MSRA2_RHILO
ID MSRA2_RHILO Reviewed; 195 AA.
AC Q98DV6;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 2;
DE Short=Protein-methionine-S-oxide reductase 2;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 2;
DE Short=Peptide Met(O) reductase 2;
GN Name=msrA2; OrderedLocusNames=mll4530;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(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; BA000012; BAB51164.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98DV6; -.
DR SMR; Q98DV6; -.
DR STRING; 266835.14024561; -.
DR EnsemblBacteria; BAB51164; BAB51164; BAB51164.
DR KEGG; mlo:mll4530; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_0_5; -.
DR OMA; PYIAYND; -.
DR Proteomes; UP000000552; Chromosome.
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 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.
FT CHAIN 1..195
FT /note="Peptide methionine sulfoxide reductase MsrA 2"
FT /id="PRO_0000138572"
FT ACT_SITE 18
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21351 MW; 9E1BAD9D7A4A2638 CRC64;
MDEKAAPGSE TAIFAGGCFW GVQGVFQHVK GVSKAVSGYT GGAKDDAVYE TVGTGRTGHA
ESVEITYDPS KVTYGQLLQV YFSVAHNPTQ LNFQGPDSGT QYRSTIFAEN DTQKQIAQSY
IDQLDKAKLY PAPIVTTIET GKTFYPAENY HQDFLTLNPT YPYIVYNDLP KVANLKQLFP
ALYSEKPVLV LSASN
