MTNA_DROPE
ID MTNA_DROPE Reviewed; 362 AA.
AC B4GYU1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=GL27236;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479198; EDW27959.1; -; Genomic_DNA.
DR RefSeq; XP_002023756.1; XM_002023720.1.
DR AlphaFoldDB; B4GYU1; -.
DR SMR; B4GYU1; -.
DR STRING; 7234.FBpp0191343; -.
DR EnsemblMetazoa; FBtr0192851; FBpp0191343; FBgn0164817.
DR GeneID; 6598669; -.
DR KEGG; dpe:6598669; -.
DR eggNOG; KOG1468; Eukaryota.
DR HOGENOM; CLU_016218_1_3_1; -.
DR OMA; RLWVDET; -.
DR PhylomeDB; B4GYU1; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000008744; 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..362
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000401980"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 172
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ SEQUENCE 362 AA; 38958 MW; E1EC2B34DE7BAACC CRC64;
MSLQSIKYTR GSLEILDQLL LPVQSKYLPV RGVEDGWKVI NKMQVRGAPA IAIVGCLSLA
VEIHPEEFDS KKSLRQELEG KLNYLVSARP TAVNMKMAAD ELLSLANDLT KDDNVDVAAM
KQRFLNATEA MLKKDIADNR AIGAHGAKAI LQLVAAAAGA PMAGPVRVLT HCNTGSLATA
GYGTALGVVR QLSELGKLEH IYCTETRPYN QGARLTAYEL VHEKFPATLV LDSMVAALLR
AKNVAAVVVG ADRVAANGDT ANKIGTYQIA VVAKHHGVPF FVAAPLTSID LHIPSGDHII
IEERPDREMT HVGEHRIAAP GINCWNPAFD VTPASLITGI ITERGVFQPA QLKETITKLL
ET