(data stored in SCRATCH zone)

SWISSPROT: A4F5Y6_SACEN

ID   A4F5Y6_SACEN            Unreviewed;       227 AA.
AC   A4F5Y6;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 88.
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:CAL99460.1};
GN   OrderedLocusNames=SACE_0107 {ECO:0000313|EMBL:CAL99460.1};
GN   ORFNames=A8924_0492 {ECO:0000313|EMBL:PFG93259.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99460.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99460.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99460.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93259.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93259.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) 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:
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; AM420293; CAL99460.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93259.1; -; Genomic_DNA.
DR   RefSeq; WP_009949312.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0107; -.
DR   EnsemblBacteria; CAL99460; CAL99460; SACE_0107.
DR   KEGG; sen:SACE_0107; -.
DR   eggNOG; ENOG4107QXP; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   HOGENOM; HOG000263862; -.
DR   KO; K07304; -.
DR   OMA; MRQGGDI; -.
DR   OrthoDB; 1554384at2; -.
DR   BioCyc; SERY405948:SACE_RS00505-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
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; A4F5Y6.
DR   SWISS-2DPAGE; A4F5Y6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01401,
KW   ECO:0000256|SAAS:SAAS00102831, ECO:0000313|EMBL:CAL99460.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN       53    208       PMSR. {ECO:0000259|Pfam:PF01625}.
FT   ACT_SITE     60     60       {ECO:0000256|HAMAP-Rule:MF_01401}.
SQ   SEQUENCE   227 AA;  24749 MW;  D690FB2398710129 CRC64;
     MALFGDPFSS HKVRMVEPGD ALAGRSTPMP VSEWHAVHPD RRIVPPFPEG LATAVVGMGC
     FWGAERTFWR TEGVWSTAVG YAGGYTPNPT YEEVCSGLTG HTEAVLVVFD PKVISYEQVL
     KVFWENHDPT QGMRQGNDVG TQYRSAIYYA DDQQRQIAEA SRDQFQAALT AAGHGTVSTE
     LAPLRDFYYA ETYHQQYLSD AKNPNGYCGI GGTGVSCPVG LAMPGDS
//

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