ID   MTNA_OSTLU              Reviewed;         365 AA.
AC   A4S068;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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   ORFNames=OSTLU_35743;
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus; unclassified Ostreococcus.
OX   NCBI_TaxID=436017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901;
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(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   -!- 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}.
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; CP000587; ABO96983.1; -; Genomic_DNA.
DR   RefSeq; XP_001418690.1; XM_001418653.1.
DR   AlphaFoldDB; A4S068; -.
DR   SMR; A4S068; -.
DR   STRING; 436017.A4S068; -.
DR   EnsemblPlants; ABO96983; ABO96983; OSTLU_35743.
DR   GeneID; 5002974; -.
DR   Gramene; ABO96983; ABO96983; OSTLU_35743.
DR   KEGG; olu:OSTLU_35743; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1410886at2759; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001568; Chromosome 7.
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   Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..365
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000401994"
FT   ACT_SITE        249
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            169
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   365 AA;  38658 MW;  3738885C6C4E59F5 CRC64;
     MSSLEAIRYA RGNLELLDQL ALPLETKYID VRDCNACWRC IKDMNVRGAP AIAIAAALAL
     AVELEAKRGT LTTCEAAEAF VRERFDHMYT SRPTAVNLGE AKNRIQALAK RLSESGDVSG
     MIEGVIEGCE AMHAEDVASC RAIGDKGAAA LLRACGAKDG ENIKVMTCCN TGSLATAGYG
     TALGVIRALW ESGRLERAYC LETRPYNQGS RLTAYELVYE KIPGTLICDN MAAALMARGD
     VDAIVVGADR VAANGDFANK IGTYSLAVNA KHHGVPMFTA APVTTLDPET ATGADIHIEE
     RPGEEVTHSL GKRVAAEGID VWNPSFDVTP AALLTGVITE HGVIEKNASG LFPVADFVAQ
     AKGGT