ID MTNB_ESOLU Reviewed; 257 AA. AC C1BYA3; DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 15-MAR-2017, entry version 34. DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116}; DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03116}; DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03116}; DE AltName: Full=APAF1-interacting protein homolog {ECO:0000255|HAMAP-Rule:MF_03116}; GN Name=apip {ECO:0000255|HAMAP-Rule:MF_03116}; OS Esox lucius (Northern pike). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; OC Esociformes; Esocidae; Esox. OX NCBI_TaxID=8010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=20433749; DOI=10.1186/1471-2164-11-279; RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., RA Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., RA Davidson W.S., Koop B.F.; RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes RT in evolutionary pressures on a post-tetraploidization genome."; RL BMC Genomics 11:279-279(2010). 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). Functions in the methionine salvage CC pathway. May play a role in apoptosis. {ECO:0000255|HAMAP- CC Rule:MF_03116}. 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_03116}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03116}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_03116}; 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_03116}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}. CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03116}. 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; BT079582; ACO14006.1; -; mRNA. DR ProteinModelPortal; C1BYA3; -. DR SMR; C1BYA3; -. DR UniPathway; UPA00904; UER00875. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB. DR Gene3D; 3.40.225.10; -; 1. DR HAMAP; MF_03116; Salvage_MtnB_euk; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB. DR InterPro; IPR027514; Salvage_MtnB_euk. 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 2: Evidence at transcript level; KW Amino-acid biosynthesis; Apoptosis; Cytoplasm; Lyase; Metal-binding; KW Methionine biosynthesis; Zinc. FT CHAIN 1 257 Methylthioribulose-1-phosphate FT dehydratase. FT /FTId=PRO_0000393773. FT ACT_SITE 149 149 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_03116}. FT METAL 125 125 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03116}. FT METAL 127 127 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03116}. FT METAL 205 205 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03116}. FT BINDING 107 107 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_03116}. SQ SEQUENCE 257 AA; 29383 MW; B98A2114037151DF CRC64; MVSSQEKMAS ISDIIQKDED SGSEKTESQD KEHPRVLIPE LCRLFYKLGW VTGTGGGISL RHGDQIYIAP SGVQKERLQP EDMFVCDVEE RDICVPPAWK NLKKGQCTPL FMNAYTMRAA QAVIHTHSKA AVMATLFYPG KEFRITHQEM IKGIRKCTSG TNYRYDETLV VPIIENTPEE QDLKERMALA MEQYPESCAV LVRRHGVYVW GESWEKAKTM CECYDYLFDI AVKMKQCGLD PSAQPVEENL YYYVQQA //