ID   MTNA_XENTR              Reviewed;         354 AA.
AC   Q0VFN1; Q28DT8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Name=mri1; ORFNames=TGas129a07.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR848601; CAJ83906.1; -; mRNA.
DR   EMBL; BC118767; AAI18768.1; -; mRNA.
DR   RefSeq; NP_001016877.1; NM_001016877.2.
DR   AlphaFoldDB; Q0VFN1; -.
DR   SMR; Q0VFN1; -.
DR   STRING; 8364.ENSXETP00000021859; -.
DR   PaxDb; Q0VFN1; -.
DR   PRIDE; Q0VFN1; -.
DR   DNASU; 549631; -.
DR   GeneID; 549631; -.
DR   KEGG; xtr:549631; -.
DR   CTD; 84245; -.
DR   Xenbase; XB-GENE-974909; mri1.
DR   eggNOG; KOG1468; Eukaryota.
DR   InParanoid; Q0VFN1; -.
DR   OrthoDB; 1410886at2759; -.
DR   Reactome; R-XTR-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021867; Expressed in gastrula and 13 other tissues.
DR   ExpressionAtlas; Q0VFN1; baseline.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000317329"
FT   ACT_SITE        246
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            166
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   CONFLICT        63
FT                   /note="L -> R (in Ref. 1; CAJ83906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  37880 MW;  EFC6FC753629DD88 CRC64;
     MSLESVRYSR GSLQVLNQLL LPHKSEYEPV TGVQQGADAI RTMKVRGAPA IAIVGVLSLA
     VELTSRTCQD VPSFIAFVQE SLCHLVDARP TAVNMKKAAD ELNAFLAKEA EKAGATTQGL
     AESVIQWAEA LLKKDVEDNQ MIGDFGAKHI LETAGPTEKV CMLTHCNTGS LATAGYGTAL
     GVVRSLHVLG RLSHVFCTET RPYNQGSRLT AYELVYEKIP ATLITDSMAS AAIRDRKVTA
     VVVGADRVVA NGDTANKIGT YQLAITARYH GIPFYVAAPS TSCDLSLPTG GSIVIEERPS
     HELTDINGVR IAAPGIGVWN PAFDVTPHEL ITGIITERGV FKPEELRDGL TKGQ