MTNA_YEAST
ID MTNA_YEAST Reviewed; 411 AA.
AC Q06489; D6W4B7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_03119};
DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_03119};
DE AltName: Full=Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein {ECO:0000255|HAMAP-Rule:MF_03119};
GN Name=MRI1 {ECO:0000255|HAMAP-Rule:MF_03119}; OrderedLocusNames=YPR118W;
GN ORFNames=P9642.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=18625006; DOI=10.1111/j.1742-4658.2008.06552.x;
RA Pirkov I., Norbeck J., Gustafsson L., Albers E.;
RT "A complete inventory of all enzymes in the eukaryotic methionine salvage
RT pathway.";
RL FEBS J. 275:4111-4120(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=15215245; DOI=10.1074/jbc.m404458200;
RA Bumann M., Djafarzadeh S., Oberholzer A.E., Bigler P., Altmann M.,
RA Trachsel H., Baumann U.;
RT "Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate
RT isomerase related to regulatory eIF2B subunits.";
RL J. Biol. Chem. 279:37087-37094(2004).
CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_03119, ECO:0000269|PubMed:15215245,
CC ECO:0000269|PubMed:18625006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03119};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 1/6. {ECO:0000255|HAMAP-Rule:MF_03119}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03119,
CC ECO:0000269|PubMed:15215245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119,
CC ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03119,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 922 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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; U40828; AAB68059.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11533.1; -; Genomic_DNA.
DR PIR; S69011; S69011.
DR RefSeq; NP_015443.1; NM_001184215.1.
DR PDB; 1W2W; X-ray; 1.75 A; A/E/I/M=1-211, B/F/J/N=221-411.
DR PDBsum; 1W2W; -.
DR AlphaFoldDB; Q06489; -.
DR SMR; Q06489; -.
DR BioGRID; 36285; 82.
DR DIP; DIP-4685N; -.
DR IntAct; Q06489; 1.
DR MINT; Q06489; -.
DR STRING; 4932.YPR118W; -.
DR iPTMnet; Q06489; -.
DR MaxQB; Q06489; -.
DR PaxDb; Q06489; -.
DR PRIDE; Q06489; -.
DR EnsemblFungi; YPR118W_mRNA; YPR118W; YPR118W.
DR GeneID; 856234; -.
DR KEGG; sce:YPR118W; -.
DR SGD; S000006322; MRI1.
DR VEuPathDB; FungiDB:YPR118W; -.
DR eggNOG; KOG1468; Eukaryota.
DR GeneTree; ENSGT00390000013732; -.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; Q06489; -.
DR OMA; RLWVDET; -.
DR BioCyc; YEAST:G3O-34257-MON; -.
DR Reactome; R-SCE-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00874.
DR EvolutionaryTrace; Q06489; -.
DR PRO; PR:Q06489; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06489; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IDA:SGD.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IMP:SGD.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR HAMAP; MF_01678; Salvage_MtnA; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR005251; IF-M1Pi.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW Methionine biosynthesis; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..411
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156110"
FT ACT_SITE 280
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1W2W"
FT TURN 23..28
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 53..73
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 129..168
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1W2W"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 261..267
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:1W2W"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:1W2W"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1W2W"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1W2W"
SQ SEQUENCE 411 AA; 45020 MW; 369B2114E12E11D8 CRC64;
MSLEAIVFDR SEPENVSVKV LDQLLLPYTT KYVPIHTIDD GYSVIKSMQV RGAPAIAIVG
SLSVLTEVQL IKHNPTSDVA TLYSLVNWES TKTVLNKRLD FLLSSRPTAV NLSNSLVEIK
NILKSSSDLK AFDGSLYNYV CELIDEDLAN NMKMGDNGAK YLIDVLQKDG FKDEFAVLTI
CNTGSLATSG YGTALGVIRS LWKDSLAKTD KADSGLDNEK CPRMGHVFPL ETRPYNQGSR
LTAYELVYDK IPSTLITDSS IAYRIRTSPI PIKAAFVGAD RIVRNGDTAN KIGTLQLAVI
CKQFGIKFFV VAPKTTIDNV TETGDDIIVE ERNPEEFKVV TGTVINPENG SLILNESGEP
ITGKVGIAPL EINVWNPAFD ITPHELIDGI ITEEGVFTKN SSGEFQLESL F
