ENO_DROME
ID ENO_DROME Reviewed; 500 AA.
AC P15007; A4UZY9; A5XD39; A5XD43; B9EQS7; C0PV73; Q8IPX8; Q8MT10; Q9VQ38;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
GN Name=Eno; ORFNames=CG17654;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RC STRAIN=Canton-S;
RX PubMed=2106662; DOI=10.1093/nar/18.1.191;
RA Bishop J.G. III, Corces V.G.;
RT "The nucleotide sequence of a Drosophila melanogaster enolase gene.";
RL Nucleic Acids Res. 18:191-191(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Sandler J., Wan K.H., Yu C., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-500, AND VARIANT ALA-380.
RC STRAIN=DPF96_10, DPF96_26, DPF96_5.1, DPF96_8.3, HFL97_23, HFL97_3,
RC HFL97_5, HFL97_68, MA96_24.2, MA96_26.4, MA96_3.5, MA96_4.4, MA96_40.1,
RC MA96_42.4, MA96_49.2, SC96_47, VT97_1, Zim(h)_26, Zim(h)_28, Zim(h)_36,
RC Zim(h)_38, Zim(h)_44, Zim(s)_28, and Zim(s)_49;
RX PubMed=17379620; DOI=10.1093/molbev/msm057;
RA Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P.,
RA Eanes W.;
RT "Adaptive evolution of metabolic pathways in Drosophila.";
RL Mol. Biol. Evol. 24:1347-1354(2007).
RN [7]
RP PROTEIN SEQUENCE OF 100-116.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
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;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=C, D, E;
CC IsoId=P15007-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P15007-2; Sequence=VSP_014147;
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X17034; CAA34895.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51344.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10455.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10456.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10457.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10458.1; -; Genomic_DNA.
DR EMBL; AY118449; AAM48478.1; -; mRNA.
DR EMBL; BT014924; AAT47775.1; -; mRNA.
DR EMBL; BT058002; ACM16712.1; -; mRNA.
DR EMBL; BT072929; ACN86077.1; -; mRNA.
DR EMBL; DQ864190; ABH06825.1; -; Genomic_DNA.
DR EMBL; DQ864191; ABH06826.1; -; Genomic_DNA.
DR EMBL; DQ864192; ABH06827.1; -; Genomic_DNA.
DR EMBL; DQ864193; ABH06828.1; -; Genomic_DNA.
DR EMBL; DQ864194; ABH06829.1; -; Genomic_DNA.
DR EMBL; DQ864195; ABH06830.1; -; Genomic_DNA.
DR EMBL; DQ864196; ABH06831.1; -; Genomic_DNA.
DR EMBL; DQ864197; ABH06832.1; -; Genomic_DNA.
DR EMBL; DQ864198; ABH06833.1; -; Genomic_DNA.
DR EMBL; DQ864199; ABH06834.1; -; Genomic_DNA.
DR EMBL; DQ864200; ABH06835.1; -; Genomic_DNA.
DR EMBL; DQ864201; ABH06836.1; -; Genomic_DNA.
DR EMBL; DQ864202; ABH06837.1; -; Genomic_DNA.
DR EMBL; DQ864203; ABH06838.1; -; Genomic_DNA.
DR EMBL; DQ864204; ABH06839.1; -; Genomic_DNA.
DR EMBL; DQ864205; ABH06840.1; -; Genomic_DNA.
DR EMBL; DQ864206; ABH06841.1; -; Genomic_DNA.
DR EMBL; DQ864207; ABH06842.1; -; Genomic_DNA.
DR EMBL; DQ864208; ABH06843.1; -; Genomic_DNA.
DR EMBL; DQ864209; ABH06844.1; -; Genomic_DNA.
DR EMBL; DQ864210; ABH06845.1; -; Genomic_DNA.
DR EMBL; DQ864211; ABH06846.1; -; Genomic_DNA.
DR EMBL; DQ864212; ABH06847.1; -; Genomic_DNA.
DR EMBL; DQ864213; ABH06848.1; -; Genomic_DNA.
DR PIR; S07586; S07586.
DR RefSeq; NP_001162853.1; NM_001169382.2. [P15007-2]
DR RefSeq; NP_477421.1; NM_058073.5. [P15007-2]
DR RefSeq; NP_722721.1; NM_164431.3. [P15007-1]
DR RefSeq; NP_722722.1; NM_164432.3. [P15007-1]
DR RefSeq; NP_722723.1; NM_164433.3. [P15007-1]
DR RefSeq; NP_722724.1; NM_164434.3. [P15007-1]
DR PDB; 5WRO; X-ray; 2.02 A; A=69-500.
