MTNA_LEIMA
ID MTNA_LEIMA Reviewed; 375 AA.
AC Q4Q0R9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 25-MAY-2022, entry version 80.
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=LmjF36.4930, LmjF_36_4930;
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin;
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B.G., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAJ09465.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FR796432; CAJ09465.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001687079.1; XM_001687027.1.
DR PDB; 2A0U; X-ray; 2.10 A; A/B=1-375.
DR PDBsum; 2A0U; -.
DR AlphaFoldDB; Q4Q0R9; -.
DR SMR; Q4Q0R9; -.
DR STRING; 5664.LmjF.36.4930; -.
DR EnsemblProtists; CAJ09465; CAJ09465; LMJF_36_4930.
DR GeneID; 5655795; -.
DR KEGG; lma:LMJF_36_4930; -.
DR VEuPathDB; TriTrypDB:LmjF.36.4930; -.
DR VEuPathDB; TriTrypDB:LMJLV39_360061100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_360060900; -.
DR eggNOG; KOG1468; Eukaryota.
DR InParanoid; Q4Q0R9; -.
DR UniPathway; UPA00904; UER00874.
DR EvolutionaryTrace; Q4Q0R9; -.
DR Proteomes; UP000000542; 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; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Isomerase;
KW Methionine biosynthesis; Nucleus; Reference proteome.
FT CHAIN 1..375
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000402001"
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"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2A0U"
FT TURN 25..30
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 55..76
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 127..165
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2A0U"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:2A0U"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:2A0U"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:2A0U"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:2A0U"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:2A0U"
SQ SEQUENCE 375 AA; 40418 MW; 4AE62D1C3C66224B CRC64;
MMSKPHHATL ESIKYTPGSL RLLDQRKLPL ETVFDDVLTV EDIWSAIKEM RVRGAPAIAV
SAALGIAVAT QRKAANGELK SGREVQTFLL TSCDFVMTSR PTAVNLFNCL RDLKAQVDKL
DPTKAAAEVA QAFVELAEAV YTNDVAFNEG IMRHGAAHIL AAAKAEGRDK VSILTICNTG
ALATSRYGTA LGVVRQLFYD GKLERVYACE TRPWNQGARL TVYECVQEDI PCTLICDGAA
SSLMLNRKID AVVVGADRIC QNGDTANKIG TYNLAVSAKF HGVKLYVAAP TTTLDVKTAS
GNHVEIEERE PTEITTNLVT KQRVVADGPH LSIWNPVFDI TPSELITGGI ITEKGVQAPA
ASAPYYDIAS IIAQA
