(data stored in SCRATCH zone)

SWISSPROT: C5BF88_EDWI9

ID   C5BF88_EDWI9            Unreviewed;       212 AA.
AC   C5BF88;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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   OrderedLocusNames=NT01EI_0436 {ECO:0000313|EMBL:ACR67674.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67674.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin. {ECO:0000256|HAMAP-
CC       Rule:MF_01401, ECO:0000256|SAAS:SAAS00684646}.
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CC       {ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00684647}.
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401, ECO:0000256|SAAS:SAAS00684649}.
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DR   EMBL; CP001600; ACR67674.1; -; Genomic_DNA.
DR   RefSeq; WP_015869877.1; NC_012779.2.
DR   ProteinModelPortal; C5BF88; -.
DR   STRING; 634503.NT01EI_0436; -.
DR   EnsemblBacteria; ACR67674; ACR67674; NT01EI_0436.
DR   GeneID; 7961261; -.
DR   KEGG; eic:NT01EI_0436; -.
DR   PATRIC; fig|634503.3.peg.396; -.
DR   eggNOG; ENOG4107QXP; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263862; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   OrthoDB; POG091H059H; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
DR   Pfam; PF01625; PMSR; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BF88.
DR   SWISS-2DPAGE; C5BF88.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
KW   ECO:0000256|SAAS:SAAS00684651, ECO:0000313|EMBL:ACR67674.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       48    201       PMSR. {ECO:0000259|Pfam:PF01625}.
FT   ACT_SITE     54     54       {ECO:0000256|HAMAP-Rule:MF_01401}.
SQ   SEQUENCE   212 AA;  23395 MW;  3BD01151E08AA391 CRC64;
     MHHHNSSTPA PFTPAQALPG RTQAMSLSGK HALNGHDMYA IPAGMEEALF AMGCFWGVER
     LFWQQPGIYS TAAGYSGGLT PNPTYREVCS GQTGHAETVR VVFDPSLIRY DDLLRLFWQH
     HDPAQGMRQG NDVGTQYRSA LFPVTSQQMQ AAQASHTRFA QAMHQVGDLR PISTEIRAAG
     PFYYAEEEHQ QYLHKHPHGY CGVGGIGVCL PD
//

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