ENOPH_YARLI
ID ENOPH_YARLI Reviewed; 233 AA.
AC Q6C8V1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Name=UTR4 {ECO:0000255|HAMAP-Rule:MF_03117};
GN OrderedLocusNames=YALI0D16797g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382130; CAG81102.1; -; Genomic_DNA.
DR RefSeq; XP_502911.1; XM_502911.1.
DR AlphaFoldDB; Q6C8V1; -.
DR SMR; Q6C8V1; -.
DR STRING; 4952.CAG81102; -.
DR EnsemblFungi; CAG81102; CAG81102; YALI0_D16797g.
DR GeneID; 2910210; -.
DR KEGG; yli:YALI0D16797g; -.
DR VEuPathDB; FungiDB:YALI0_D16797g; -.
DR HOGENOM; CLU_023273_1_1_1; -.
DR InParanoid; Q6C8V1; -.
DR OMA; QLKGHVY; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000001300; Chromosome D.
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_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 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..233
FT /note="Enolase-phosphatase E1"
FT /id="PRO_0000394016"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 128..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
SQ SEQUENCE 233 AA; 25744 MW; 0B9E033DC45D6A37 CRC64;
MATLLDIEGT VCSISFVHDI LFPYALEKLP QLLKNEQFPI KPGGNQTSDL TPYLESFPEE
YKQSAQALED HVIDLTEKNV KAPYLKALQG YIWKSGYQSG EIKAPLYPDA VDYMKRVVDG
GNKVFIYSSG SVPAQKLLFG YSSAGDLTPL ISDYFDTVNA GPKMEAASYT TILKAIGFEA
DRVLFLSDNV REIEAAKKAG LRAYVAERPG NAKLTPQEKE DNVIKTSFEG IEI
