ERR2_YEAST
ID ERR2_YEAST Reviewed; 437 AA.
AC P0CX11; D6W385; Q12007; Q7LGJ4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Enolase-related protein 2;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=ERR2; OrderedLocusNames=YPL281C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; Z73637; CAA98018.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11157.1; -; Genomic_DNA.
DR PIR; S67305; S67305.
DR RefSeq; NP_015038.1; NM_001183813.1.
DR RefSeq; NP_015042.1; NM_001184095.1.
DR AlphaFoldDB; P0CX11; -.
DR SMR; P0CX11; -.
DR BioGRID; 34773; 122.
DR BioGRID; 35934; 9.
DR PRIDE; P0CX11; -.
DR EnsemblFungi; YOR393W_mRNA; YOR393W; YOR393W.
DR EnsemblFungi; YPL281C_mRNA; YPL281C; YPL281C.
DR GeneID; 854575; -.
DR GeneID; 855848; -.
DR KEGG; sce:YOR393W; -.
DR KEGG; sce:YPL281C; -.
DR SGD; S000006202; ERR2.
DR VEuPathDB; FungiDB:YOR393W; -.
DR VEuPathDB; FungiDB:YPL281C; -.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P0CX11; -.
DR BioCyc; YEAST:YPL281C-MON; -.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P0CX11; -.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P0CX11; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0CX11; protein.
DR ExpressionAtlas; P0CX11; baseline and differential.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:SGD.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..437
FT /note="Enolase-related protein 2"
FT /id="PRO_0000409749"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 47328 MW; FAF09C00BE0E711C CRC64;
MSITKVHART VYDSRGNPTV EVEITTENGL FRAIVPSGAS TGIHEAVELR DGNKSEWMGK
GVTKAVSNVN SIIGPALIKS ELCVTNQKGI DELMISLDGT SNKSRLGANA ILGVSLCVAR
AAAAQKGITL YKYIAELADA RQDPFVIPVP FFNVLNGGAH AGGSLAMQEF KIAPVGAQSF
AEAMRMGSEV YHHLKILAKE QYGPSAGNVG DEGGVAPDID TAEDALDMIV EAINICGYEG
RVKVGIDSAP SVFYKDGKYD LNFKEPNSDP SHWLSPAQLA EYYHSLLKKY PIISLEDPYA
EDDWSSWSAF LKTVNVQIIA DDLTCTNKTR IARAIEEKCA NTLLLKLNQI GTLTESIEAA
NQAFDAGWGV MISHRSGETE DPFIADLVVG LRCGQIKSGA LSRSERLAKY NELLRIEEEL
GDDCIYAGHR FHDGNKL
