ID   MTNA_YEAS7              Reviewed;         411 AA.
AC   A6ZWZ9;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 58.
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}; ORFNames=SCY_5826;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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}.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03119}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03119}.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000255|HAMAP-Rule:MF_03119}.
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DR   EMBL; AAFW02000135; EDN61241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZWZ9; -.
DR   SMR; A6ZWZ9; -.
DR   EnsemblFungi; EDN61241; EDN61241; SCY_5826.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Acetylation; Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW   Methionine biosynthesis; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q06489"
FT   CHAIN           2..411
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000402051"
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:0000250|UniProtKB:Q06489"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06489"
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