ID A0A0A6MYN1_9THEM Unreviewed; 343 AA. AC A0A0A6MYN1; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 04-MAR-2015, entry version 2. 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. OX NCBI_TaxID=1231241 {ECO:0000313|EMBL:KHC90643.1}; RN [1] {ECO:0000313|EMBL:KHC90643.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mc24 {ECO:0000313|EMBL:KHC90643.1}; 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- CC phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- CC P). {ECO:0000256|HAMAP-Rule:MF_01678}. CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate = CC S-methyl-5-thio-D-ribulose 1-phosphate. {ECO:0000256|HAMAP- CC Rule:MF_01678}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose CC 1-phosphate: step 1/6. {ECO:0000256|HAMAP-Rule:MF_01678}. CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits CC family. MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00904; UER00874. 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|HAMAP-Rule:MF_01678}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678}; KW Protein biosynthesis {ECO:0000313|EMBL:KHC90643.1}. FT REGION 48 50 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01678}. FT REGION 244 245 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01678}. FT ACT_SITE 234 234 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01678}. FT BINDING 88 88 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01678}. FT BINDING 193 193 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01678}. FT SITE 154 154 Transition state stabilizer. FT {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 //