ID Q1CX92_MYXXD Unreviewed; 407 AA.
AC Q1CX92;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 121.
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=msrBA {ECO:0000313|EMBL:ABF92291.1};
GN Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN OrderedLocusNames=MXAN_6864 {ECO:0000313|EMBL:ABF92291.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92291.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92291.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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|HAMAP-Rule:MF_01401}.
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; CP000113; ABF92291.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1CX92; -.
DR SMR; Q1CX92; -.
DR STRING; 246197.MXAN_6864; -.
DR EnsemblBacteria; ABF92291; ABF92291; MXAN_6864.
DR KEGG; mxa:MXAN_6864; -.
DR eggNOG; COG0225; Bacteria.
DR eggNOG; COG0229; Bacteria.
DR HOGENOM; CLU_031040_7_2_7; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
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; 2.170.150.20; Peptide methionine sulfoxide reductase; 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; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR NCBIfam; TIGR00401; msrA; 1.
DR NCBIfam; TIGR00357; peptide-methionine (R)-S-oxide reductase MsrB; 1.
DR PANTHER; PTHR43774; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR43774:SF1; PEPTIDE METHIONINE SULFOXIDE REDUCTASE MSRA 2; 1.
DR Pfam; PF01625; PMSR; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; Mss4-like; 1.
DR SUPFAM; SSF55068; Peptide methionine sulfoxide reductase; 1.
DR PROSITE; PS51790; MSRB; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01401}; Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 90..212
FT /note="MsrB"
FT /evidence="ECO:0000259|PROSITE:PS51790"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01401"
SQ SEQUENCE 407 AA; 44698 MW; 98FA13088714A97B CRC64;
MPGGRRPGAT ASETTWGPRA YTQKHPRSRE LPETASMPTA STSSSLARRL MPLALAALAV
LSACTEARGA APAAPGPTIQ DTRRYEKPSD ADLRRTLSPL AYEVTQKGAT EPAFRNPLWN
HHEEGLYVDV VSGEPLFSSR DKFDSGTGWP SFTRPVDSAR IVEKRDSTQG MERVEVRSKA
AGSHLGHLFG DGPAPAKTRY CINSAALRFV AVNDLAKEGY GAWLPLFGRP APAAATKRQD
TSPFTETALL AGGCFWGMED LLRKIPGVVQ TEVGYTGGSS AFRNPTYHDV SSDKTGHAEA
VRVVFDPTRL TYETLLEQWF FRMHDPTTLN RQGNDVGTQY RSAIFYLSDA QKRVAEEVKA
RVDASRKWPR PVVTQIVSAG AFTPAEDYHQ DYLVKNPGGY TCHYMRD
//
