ID A0A0A6MYN1_9THEM Unreviewed; 343 AA. AC A0A0A6MYN1; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-OCT-2022, entry version 21. DE RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678}; DE Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678}; DE Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678}; DE EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678}; DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678}; GN Name=mtnA {ECO:0000256|HAMAP-Rule:MF_01678}; GN ORFNames=Mc24_06928 {ECO:0000313|EMBL:KHC90643.1}; OS Thermotoga sp. Mc24. OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga; OC unclassified Thermotoga. OX NCBI_TaxID=1231241 {ECO:0000313|EMBL:KHC90643.1, ECO:0000313|Proteomes:UP000030509}; RN [1] {ECO:0000313|EMBL:KHC90643.1, ECO:0000313|Proteomes:UP000030509} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mc24 {ECO:0000313|EMBL:KHC90643.1, RC ECO:0000313|Proteomes:UP000030509}; RA Nesbo C.L., Dlutek M., Marquis P., Bonch-Osmolovskaya E., Ilya K., RA Doolittle F.W.; RT "Genomes of Thermotoga isolates."; RL Submitted (SEP-2012) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01678}. CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family. CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KHC90643.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JSFH01000011; KHC90643.1; -; Genomic_DNA. DR RefSeq; WP_038053817.1; NZ_JSFH01000011.1. DR STRING; 1231241.Mc24_06928; -. DR EnsemblBacteria; KHC90643; KHC90643; Mc24_06928. DR PATRIC; fig|1231241.4.peg.1393; -. DR eggNOG; COG0182; Bacteria. DR UniPathway; UPA00904; UER00874. DR Proteomes; UP000030509; Unassembled WGS sequence. DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. 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 {ECO:0000256|HAMAP-Rule:MF_01678}; KW Initiation factor {ECO:0000313|EMBL:KHC90643.1}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678}; KW Protein biosynthesis {ECO:0000313|EMBL:KHC90643.1}. FT ACT_SITE 234 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" FT BINDING 48..50 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" FT BINDING 244..245 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" FT SITE 154 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678" SQ SEQUENCE 343 AA; 38067 MW; A1445F099BD8C60D CRC64; MKLRTKTMEW SGDSLRLLDQ RKLPFVEEYV ECKTHEEVAY AIKEMIVRGA PAIGVTAAFG YVLGLKEYKT GSLMDWMRQV KETLARTRPT AVNLFWALNR MEKVFSENFD RENLFEILEN EALKMAYEDI EVNKAIGRNG AQLIKDGSTI LTHCNAGALA TVDYGTALGV IRAAVEAGKR IKVFADETRP YLQGARLTAW ELMKDGIEVY VITDNMAGWL MKKGLIDAVV VGADRIALNG DTANKIGTYS LAVLAKRNNI PFYVAAPVST IDPTIKSGEE IPIEERRPEE VTHCGGNRIT PEGIKVLNPA FDVTENSLIT AIITEKGVIK PPFEENIKKI LGV //