ENOPH_DROWI
ID ENOPH_DROWI Reviewed; 247 AA.
AC B4NI64;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03117};
DE EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03117};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03117};
GN ORFNames=GK14286;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of 2,3-
CC diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-
CC MTPenyl-1-P), which is then dephosphorylated to form the acireductone
CC 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
CC {ECO:0000255|HAMAP-Rule:MF_03117}.
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:0000255|HAMAP-Rule:MF_03117};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03117};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03117};
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:0000255|HAMAP-Rule:MF_03117}.
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:0000255|HAMAP-Rule:MF_03117}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03117}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03117}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC family. {ECO:0000255|HAMAP-Rule:MF_03117}.
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DR EMBL; CH964272; EDW84756.1; -; Genomic_DNA.
DR RefSeq; XP_002073770.1; XM_002073734.1.
DR AlphaFoldDB; B4NI64; -.
DR SMR; B4NI64; -.
DR STRING; 7260.FBpp0243429; -.
DR EnsemblMetazoa; FBtr0244937; FBpp0243429; FBgn0216292.
DR GeneID; 6650709; -.
DR KEGG; dwi:6650709; -.
DR eggNOG; KOG2630; Eukaryota.
DR HOGENOM; CLU_023273_0_0_1; -.
DR InParanoid; B4NI64; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1475361at2759; -.
DR PhylomeDB; B4NI64; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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; 3.40.50.1000; -; 1.
DR HAMAP; MF_01681; Salvage_MtnC; 1.
DR HAMAP; MF_03117; Salvage_MtnC_euk; 1.
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; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDF00044; enolase-phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Nucleus; Reference proteome.
FT CHAIN 1..247
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000393986"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 141..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ SEQUENCE 247 AA; 27529 MW; 37F4070BD49596AA CRC64;
MLGNEIKVIL LDIEGTTTSI GFVHHILFPY AKQNVEEYLK KEWDSDEIKQ IVQDLQQVPS
FEVYKATLVD SSASSITVEL ITGFVRYLID KDLKVTPLKT LQGLIWANGY ESGELKGHVY
DDVKEAFEHW NNSGLKLAIY SSGSVAAQKL IFGYSTSGNL LPYLSAHFDT HVGHKQEKDS
YINIAKSLET NPEHILFLTD IPGEADAARA AGLQAIILQR FGNAPLTDDE KSLNKIINDF
SVLKVDK