DR PDBsum; 5WRO; -.
DR AlphaFoldDB; P15007; -.
DR SMR; P15007; -.
DR BioGRID; 59591; 93.
DR IntAct; P15007; 5.
DR STRING; 7227.FBpp0077572; -.
DR PaxDb; P15007; -.
DR PRIDE; P15007; -.
DR DNASU; 33351; -.
DR EnsemblMetazoa; FBtr0077905; FBpp0077571; FBgn0000579. [P15007-1]
DR EnsemblMetazoa; FBtr0077906; FBpp0077572; FBgn0000579. [P15007-1]
DR EnsemblMetazoa; FBtr0077907; FBpp0077573; FBgn0000579. [P15007-1]
DR EnsemblMetazoa; FBtr0077908; FBpp0077574; FBgn0000579. [P15007-1]
DR EnsemblMetazoa; FBtr0077909; FBpp0077575; FBgn0000579. [P15007-2]
DR EnsemblMetazoa; FBtr0302115; FBpp0291325; FBgn0000579. [P15007-2]
DR GeneID; 33351; -.
DR KEGG; dme:Dmel_CG17654; -.
DR CTD; 33351; -.
DR FlyBase; FBgn0000579; Eno.
DR VEuPathDB; VectorBase:FBgn0000579; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR InParanoid; P15007; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P15007; -.
DR BRENDA; 4.2.1.11; 1994.
DR Reactome; R-DME-70171; Glycolysis.
DR Reactome; R-DME-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 33351; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Eno; fly.
DR GenomeRNAi; 33351; -.
DR PRO; PR:P15007; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000579; Expressed in secondary oocyte and 24 other tissues.
DR ExpressionAtlas; P15007; baseline and differential.
DR Genevisible; P15007; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:FlyBase.
DR GO; GO:0061621; P:canonical glycolysis; ISS:FlyBase.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
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 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..500
FT /note="Enolase"
FT /id="PRO_0000134081"
FT ACT_SITE 277
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 411
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 438..441
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.5"
FT /id="VSP_014147"
FT VARIANT 380
FT /note="D -> A (in strain: SC96_47)"
FT /evidence="ECO:0000269|PubMed:17379620"
FT CONFLICT 335
FT /note="K -> R (in Ref. 4; AAM48478 and 5; AAT47775)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="Q -> K (in Ref. 1; CAA34895)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="R -> G (in Ref. 1; CAA34895)"
FT /evidence="ECO:0000305"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:5WRO"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 245..267
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:5WRO"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:5WRO"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 341..354
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:5WRO"
FT TURN 387..391
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 418..430
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 448..456
FT /evidence="ECO:0007829|PDB:5WRO"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 469..485
FT /evidence="ECO:0007829|PDB:5WRO"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:5WRO"
SQ SEQUENCE 500 AA; 54310 MW; 41CCA31672C01280 CRC64;
MSWTASVFLR TSTTSMKFLR LRWPLPRIPQ NKSANVAPRF RSKSAVSQLS SGFKFVQIRK
STCDSNEMTI KAIKARQIYD SRGNPTVEVD LTTELGLFRA AVPSGASTGV HEALELRDND
KANYHGKSVL KAVGHVNDTL GPELIKANLD VVDQASIDNF MIKLDGTENK SKFGANAILG
VSLAVAKAGA AKKGVPLYKH IADLAGNKEI ILPVPAFNVI NGGSHAGNKL AMQEFMILPT
GATSFTEAMK MGSEVYHHLK NVIKAKFGLD ATAVGDEGGF APNIQSNKEA LNLISDAIAK
AGYTGKIEIG MDVAASEFYK DGQYDLDFKN EKSDKSQWLP ADKLANLYQE FIKDFPIVSI
EDPFDQDHWE AWSNLTGCTD IQIVGDDLTV TNPKRIATAV EKKACNCLLL KVNQIGTVTE
SIAAHLLAKK NGWGTMVSHR SGETEDSFIG DLVVGLSTGQ IKTGAPCRSE RLAKYNQILR
IEEEIGAGVK FAGKSFRKPQ
