MSRA3_RHIME
ID MSRA3_RHIME Reviewed; 168 AA.
AC Q92Y45;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA 3;
DE Short=Protein-methionine-S-oxide reductase 3;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase 3;
DE Short=Peptide Met(O) reductase 3;
GN Name=msrA3; OrderedLocusNames=RA1043; ORFNames=SMa1896;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AE006469; AAK65701.1; -; Genomic_DNA.
DR PIR; C95392; C95392.
DR RefSeq; NP_436289.1; NC_003037.1.
DR RefSeq; WP_010968000.1; NC_003037.1.
DR PDB; 4GWB; X-ray; 1.20 A; A=1-168.
DR PDBsum; 4GWB; -.
DR AlphaFoldDB; Q92Y45; -.
DR SMR; Q92Y45; -.
DR EnsemblBacteria; AAK65701; AAK65701; SMa1896.
DR GeneID; 61599789; -.
DR KEGG; sme:SMa1896; -.
DR PATRIC; fig|266834.11.peg.1079; -.
DR HOGENOM; CLU_031040_10_2_5; -.
DR OMA; WVLPRRS; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..168
FT /note="Peptide methionine sulfoxide reductase MsrA 3"
FT /id="PRO_0000138575"
FT ACT_SITE 11
FT /evidence="ECO:0000250"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:4GWB"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4GWB"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4GWB"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4GWB"
SQ SEQUENCE 168 AA; 19344 MW; 0FACD9C4642CDC25 CRC64;
MTKRAVLAGG CFWGMQDLIR KLPGVIETRV GYTGGDVPNA TYRNHGTHAE GIEIIFDPER
ISYRRILELF FQIHDPTTKD RQGNDIGTSY RSAIYYVDDE QKRIAQETIA DVEASGLWPG
KVVTEVEPVR DFWEAEPEHQ NYLERYPNGY TCHFPRPNWV LPRRSAAE
