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 11-JUL-2012, entry version 25. DE RecName: Full=Methylthioribulose-1-phosphate dehydratase; DE Short=MTRu-1-P dehydratase; DE EC=4.2.1.109; GN Name=mtnB; OrderedLocusNames=BAMEG_4298; OS Bacillus anthracis (strain CDC 684 / NRRL 3495). OC Bacteria; Firmicutes; 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) (By similarity). CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5- CC (methylthio)-2,3-dioxopentyl phosphate + H(2)O. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). 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. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB CC subfamily. 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; YP_002816825.1; NC_012581.1. DR ProteinModelPortal; C3LIA8; -. DR STRING; C3LIA8; -. DR EnsemblBacteria; EBBACT00000120541; EBBACP00000119742; EBBACG00000120178. DR GeneID; 7783870; -. DR GenomeReviews; CP001215_GR; BAMEG_4298. DR KEGG; bah:BAMEG_4298; -. DR PATRIC; 18798425; VBIBacAnt127120_4544. DR eggNOG; COG0235; -. DR HOGENOM; HOG000086153; -. DR KO; K08964; -. DR OMA; ELCRLFY; -. DR ProtClustDB; PRK06754; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:EC. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway. DR Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 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 PANTHER; PTHR10640:SF6; PTHR10640:SF6; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; Aldolase_II_N; 1. DR TIGRFAMs; TIGR03328; Salvage_mtnB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; 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 (By similarity). FT METAL 99 99 Zinc (By similarity). 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 //