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MTNA_THAPS
ID   MTNA_THAPS              Reviewed;         373 AA.
AC   B8C6V3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
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=THAPSDRAFT_35896;
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Schmutz J., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T.,
RA   Bruce D., Pitluck S., Rokhsar D., Armbrust V.;
RL   Submitted (SEP-2008) 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}.
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DR   EMBL; CM000644; EED90637.1; -; Genomic_DNA.
DR   RefSeq; XP_002291786.1; XM_002291750.1.
DR   AlphaFoldDB; B8C6V3; -.
DR   SMR; B8C6V3; -.
DR   STRING; 35128.Thaps35896; -.
DR   EnsemblProtists; EED90637; EED90637; THAPSDRAFT_35896.
DR   GeneID; 7445592; -.
DR   KEGG; tps:THAPSDRAFT_35896; -.
DR   eggNOG; KOG1468; Eukaryota.
DR   InParanoid; B8C6V3; -.
DR   OMA; RLWVDET; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000001449; Chromosome 8.
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..373
FT                   /note="Methylthioribose-1-phosphate isomerase"
FT                   /id="PRO_0000402006"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT   SITE            182
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ   SEQUENCE   373 AA;  40403 MW;  71F018C216A6FBFF CRC64;
     MTDPANTLRS LIFDVDSATN KATLSVLDQL RLPDETMYTK IVNVQDAWDA IRSMRIRGAP
     LIAVVAVLGL AVDLSSNELT IGELDLISGI DEVKAFVTTK MEYLKTSRPT AVNLFNAMDE
     LKSFIDDDAI KTREEVVSAI VQHAYLMLER DVSDNKAIGS HGADDLLSRH VHPEGVCVVT
     ICNTGSLATA GWGTALGVAR ELQRRGKLRS IAALETRPYN QGSRLTAYEI MQEQMPNPIL
     LCDSMAASYL KSKGADVCVV GADRVCANGD TANKIGTFQL SIIAKEMGVE FFVASPFTTL
     DVELESGDMI EIEERPDGEM LESSGAPKGM KCWNPAFDVT PAKYISGIIT EKGVLKPSAD
     GTFDVKGFVS MHS
 
 
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