MSRA2_CAUVC
ID MSRA2_CAUVC Reviewed; 196 AA.
AC Q9A9E9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=CC_1039;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005673; AAK23023.1; -; Genomic_DNA.
DR PIR; C87378; C87378.
DR RefSeq; NP_419855.1; NC_002696.2.
DR RefSeq; WP_010918923.1; NC_002696.2.
DR AlphaFoldDB; Q9A9E9; -.
DR SMR; Q9A9E9; -.
DR STRING; 190650.CC_1039; -.
DR EnsemblBacteria; AAK23023; AAK23023; CC_1039.
DR KEGG; ccr:CC_1039; -.
DR PATRIC; fig|190650.5.peg.1055; -.
DR eggNOG; COG0225; Bacteria.
DR HOGENOM; CLU_031040_10_1_5; -.
DR OMA; PYIAYND; -.
DR BioCyc; CAULO:CC1039-MON; -.
DR Proteomes; UP000001816; 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; Reference proteome.
FT CHAIN 1..196
FT /note="Peptide methionine sulfoxide reductase MsrA 2"
FT /id="PRO_0000138537"
FT ACT_SITE 36
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21916 MW; A5A50429EA8D1217 CRC64;
MRRLIVLFAA ALAVLGATAP ALAAPKTETA VFAGGCFWCM EHDMQGVPGV LKVESGYTGG
HLKNPTYRDV TSETSGHYEA VRVTYDPAKL DYGFLLYRYW RLVDPTDDGG QFCDRGPSYR
PAVFVTPAQR PIAEKSRTEA AKRLKTGTMK TQILPAQTFY LAEEYHRDYA KRNKLNYFAY
RTGCGRDARL KQVWGG
