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Database: UniProt
Entry: A0A0W1RWF6_9GAMM
LinkDB: A0A0W1RWF6_9GAMM
Original site: A0A0W1RWF6_9GAMM 
ID   A0A0W1RWF6_9GAMM        Unreviewed;       314 AA.
AC   A0A0W1RWF6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=AUR63_08635 {ECO:0000313|EMBL:KTG17690.1};
OS   Guyparkeria sp. XI15.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Thioalkalibacteraceae; Guyparkeria.
OX   NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG17690.1, ECO:0000313|Proteomes:UP000053033};
RN   [1] {ECO:0000313|Proteomes:UP000053033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT   seawater interface in the Red Sea.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|HAMAP-Rule:MF_01401}.
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         Evidence={ECO:0000256|ARBA:ARBA00001063, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
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         Evidence={ECO:0000256|ARBA:ARBA00001497, ECO:0000256|HAMAP-
CC         Rule:MF_01401};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|ARBA:ARBA00005591, ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTG17690.1}.
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DR   EMBL; LOPX01000003; KTG17690.1; -; Genomic_DNA.
DR   RefSeq; WP_058574396.1; NZ_LOPX01000003.1.
DR   AlphaFoldDB; A0A0W1RWF6; -.
DR   STRING; 1766620.AUR63_08635; -.
DR   Proteomes; UP000053033; Unassembled WGS sequence.
DR   GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.30.1060.10; Peptide methionine sulphoxide reductase MsrA; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR00401; msrA; 1.
DR   PANTHER; PTHR42799; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   PANTHER; PTHR42799:SF2; MITOCHONDRIAL PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01401}; Reference proteome {ECO:0000313|Proteomes:UP000053033};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..314
FT                   /note="Peptide methionine sulfoxide reductase MsrA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006927505"
FT   DOMAIN          29..191
FT                   /note="Peptide methionine sulphoxide reductase MsrA"
FT                   /evidence="ECO:0000259|Pfam:PF01625"
FT   DOMAIN          226..307
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ   SEQUENCE   314 AA;  34879 MW;  C640363ECCBD1685 CRC64;
     MRITRTAPLL AFWLLLLAAG SVVAGTQTVV LGMGCFWGAE MRMSKLTGVV DVEAGYAGGD
     AETVTYRDVL STARAIRRGE TDQTGHAEVV KVTFDTDKTS LERVLAGFWE NHNPTQGNRQ
     GNDIGSNYRS AVFYANDRQR QVAEETRAIY QQALAAEGFG SITTEIAPLR NYNRAETYHQ
     DYLEKNPNGY CGIGGTGVAY PGGMTESDRT ESPTAERLDA GDLQRERQLI VFEAVDCPFC
     ERFEQDILEN WQSVVPITTT LHPRPPEGWT LAKPLFGTPT IVLFEDGRET ARYTGYQGDP
     DRFRQWLAPH EPTP
//
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