ID A0A2J6M8G5_LACSA Unreviewed; 502 AA. AC A0A2J6M8G5; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 10-APR-2019, entry version 9. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Asterales; Asteraceae; OC Cichorioideae; Cichorieae; Lactucinae; Lactuca. OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY95817.1, ECO:0000313|Proteomes:UP000235145}; RN [1] {ECO:0000313|EMBL:PLY95817.1, ECO:0000313|Proteomes:UP000235145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Salinas {ECO:0000313|Proteomes:UP000235145}; RX PubMed=28401891; DOI=10.1038/ncomms14953; RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., RA Xia L., Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., RA Xu H., Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.; RT "Genome assembly with in vitro proximity ligation data and whole- RT genome 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 ECO:0000256|SAAS:SAAS01117276}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methylsulfanyl-D-ribulose 1-phosphate = 5- CC methylsulfanyl-2,3-dioxopentyl phosphate + H2O; CC Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377, ChEBI:CHEBI:58548, CC ChEBI:CHEBI:58828; EC=4.2.1.109; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03118, ECO:0000256|SAAS:SAAS01115951}; 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 4/6. {ECO:0000256|HAMAP-Rule:MF_03118, CC ECO:0000256|SAAS:SAAS00338558}. 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 CC class II family. MtnB subfamily. {ECO:0000256|HAMAP- CC Rule:MF_03118}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniGene; Lsa.6228; -. DR UniPathway; UPA00904; UER00877. DR Proteomes; UP000235145; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 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; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway. DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule. DR CDD; cd01629; HAD_EP; 1. DR Gene3D; 3.40.225.10; -; 1. DR Gene3D; 3.40.50.1000; -; 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 PANTHER; PTHR10640; PTHR10640; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01691; enolase-ppase; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR03328; salvage_mtnB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00035241}; KW Complete proteome {ECO:0000313|Proteomes:UP000235145}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00003607}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00003633}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00003622}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00035247}; KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03118, KW ECO:0000256|SAAS:SAAS00003642}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03118}; KW Reference proteome {ECO:0000313|Proteomes:UP000235145}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_03118, ECO:0000256|SAAS:SAAS00003660}. FT DOMAIN 26 229 Aldolase_II. {ECO:0000259|SMART:SM01007}. FT REGION 1 237 Methylthioribulose-1-phosphate FT dehydratase. {ECO:0000256|HAMAP-Rule: FT MF_03118}. FT REGION 263 502 Enolase-phosphatase E1. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT REGION 401 402 Substrate binding; for enolase- FT phosphatase activity. {ECO:0000256|HAMAP- FT Rule:MF_03118}. FT ACT_SITE 152 152 Proton donor/acceptor; for FT methylthioribulose-1-phosphate FT dehydratase activity. {ECO:0000256|HAMAP- FT Rule:MF_03118}. FT METAL 127 127 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT METAL 129 129 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT METAL 202 202 Zinc; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT METAL 266 266 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_03118}. FT METAL 268 268 Magnesium; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT METAL 461 461 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_03118}. FT BINDING 109 109 Substrate; for methylthioribulose-1- FT phosphate dehydratase activity. FT {ECO:0000256|HAMAP-Rule:MF_03118}. FT BINDING 435 435 Substrate; for enolase-phosphatase FT activity. {ECO:0000256|HAMAP-Rule: FT 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 //