ID   MTNA_LEIIN              Reviewed;         375 AA.
AC   A4ICE5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=LinJ36.0740, LinJ_36_5160;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5;
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(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; FR796468; CAM72523.1; -; Genomic_DNA.
DR   RefSeq; XP_001469414.1; XM_001469377.1.
DR   AlphaFoldDB; A4ICE5; -.
DR   SMR; A4ICE5; -.
DR   STRING; 5671.XP_001469414.1; -.
DR   GeneID; 5073515; -.
DR   KEGG; lif:LINJ_36_5160; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   InParanoid; A4ICE5; -.
DR   OMA; GDVIMTH; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000008153; Chromosome 36.
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..375
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000402000"
FT   ACT_SITE        257
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            177
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   375 AA;  40372 MW;  D0DA27611D839B6D CRC64;
     MMSKPHHATL ESIKYTPGSL RLLDQRKLPL ETVFDDVLTV EDIWSAINEM RVRGAPAIAV
     SAALGIAVAT QRKVANGELK SGSEVQAFFL SSCDFVMTSR PTAVNLFNCL RDLKEQVEKL
     DPTKAAAEVA QACVELAEAV YTKDVAFNEG IMRHGAAHIL AVAKAEGRDK VSILTICNTG
     ALATSRYGTA LGVVRQLFYD GKLERVYACE TRPWNQGARL TVYECVQEGI PCTLICDGAA
     SSLMLNRKID AVVVGADRIC QNGDTANKIG TYNLAVSAKF HGVKLYVAAP STTLDAKTAS
     GNRVEIEERE PTEITTNMVT KQRVVADGPH LSVWNPVFDI TPGELITGGI ITEKGVQAPT
     ASAPYYDIAS IIAQP