ENOPH_YEAST
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 03-AUG-2022, entry version 164.
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}; OrderedLocusNames=YEL038W;
GN 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; 32.
DR DIP; DIP-5487N; -.
DR STRING; 4932.YEL038W; -.
DR MaxQB; P32626; -.
DR PaxDb; P32626; -.
DR PRIDE; P32626; -.
DR EnsemblFungi; YEL038W_mRNA; YEL038W; YEL038W.
DR GeneID; 856673; -.
DR KEGG; sce:YEL038W; -.
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; QLKGHVY; -.
DR BioCyc; YEAST:MON3O-175; -.
DR Reactome; R-SCE-1237112; Methionine salvage pathway.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
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; 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; IPR023214; HAD_sf.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 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
