ID MTNB_BACAC Reviewed; 212 AA. AC C3LIA8; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 02-NOV-2016, entry version 49. DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01677}; DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_01677}; DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_01677}; GN Name=mtnB {ECO:0000255|HAMAP-Rule:MF_01677}; GN OrderedLocusNames=BAMEG_4298; OS Bacillus anthracis (strain CDC 684 / NRRL 3495). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=568206; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 684 / NRRL 3495; RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., RA Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus anthracis str. CDC 684."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1- CC phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1- CC phosphate (DK-MTP-1-P). {ECO:0000255|HAMAP-Rule:MF_01677}. CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5- CC (methylthio)-2,3-dioxopentyl phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01677}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01677}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01677}; 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 2/6. {ECO:0000255|HAMAP-Rule:MF_01677}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01677}. CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01677}. 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; CP001215; ACP12897.1; -; Genomic_DNA. DR RefSeq; WP_000811328.1; NC_012581.1. DR ProteinModelPortal; C3LIA8; -. DR EnsemblBacteria; ACP12897; ACP12897; BAMEG_4298. DR KEGG; bah:BAMEG_4298; -. DR PATRIC; 18798425; VBIBacAnt127120_4544. DR HOGENOM; HOG000086153; -. DR KO; K08964; -. DR OMA; IRGHGLY; -. DR UniPathway; UPA00904; UER00875. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.225.10; -; 1. DR HAMAP; MF_01677; Salvage_MtnB; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB. DR PANTHER; PTHR10640; PTHR10640; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. DR TIGRFAMs; TIGR03328; salvage_mtnB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Lyase; Metal-binding; KW Methionine biosynthesis; Zinc. FT CHAIN 1 212 Methylthioribulose-1-phosphate FT dehydratase. FT /FTId=PRO_1000187340. FT METAL 97 97 Zinc. {ECO:0000255|HAMAP-Rule:MF_01677}. FT METAL 99 99 Zinc. {ECO:0000255|HAMAP-Rule:MF_01677}. SQ SEQUENCE 212 AA; 23911 MW; 0782B4DA78BD7021 CRC64; MKQLFRQWYD LSEIKKELTT RNWFPATSGN ISIKVSHEPL TFLITASGKD KTKTTPDDFL LVDHLGVPVL ETELRPSAET ILHTHIYNNT NAGCVLHVHT TDNNVITNLY SDAVTLQNQE IIKALDIWEE GATIHIPIIE NHAHIPTLGE NFRKHIQGDS GAVLIRNHGI TVWGRDSFDA KKRLEAYEFL FQFHIKLLSI QGGVSNGANS YS //