ERR1_YEAST
ID ERR1_YEAST Reviewed; 437 AA.
AC P0CX10; 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 72.
DE RecName: Full=Enolase-related protein 1;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=ERR1; OrderedLocusNames=YOR393W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-437.
RC STRAIN=ATCC 90839 / S288c / YP1;
RX PubMed=7785338; DOI=10.1002/yea.320110410;
RA Pryde F.E., Huckle T.C., Louis E.J.;
RT "Sequence analysis of the right end of chromosome XV in Saccharomyces
RT cerevisiae: an insight into the structural and functional significance of
RT sub-telomeric repeat sequences.";
RL Yeast 11:371-382(1995).
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; Z75301; CAA99725.1; -; Genomic_DNA.
DR EMBL; Z75302; CAA99728.1; -; Genomic_DNA.
DR EMBL; U23472; AAC48992.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11151.1; -; Genomic_DNA.
DR PIR; S67305; S67305.
DR RefSeq; NP_015038.1; NM_001183813.1.
DR RefSeq; NP_015042.1; NM_001184095.1.
DR AlphaFoldDB; P0CX10; -.
DR SMR; P0CX10; -.
DR BioGRID; 34773; 122.
DR BioGRID; 35934; 9.
DR IntAct; P0CX10; 7.
DR MINT; P0CX10; -.
DR STRING; 4932.YOR393W; -.
DR PaxDb; P0CX10; -.
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; S000005920; ERR1.
DR VEuPathDB; FungiDB:YOR393W; -.
DR VEuPathDB; FungiDB:YPL281C; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P0CX10; -.
DR OMA; KHADNGI; -.
DR BioCyc; YEAST:YOR393W-MON; -.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:P0CX10; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P0CX10; protein.
DR ExpressionAtlas; P0CX10; 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; ISA: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 1"
FT /id="PRO_0000134064"
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"
FT CONFLICT 231
FT /note="E -> K (in Ref. 3; AAC48992)"
FT /evidence="ECO:0000305"
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
