MSRA_PSEAE
ID MSRA_PSEAE Reviewed; 215 AA.
AC Q9HUF1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=msrA; OrderedLocusNames=PA5018;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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-(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: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG08403.1; -; Genomic_DNA.
DR PIR; B83019; B83019.
DR RefSeq; NP_253705.1; NC_002516.2.
DR RefSeq; WP_003095789.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUF1; -.
DR SMR; Q9HUF1; -.
DR STRING; 287.DR97_2373; -.
DR PaxDb; Q9HUF1; -.
DR PRIDE; Q9HUF1; -.
DR DNASU; 881240; -.
DR EnsemblBacteria; AAG08403; AAG08403; PA5018.
DR GeneID; 881240; -.
DR KEGG; pae:PA5018; -.
DR PATRIC; fig|208964.12.peg.5260; -.
DR PseudoCAP; PA5018; -.
DR HOGENOM; CLU_031040_10_3_6; -.
DR InParanoid; Q9HUF1; -.
DR OMA; AGPFYYA; -.
DR PhylomeDB; Q9HUF1; -.
DR BioCyc; PAER208964:G1FZ6-5134-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PseudoCAP.
DR GO; GO:1901530; P:response to hypochlorite; IMP:PseudoCAP.
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 Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..215
FT /note="Peptide methionine sulfoxide reductase MsrA"
FT /id="PRO_0000138566"
FT ACT_SITE 58
FT /evidence="ECO:0000250"
SQ SEQUENCE 215 AA; 23518 MW; 6B5BC8E8D63FDA6D CRC64;
MVLRSEILTK KSELPTPDQA LPGRESAMPV PEAHFVNGRP LTAPFPAGLQ QVLFGMGCFW
GAERRLWQQP GVWVTAVGYA GGYTPNPTYD EVCSGLTGHS EVVLVVYNPQ ETSFEQLLKV
FWEAHDPTQG MRQGGDIGTQ YRSVIYTFDA AQKAAAMASR ESFQAELAKA GYDRITTEIA
DVPPFYYAEA YHQQYLAKNP NGYCGLGGTG VCLPA