AC   MF_03117;
DC   Protein; auto
TR   HAMAP; MF_03117; -; 1; level=0
XX
Names: Salvage_MtnC_euk
XX
ID   ENOPH
case <OC:Vertebrata>
DE   RecName: Full=Enolase-phosphatase E1;
DE            EC=3.1.3.77;
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE   AltName: Full=MASA homolog;
else case <OC:Saccharomyces>
DE   RecName: Full=Enolase-phosphatase E1;
DE            EC=3.1.3.77;
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE   AltName: Full=Unknown transcript 4 protein;
else
DE   RecName: Full=Enolase-phosphatase E1;
DE            EC=3.1.3.77;
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
end case
case <OC:Vertebrata>
GN   Name=ENOPH1; Synonyms=MASA;
else case <OC:Fungi>
GN   Name=UTR4;
end case
XX
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   -!- 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;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
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.
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.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family.
XX
DR   Pfam; PF00702; Hydrolase; 1; trigger=no
DR   PRINTS; PR00413; HADHALOGNASE; 1; trigger=no
DR   NCBIfam; TIGR01691; enolase-ppase; 1; trigger=no
DR   NCBIfam; TIGR01549; HAD-SF-IA-v1; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Cytoplasm
KW   Hydrolase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
KW   Methionine biosynthesis
KW   Nucleus
XX
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity
GO   GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity
GO   GO:0019284; P:L-methionine salvage from S-adenosylmethionine
XX
FT   From: ENOPH_HUMAN (Q9UHY7)
FT   BINDING         153..154
FT                   /ligand="substrate"
FT   Condition: S-S
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         187
FT                   /ligand="substrate"
FT   Condition: K
XX
Size: 215-1107;
Related: MF_03118!;
Template: Q9UHY7; P32626;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.12 2023/06/01
//