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MTNA_DROAN
ID   MTNA_DROAN              Reviewed;         364 AA.
AC   B3M098;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=GF17194;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV42055.1; -; Genomic_DNA.
DR   RefSeq; XP_001953494.1; XM_001953458.2.
DR   RefSeq; XP_014766304.1; XM_014910818.1.
DR   RefSeq; XP_014766305.1; XM_014910819.1.
DR   AlphaFoldDB; B3M098; -.
DR   SMR; B3M098; -.
DR   STRING; 7217.FBpp0120386; -.
DR   EnsemblMetazoa; FBtr0121894; FBpp0120386; FBgn0094212.
DR   EnsemblMetazoa; FBtr0382330; FBpp0342553; FBgn0094212.
DR   EnsemblMetazoa; FBtr0390174; FBpp0349719; FBgn0094212.
DR   GeneID; 6499981; -.
DR   KEGG; dan:6499981; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   InParanoid; B3M098; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1410886at2759; -.
DR   PhylomeDB; B3M098; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000007801; 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_0000401975"
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;  39093 MW;  8CB4D93D65E7CD82 CRC64;
     MSLQSIKYSR GSLDILDQLL LPVQSKYVAV RGVEDGWKVI NKMQVRGAPA IAIVGCLSLA
     VEIYPEEFES KKRLRQEVEG KLNYLVSARP TAVNMKIAAD ELLALANDLT KDETIDVAGM
     KERFLNATEA MLEKDIADNQ AIGSHGAQAI LKRVAEAAGA QTGTAGPVRV LTHCNTGSLA
     TAGYGTALGV VRQLAELGKL EHVYCTETRP YNQGARLTAY ELVHEKFPAT LVLDSMVAAL
     LRAKNVAGVV VGADRVAANG DTANKIGTYQ IAVVAKHHGV PFYVAAPLTS IDLAIPGGDH
     IIIEERPDRE MTHVGEHRIA APGINCWNPA FDVTPASLIT GIITERGVFK PEELKEAITK
     LLES
 
 
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