTHKN
//

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