ENOPH_CAEEL
ID ENOPH_CAEEL Reviewed; 248 AA.
AC Q21012;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 140.
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=F58H1.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z75954; CAB00106.3; -; Genomic_DNA.
DR RefSeq; NP_001041138.2; NM_001047673.2.
DR AlphaFoldDB; Q21012; -.
DR SMR; Q21012; -.
DR BioGRID; 44658; 2.
DR STRING; 6239.F58H1.3a; -.
DR EPD; Q21012; -.
DR PaxDb; Q21012; -.
DR PeptideAtlas; Q21012; -.
DR EnsemblMetazoa; F58H1.3a.1; F58H1.3a.1; WBGene00010286.
DR GeneID; 179634; -.
DR KEGG; cel:CELE_F58H1.3; -.
DR UCSC; F58H1.3a; c. elegans.
DR CTD; 179634; -.
DR WormBase; F58H1.3a; CE43080; WBGene00010286; -.
DR eggNOG; KOG2630; Eukaryota.
DR GeneTree; ENSGT00440000039914; -.
DR HOGENOM; CLU_023273_0_0_1; -.
DR InParanoid; Q21012; -.
DR OMA; QLKGHVY; -.
DR OrthoDB; 1475361at2759; -.
DR PhylomeDB; Q21012; -.
DR Reactome; R-CEL-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR PRO; PR:Q21012; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010286; Expressed in embryo and 3 other tissues.
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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium 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; 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; IPR023214; HAD_sf.
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..248
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000393989"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 145..146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ SEQUENCE 248 AA; 27955 MW; 2ED20FBDC2EFC510 CRC64;
MTTTTIQFNA LLLDIEGTIT SISFVKDELF PYAFENVGNY LEEHYDNPAT QIIVEDLRHI
ADQQAENDVA VVRIREPRKE CIEDVTKNVR HWIKRDKKLT PMKALQGLIW EEAYQRGDVK
GHVYPDVLPV LKIVENRKIP IYIYSSGSVH AQKLLFANSI EGDMTKILYG YFDTNIGLKG
ESNSYTKISE RIKIPPSEIL FLTDVEAEAA AAKKAGLQTK LVVRPGNAGL TQEAINAYGT
IESLEEIL
