MTNA1_PSELT
ID MTNA1_PSELT Reviewed; 346 AA.
AC A8F3A3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Methylthioribose-1-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=M1Pi 1 {ECO:0000255|HAMAP-Rule:MF_01678};
DE Short=MTR-1-P isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01678};
DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678};
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase 1 {ECO:0000255|HAMAP-Rule:MF_01678};
GN Name=mtnA1 {ECO:0000255|HAMAP-Rule:MF_01678}; OrderedLocusNames=Tlet_0065;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) 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_01678}.
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_01678};
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_01678}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000305}.
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DR EMBL; CP000812; ABV32637.1; -; Genomic_DNA.
DR RefSeq; WP_012002118.1; NC_009828.1.
DR AlphaFoldDB; A8F3A3; -.
DR SMR; A8F3A3; -.
DR STRING; 416591.Tlet_0065; -.
DR EnsemblBacteria; ABV32637; ABV32637; Tlet_0065.
DR KEGG; tle:Tlet_0065; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_0; -.
DR OMA; RLWVDET; -.
DR OrthoDB; 1290468at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000002016; Chromosome.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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; Isomerase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..346
FT /note="Methylthioribose-1-phosphate isomerase 1"
FT /id="PRO_0000357260"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 48..50
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT BINDING 247..248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01678"
SQ SEQUENCE 346 AA; 37585 MW; 61246FD79BFE7ADE CRC64;
MNFKTLTMQW TGNSLILVDQ RKLPHVVNYV ECKSYAEVAR AIKDMVVRGA PAIGATAAFG
YVLGAKEAAT LKNQNFIDVM KNVYDVLAST RPTAVNLFWA LNRMEKCVDL SKAVDEILED
LEKEAIKIAE EDIRINKTIG THGQTLLKDG CAVLTHCNAG ALATVDYGTA LGVIRAAVES
GKKIKVYVDE TRPYLQGARL TAWELLEIGV ETILITDNMA GWVMKQGKID AVIVGADRIA
ANGDVANKIG TYSVAVLSNQ HGIPFYVAAP TSTIDIKIKN GSEIPIEERS HDEVTHVHGV
KVAPDGVAVY NPAFDVTEHQ LITAIITEKG ILRPPYKENI AKLFGG