ID A0A2J6M8G5_LACSA Unreviewed; 502 AA. AC A0A2J6M8G5; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 24-JAN-2024, entry version 26. DE RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 {ECO:0000256|HAMAP-Rule:MF_03118}; DE Includes: DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_03118}; DE Short=MTRu-1-P dehydratase {ECO:0000256|HAMAP-Rule:MF_03118}; DE EC=4.2.1.109 {ECO:0000256|HAMAP-Rule:MF_03118}; DE Includes: DE RecName: Full=Enolase-phosphatase E1 {ECO:0000256|HAMAP-Rule:MF_03118}; DE EC=3.1.3.77 {ECO:0000256|HAMAP-Rule:MF_03118}; DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000256|HAMAP-Rule:MF_03118}; GN ORFNames=LSAT_7X104120 {ECO:0000313|EMBL:PLY95817.1}; OS Lactuca sativa (Garden lettuce). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae; OC Lactucinae; Lactuca. OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY95817.1}; RN [1] {ECO:0000313|EMBL:PLY95817.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=28401891; DOI=10.1038/ncomms14953; RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L., RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H., RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.; RT "Genome assembly with in vitro proximity ligation data and whole-genome RT triplication in lettuce."; RL Nat. Commun. 8:14953-14953(2017). CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2- CC dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate; CC Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03118}; 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:0000256|HAMAP-Rule:MF_03118}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03118}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03118}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03118}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03118}; 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:0000256|HAMAP-Rule:MF_03118}. 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 3/6. {ECO:0000256|HAMAP-Rule:MF_03118}. 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 4/6. {ECO:0000256|HAMAP-Rule:MF_03118}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like CC hydrolase superfamily. MasA/MtnC family. {ECO:0000256|HAMAP- CC Rule:MF_03118}. CC -!- SIMILARITY: In the N-terminal section; belongs to the aldolase class II CC family. MtnB subfamily. {ECO:0000256|HAMAP-Rule:MF_03118}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PLY95817.1}. 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; NBSK01000935; PLY95817.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2J6M8G5; -. DR STRING; 4236.A0A2J6M8G5; -. DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_7X104120_mrna; cds-PLY95817.1; gene-LSAT_7X104120. DR Gramene; rna-gnl|WGS:NBSK|LSAT_7X104120_mrna; cds-PLY95817.1; gene-LSAT_7X104120. DR OrthoDB; 275419at2759; -. DR UniPathway; UPA00904; UER00875. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central. DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule. DR CDD; cd01629; HAD_EP; 1. DR Gene3D; 1.10.720.60; -; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR HAMAP; MF_03116; Salvage_MtnB_euk; 1. DR HAMAP; MF_03118; Salvage_MtnBC; 1. DR HAMAP; MF_03117; Salvage_MtnC_euk; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR023943; Enolase-ppase_E1. DR InterPro; IPR027511; ENOPH1_eukaryotes. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB. DR InterPro; IPR027505; MtnB_viridiplantae. DR InterPro; IPR027514; Salvage_MtnB_euk. DR NCBIfam; TIGR01691; enolase-ppase; 1. DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1. DR NCBIfam; TIGR03328; salvage_mtnB; 1. DR PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1. DR PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1. DR Pfam; PF00596; Aldolase_II; 1. DR Pfam; PF00702; Hydrolase; 1. DR SFLD; SFLDF00044; enolase-phosphatase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_03118}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03118}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03118}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03118}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03118}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_03118}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_03118}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03118}. FT DOMAIN 26..229 FT /note="Class II aldolase/adducin N-terminal" FT /evidence="ECO:0000259|SMART:SM01007" FT REGION 1..237 FT /note="Methylthioribulose-1-phosphate dehydratase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT REGION 263..502 FT /note="Enolase-phosphatase E1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT ACT_SITE 152 FT /note="Proton donor/acceptor; for methylthioribulose-1- FT phosphate dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 109 FT /ligand="substrate" FT /ligand_label="1" FT /ligand_note="for methylthioribulose-1-phosphate FT dehydratase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 266 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 401..402 FT /ligand="substrate" FT /ligand_label="2" FT /ligand_note="for enolase-phosphatase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 435 FT /ligand="substrate" FT /ligand_label="2" FT /ligand_note="for enolase-phosphatase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" FT BINDING 461 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118" SQ SEQUENCE 502 AA; 55422 MW; 8BF9C840AD7FC0E1 CRC64; MAANGVKSAV TSQAYLEGSQ VKQTKSLISE LCRLFYNLGW VSGTGGSITA KVHDDSVPKS EQLIIMSPSG VQKERMVEED MYVLSSTGDI LFSPSPKPYP HKPPKCSDCA PLFMKAYDKR NAGAVIHSHG MESCLVTMMD PLAKEFRITH MEMIKGIQGH GYYDELVVPI IENTAQEREL TESLAAAIEA YPKTTAVLVR NHGIYVWGDS WISAKTQSEC YHYLFEAAIK LHQLGLDWST PSHGPKPLLC GQSQTTNPSH RCVVLDIEGT TTPISFVTDV LFPYARDNVQ KHLEETYDTD ATQDDIKLLR SQVEDDLKNG VANAVIIPSD EAGKQEVIAA LVANVEGMIK SDRKITSLKQ LQGHIWQTGF EKNELKGVVF DDVPVSLQKW HSSGIKVYIY SSGSRLAQRL LFGYSNHGDL RTYLSGFFDT TVGNKKERKS YVEICESVGV HKPSDVLFVT DVFQEAVAAK AAGLEVIISV RPGNGQLPEN HGFKTVKSFS EI //