ID   MTNA_DROSE              Reviewed;         364 AA.
AC   B4I029;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=GM12085;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(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}.
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DR   EMBL; CH480819; EDW53636.1; -; Genomic_DNA.
DR   RefSeq; XP_002037477.1; XM_002037441.1.
DR   AlphaFoldDB; B4I029; -.
DR   SMR; B4I029; -.
DR   STRING; 7238.B4I029; -.
DR   EnsemblMetazoa; FBtr0195070; FBpp0193562; FBgn0167026.
DR   GeneID; 6612986; -.
DR   KEGG; dse:6612986; -.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   OMA; RLWVDET; -.
DR   PhylomeDB; B4I029; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001292; 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   Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000401982"
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            174
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   364 AA;  39255 MW;  675975BFB337551E CRC64;
     MSLQSIKYSR GSLEILDQLL LPGQSKYVVV RGVEDGWKVI NKMQVRGAPA IAIVGCLSLA
     VEINPEDFEN KKSLRQEIEG KLNYLVSARP TAVNMKIAAD ELITLANELY KDEAIDVTQM
     KHRFLDATEA MLKKDIADNR AIGANGAQAI LQRVAKAGKT TAGTTGSVRV LTHCNTGSLA
     TAGYGTALGV VRQLAELGKL EHVYCTETRP YNQGARLTAY ELVHEKFPAT LVLDSMVAAL
     LRAKNVAAVV VGADRVASNG DTANKIGTYQ IAVVAKHHDV PFYVAAPLTS IDLAIPGGDH
     IIIEERPDRE MTHVGEHRIA APGINCWNPA FDVTPASLIT GIITERGVFK PAELKEAITK
     LLES