FRMSR_YEAST
ID FRMSR_YEAST Reviewed; 180 AA.
AC P36088; D6VXL7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Free methionine-R-sulfoxide reductase;
DE Short=fRMsr;
DE EC=1.8.4.14;
DE AltName: Full=GAF domain-containing protein YKL069W;
GN OrderedLocusNames=YKL069W; ORFNames=YKL340;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091863; DOI=10.1002/yea.320100009;
RA Rasmussen S.W.;
RT "Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100
RT gene, an open reading frame (ORF) possibly representing a nucleoside
RT diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven
RT ORFs with weak or no significant similarity to known proteins.";
RL Yeast 10:S69-S74(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF CYS-91; CYS-101 AND CYS-125.
RX PubMed=19049972; DOI=10.1074/jbc.m805891200;
RA Le D.T., Lee B.C., Marino S.M., Zhang Y., Fomenko D.E., Kaya A.,
RA Hacioglu E., Kwak G.H., Koc A., Kim H.Y., Gladyshev V.N.;
RT "Functional analysis of free methionine-R-sulfoxide reductase from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 284:4354-4364(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11032796; DOI=10.1093/emboj/19.20.5288;
RA Ho Y.S., Burden L.M., Hurley J.H.;
RT "Structure of the GAF domain, a ubiquitous signaling motif and a new class
RT of cyclic GMP receptor.";
RL EMBO J. 19:5288-5299(2000).
CC -!- FUNCTION: Catalyzes the reversible oxidation-reduction of the R-
CC enantiomer of free methionine sulfoxide to methionine. Does not act on
CC S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated
CC methionine sulfoxide. Involved in protection against oxidative stress.
CC {ECO:0000269|PubMed:19049972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (R)-S-oxide; Xref=Rhea:RHEA:21260, 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:58773; EC=1.8.4.14;
CC Evidence={ECO:0000269|PubMed:19049972};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for free methionine-R-sulfoxide
CC {ECO:0000269|PubMed:19049972};
CC Vmax=443 nmol/min/mg enzyme {ECO:0000269|PubMed:19049972};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Single deletion of fRMsr has complete growth
CC inhibition on methionine-R-sulfoxide medium and fRMsr and MXR1 double
CC deletion completely blocks the growth on both methionine-R-sulfoxide
CC and methionine-S-sulfoxide medium. FRMsr and MXR2 double deletion has
CC no effect on growth on methionine-S-sulfoxide medium. Single mutant or
CC any of the double mutants show no growth defects in methionine medium,
CC even the fRMsr, MXR1 and MXR2 triple deletion mutant is viable and
CC grows similarly to wild-type. Single deletion of fRMsr has an increased
CC sensitivity to oxidative stress and a decreased life span of 18%
CC compared to wild-type. FRMsr and MXR1, as well as fRMsr and MXR2 double
CC mutants, and fRMsr, MXR1 and MXR2 triple mutant show 20% reduction in
CC life span compared with wild-type cells. {ECO:0000269|PubMed:19049972}.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the free Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; X75780; CAA53405.1; -; Genomic_DNA.
DR EMBL; Z28069; CAA81906.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09087.1; -; Genomic_DNA.
DR PIR; S37891; S37891.
DR RefSeq; NP_012854.1; NM_001179635.1.
DR PDB; 1F5M; X-ray; 1.90 A; A/B=1-180.
DR PDB; 3KO6; X-ray; 2.55 A; A/B=1-180.
DR PDBsum; 1F5M; -.
DR PDBsum; 3KO6; -.
DR AlphaFoldDB; P36088; -.
DR SMR; P36088; -.
DR BioGRID; 34063; 358.
DR DIP; DIP-4301N; -.
DR IntAct; P36088; 4.
DR MINT; P36088; -.
DR STRING; 4932.YKL069W; -.
DR iPTMnet; P36088; -.
DR MaxQB; P36088; -.
DR PaxDb; P36088; -.
DR PRIDE; P36088; -.
DR EnsemblFungi; YKL069W_mRNA; YKL069W; YKL069W.
DR GeneID; 853794; -.
DR KEGG; sce:YKL069W; -.
DR SGD; S000001552; YKL069W.
DR VEuPathDB; FungiDB:YKL069W; -.
DR eggNOG; ENOG502RXXR; Eukaryota.
DR GeneTree; ENSGT00390000006659; -.
DR HOGENOM; CLU_077738_1_1_1; -.
DR InParanoid; P36088; -.
DR OMA; DNYIACS; -.
DR BioCyc; YEAST:G3O-31865-MON; -.
DR SABIO-RK; P36088; -.
DR EvolutionaryTrace; P36088; -.
DR PRO; PR:P36088; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36088; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0033745; F:L-methionine-(R)-S-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0070191; F:methionine-R-sulfoxide reductase activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR Gene3D; 3.30.450.40; -; 1.
DR InterPro; IPR000614; FRMsr_CS.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR Pfam; PF13185; GAF_2; 1.
DR PROSITE; PS01320; UPF0067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..180
FT /note="Free methionine-R-sulfoxide reductase"
FT /id="PRO_0000171552"
FT DOMAIN 99..177
FT /note="GAF"
FT MUTAGEN 91
FT /note="C->S: Dramatic reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19049972"
FT MUTAGEN 101
FT /note="C->S: Dramatic reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19049972"
FT MUTAGEN 125
FT /note="C->S: Dramatic reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:19049972"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:1F5M"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:1F5M"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1F5M"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1F5M"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:1F5M"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:1F5M"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:1F5M"
SQ SEQUENCE 180 AA; 19734 MW; 911158E8C0F2B0A9 CRC64;
MGSSTGFHHA DHVNYSSNLN KEEILEQLLL SYEGLSDGQV NWVCNLSNAS SLIWHAYKSL
AVDINWAGFY VTQASEENTL ILGPFQGKVA CQMIQFGKGV CGTAASTKET QIVPDVNKYP
GHIACDGETK SEIVVPIISN DGKTLGVIDI DCLDYEGFDH VDKEFLEKLA KLINKSCVFK
