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 13-SEP-2023, entry version 50. 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; Esociformes; OC 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., Messmer A.M., RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S., RA Koop B.F.; RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in RT evolutionary pressures on a post-tetraploidization genome."; RL BMC Genomics 11:279-279(2010). CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate CC (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). CC Functions in the methionine salvage pathway. May play a role in CC apoptosis. {ECO:0000255|HAMAP-Rule:MF_03116}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3- CC dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109; CC Evidence={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-Rule:MF_03116}; 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 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 subfamily. CC {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 AlphaFoldDB; C1BYA3; -. DR SMR; C1BYA3; -. DR STRING; 8010.XP_010894206.1; -. DR InParanoid; C1BYA3; -. DR UniPathway; UPA00904; UER00875. DR Proteomes; UP000265140; LG25. 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 GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR HAMAP; MF_03116; Salvage_MtnB_euk; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB. DR InterPro; IPR027514; Salvage_MtnB_euk. DR NCBIfam; TIGR03328; salvage_mtnB; 1. DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1. DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. PE 2: Evidence at transcript level; KW Amino-acid biosynthesis; Apoptosis; Cytoplasm; Lyase; Metal-binding; KW Methionine biosynthesis; Reference proteome; Zinc. FT CHAIN 1..257 FT /note="Methylthioribulose-1-phosphate dehydratase" FT /id="PRO_0000393773" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..33 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 149 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116" FT BINDING 205 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-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 //