MTNA_TRIAD
ID MTNA_TRIAD Reviewed; 360 AA.
AC B3RLE6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-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=TRIADDRAFT_19292;
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX NCBI_TaxID=10228;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999;
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985241; EDV28753.1; -; Genomic_DNA.
DR RefSeq; XP_002107955.1; XM_002107919.1.
DR AlphaFoldDB; B3RLE6; -.
DR SMR; B3RLE6; -.
DR STRING; 10228.TriadP19292; -.
DR EnsemblMetazoa; TriadT19292; TriadP19292; TriadG19292.
DR GeneID; 6749947; -.
DR KEGG; tad:TRIADDRAFT_19292; -.
DR CTD; 6749947; -.
DR eggNOG; KOG1468; Eukaryota.
DR HOGENOM; CLU_016218_1_3_1; -.
DR InParanoid; B3RLE6; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; B3RLE6; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000009022; 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..360
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000402063"
FT ACT_SITE 252
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 172
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ SEQUENCE 360 AA; 39509 MW; D0C2694C1E5151C1 CRC64;
MTEQQSLEAI RYDHDHGQLK ILNQLLLPSE YVYENVEGIE DGWQAIRQMK VRGAPAIAIV
GMLSLAVELR SKSFTEMNEF DKFIRDSLEH LKTARPTAVN IFLACDLITK LIDNLIILGD
EAVGVAKIEV IRHIEEMLHK DVESNKRIGS YGAEAILAKV PSKEKINVLT HCNTGSLATA
GYGTALGVIR SLYGRDSIDR VFCTETRPYN QGSRLTAFEL VHDGIPATLI TDSMASLVMK
KKDISAVVVG ADRVLGNGDT ANKIGTYQLA ITAKYHKIPF YIAAPTTTIV LDDSKDIVIE
ERSHKEVTEI QGIPIAPSGI NVYNPAFDVT PAELITGIIT EVGVFSPSEM KSKLQTILNS
