MTNA_CAEEL
ID MTNA_CAEEL Reviewed; 366 AA.
AC Q93169;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=C01G10.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z81030; CAB02711.1; -; Genomic_DNA.
DR PIR; T18820; T18820.
DR RefSeq; NP_506714.1; NM_074313.6.
DR AlphaFoldDB; Q93169; -.
DR SMR; Q93169; -.
DR BioGRID; 45011; 1.
DR STRING; 6239.C01G10.9; -.
DR EPD; Q93169; -.
DR PaxDb; Q93169; -.
DR PeptideAtlas; Q93169; -.
DR EnsemblMetazoa; C01G10.9.1; C01G10.9.1; WBGene00007236.
DR GeneID; 180016; -.
DR KEGG; cel:CELE_C01G10.9; -.
DR UCSC; C01G10.9; c. elegans.
DR CTD; 180016; -.
DR WormBase; C01G10.9; CE07818; WBGene00007236; -.
DR eggNOG; KOG1468; Eukaryota.
DR GeneTree; ENSGT00390000013732; -.
DR HOGENOM; CLU_016218_1_2_1; -.
DR InParanoid; Q93169; -.
DR OMA; GDVIMTH; -.
DR OrthoDB; 1410886at2759; -.
DR PhylomeDB; Q93169; -.
DR Reactome; R-CEL-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00874.
DR PRO; PR:Q93169; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007236; Expressed in embryo and 4 other tissues.
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..366
FT /note="Methylthioribose-1-phosphate isomerase"
FT /id="PRO_0000156111"
FT ACT_SITE 260
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03119"
SQ SEQUENCE 366 AA; 40861 MW; F18E6FBD3BA8E39C CRC64;
MTSKINKIVN GPIPDSFLFD ESKRLDSLKF DGTNLEVLDQ LLLPHEFKYI PVEGVSDAFA
VIKSMQVRGA PLIAVVGSLG LLLEIQKASE LDSESIIQKI NFLISSRPTA VDLRNSLNGL
KPILESQDYS DVVKLEKCRS YLLNVYTDEK LQNRILVWNA YQELLSAFPD KEKLTVMTIC
NTGSLATISW GTALGVIRAL HSENRLKLVY VLETRPYNQG IRLTSIELLH GEVPFKLITD
SMAAWAMKNH QVDCVLTGAD NVARNGDTAN KIGTYMLAVL CKHHNINFYP VVPFTTINKN
IATGEEIKIE ERPSAEMLRV NGVLIGNSEC PVWNPAFDVT PAHLITKILT DFGNWPPEML
EQQIPK
