ID   ENOPH_YEAST             Reviewed;         227 AA.
AC   P32626; D3DLL1;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   27-MAR-2024, entry version 170.
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};
DE   AltName: Full=Unknown transcript 4 protein {ECO:0000255|HAMAP-Rule:MF_03117};
GN   Name=UTR4 {ECO:0000255|HAMAP-Rule:MF_03117};
GN   OrderedLocusNames=YEL038W; ORFNames=SYGP-ORF20;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=B-6441;
RX   PubMed=8411151; DOI=10.1006/jmbi.1993.1518;
RA   Melnick L., Sherman F.;
RT   "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of
RT   Saccharomyces cerevisiae share a common ancestry.";
RL   J. Mol. Biol. 233:372-388(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of UTR4 protein (unknown transcript 4 protein) (YEL038w)
RT   from Saccharomyces cerevisiae at 2.28 A resolution.";
RL   Submitted (MAR-2006) to the PDB data bank.
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       Note=Binds 1 Mg(2+) ion per subunit.;
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       ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03117,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 2850 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MasA/MtnC
CC       family. {ECO:0000255|HAMAP-Rule:MF_03117}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA34939.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA34939.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB28443.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAB28443.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB65004.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAD13973.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAD13973.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L22173; AAA34939.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; S65964; AAD13973.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; S66121; AAB28443.1; ALT_SEQ; mRNA.
DR   EMBL; U18779; AAB65004.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006939; DAA07615.1; -; Genomic_DNA.
DR   PIR; S30843; S30843.
DR   RefSeq; NP_010876.2; NM_001178853.1.
DR   PDB; 2G80; X-ray; 2.28 A; A/B/C/D=1-227.
DR   PDBsum; 2G80; -.
DR   AlphaFoldDB; P32626; -.
DR   SMR; P32626; -.
DR   BioGRID; 36691; 33.
DR   DIP; DIP-5487N; -.
DR   STRING; 4932.YEL038W; -.
DR   MaxQB; P32626; -.
DR   PaxDb; 4932-YEL038W; -.
DR   PeptideAtlas; P32626; -.
DR   EnsemblFungi; YEL038W_mRNA; YEL038W; YEL038W.
DR   GeneID; 856673; -.
DR   KEGG; sce:YEL038W; -.
DR   AGR; SGD:S000000764; -.
DR   SGD; S000000764; UTR4.
DR   VEuPathDB; FungiDB:YEL038W; -.
DR   eggNOG; KOG2630; Eukaryota.
DR   GeneTree; ENSGT00440000039914; -.
DR   HOGENOM; CLU_023273_1_1_1; -.
DR   InParanoid; P32626; -.
DR   OMA; LQGMVWE; -.
DR   OrthoDB; 275419at2759; -.
DR   BioCyc; YEAST:MONOMER3O-175; -.
DR   Reactome; R-SCE-1237112; Methionine salvage pathway.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   BioGRID-ORCS; 856673; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P32626; -.
DR   PRO; PR:P32626; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P32626; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
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; ISS:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IMP:SGD.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 1.10.720.60; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR023214; HAD_sf.
DR   NCBIfam; TIGR01691; enolase-ppase; 1.
DR   PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1.
DR   PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SFLD; SFLDG01133; C1.5.4:_Enolase-phosphatase_Li; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Cytoplasm; Hydrolase; Magnesium;
KW   Metal-binding; Methionine biosynthesis; Nucleus; Reference proteome.
FT   CHAIN           1..227
FT                   /note="Enolase-phosphatase E1"
FT                   /id="PRO_0000065746"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT                   ECO:0000269|Ref.7"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT                   ECO:0000269|Ref.7"
FT   BINDING         118..119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03117,
FT                   ECO:0000269|Ref.7"
FT   CONFLICT        56..57
FT                   /note="ID -> MH (in Ref. 1; AAA34939/AAD13973/AAB28443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="S -> T (in Ref. 1; AAA34939/AAD13973/AAB28443)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           26..39
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           46..52
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           77..92
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           102..110
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   STRAND          114..117
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           122..130
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           164..174
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:2G80"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:2G80"
SQ   SEQUENCE   227 AA;  25187 MW;  147305E847F765DB CRC64;
     MGDNYSTYLL DIEGTVCPIS FVKETLFPYF TNKVPQLVQQ DTRDSPVSNI LSQFHIDNKE
     QLQAHILELV AKDVKDPILK QLQGYVWAHG YESGQIKAPV YADAIDFIKR KKRVFIYSSG
     SVKAQKLLFG YVQDPNAPAH DSLDLNSYID GYFDINTSGK KTETQSYANI LRDIGAKASE
     VLFLSDNPLE LDAAAGVGIA TGLASRPGNA PVPDGQKYQV YKNFETL
//