(data stored in SCRATCH zone)

SWISSPROT: C0ZLP7_RHOE4

ID   C0ZLP7_RHOE4            Unreviewed;       237 AA.
AC   C0ZLP7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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:BAH30874.1};
GN   OrderedLocusNames=RER_01660 {ECO:0000313|EMBL:BAH30874.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH30874.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH30874.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH30874.1; -; Genomic_DNA.
DR   RefSeq; WP_020905733.1; NC_012490.1.
DR   STRING; 234621.RER_01660; -.
DR   EnsemblBacteria; BAH30874; BAH30874; RER_01660.
DR   GeneID; 31540040; -.
DR   KEGG; rer:RER_01660; -.
DR   PATRIC; fig|234621.6.peg.596; -.
DR   eggNOG; ENOG4108HW8; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263862; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   Proteomes; UP000002204; 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; C0ZLP7.
DR   SWISS-2DPAGE; C0ZLP7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
KW   ECO:0000256|SAAS:SAAS00102831, ECO:0000313|EMBL:BAH30874.1}.
FT   DOMAIN       54    207       PMSR. {ECO:0000259|Pfam:PF01625}.
FT   ACT_SITE     61     61       {ECO:0000256|HAMAP-Rule:MF_01401}.
SQ   SEQUENCE   237 AA;  25827 MW;  7F39227F5EBECC51 CRC64;
     MSWYDDILGR ASAKSTLIAP EDALPGREQK MPVPTAHYVN GHPLTPPFPA ELQTVVVGMG
     CFWGAEKEFW QLPGVYTTAA GYAGGFTPNP TYEETCSGRT GHTEVVLVVF DPAVISYEQI
     LAHFWENHDP TQGMRQGNDQ GSQYRSAIFT TSAEQEEIAH ASAVAFGERL AEAGYGAITT
     EIGPLRDFFY AEDYHQQYLA KNPGGYCPVH ATGVSCPVGL LRQDQVPAQT DILPPSE
//

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