ID   MTNA_NEMVE              Reviewed;         350 AA.
AC   A7RF00;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=v1g237765;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(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; DS469507; EDO49882.1; -; Genomic_DNA.
DR   RefSeq; XP_001641945.1; XM_001641895.1.
DR   AlphaFoldDB; A7RF00; -.
DR   SMR; A7RF00; -.
DR   STRING; 45351.EDO49882; -.
DR   EnsemblMetazoa; EDO49882; EDO49882; NEMVEDRAFT_v1g237765.
DR   GeneID; 5522310; -.
DR   KEGG; nve:5522310; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   HOGENOM; CLU_016218_1_3_1; -.
DR   InParanoid; A7RF00; -.
DR   OMA; RLWVDET; -.
DR   OrthoDB; 1410886at2759; -.
DR   PhylomeDB; A7RF00; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001593; 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; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Isomerase; Methionine biosynthesis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000401987"
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            161
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   350 AA;  37569 MW;  8D6D19F9368AB799 CRC64;
     MSLEAIKYKK GRLEILNQLL LPHESTYEVV SDTEDGWKAI REMKVRGAPA IAIVGALSLA
     AEIYSKPFAS SEELAEFVKQ KLQYLNTARP TAVNMTNAVI ELTAFVADLT KCSPKDMKQK
     LLSKIEGMLS EDIAQNKAIG KFGAESILGA VGGPVRMLTH CNTGSLATAG YGTGLGVIRS
     IHEMKQLEHV YCTETRPYNQ GSRLTAYELV YEKIPSTLIA DSAVSMAMKT KKISAVVVGA
     DRIACNGDTA NKIGTYQLAL AAKHHEIPFY VAAPVTSIDF SLVNGDAIVI EERSPLELTS
     VKGIPVAASG IGVWNPAFDV TPAGLITGIV TEHGTFSPQE MKDKLLALKG