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Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

 ENO_DROME               Reviewed;         500 AA.
P15007; A4UZY9; A5XD39; A5XD43; B9EQS7; C0PV73; Q8IPX8; Q8MT10;
Q9VQ38;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
22-NOV-2017, entry version 156.
RecName: Full=Enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=2-phosphoglycerate dehydratase;
Name=Eno; ORFNames=CG17654;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
STRAIN=Canton-S;
PubMed=2106662; DOI=10.1093/nar/18.1.191;
Bishop J.G. III, Corces V.G.;
"The nucleotide sequence of a Drosophila melanogaster enolase gene.";
Nucleic Acids Res. 18:191-191(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
STRAIN=Berkeley; TISSUE=Testis;
Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E.,
George R.A., Pacleb J.M., Park S., Sandler J., Wan K.H., Yu C.,
Rubin G.M., Celniker S.E.;
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-500, AND VARIANT ALA-380.
STRAIN=DPF96_10, DPF96_26, DPF96_5.1, DPF96_8.3, HFL97_23, HFL97_3,
HFL97_5, HFL97_68, MA96_24.2, MA96_26.4, MA96_3.5, MA96_4.4,
MA96_40.1, MA96_42.4, MA96_49.2, SC96_47, VT97_1, Zim(h)_26,
Zim(h)_28, Zim(h)_36, Zim(h)_38, Zim(h)_44, Zim(s)_28, and Zim(s)_49;
PubMed=17379620; DOI=10.1093/molbev/msm057;
Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L.,
Schmidt P., Eanes W.;
"Adaptive evolution of metabolic pathways in Drosophila.";
Mol. Biol. Evol. 24:1347-1354(2007).
[7]
PROTEIN SEQUENCE OF 100-116.
STRAIN=Vallecas; TISSUE=Wing imaginal disk;
PubMed=8500545; DOI=10.1006/excr.1993.1141;
Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
Garcia-Bellido A.;
"Identification of Drosophila wing imaginal disc proteins by two-
dimensional gel analysis and microsequencing.";
Exp. Cell Res. 206:220-226(1993).
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Mg(2+) is required for catalysis and for stabilizing the
dimer.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B; Synonyms=C, D, E;
IsoId=P15007-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=A;
IsoId=P15007-2; Sequence=VSP_014147;
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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EMBL; X17034; CAA34895.1; -; Genomic_DNA.
EMBL; AE014134; AAF51344.2; -; Genomic_DNA.
EMBL; AE014134; AAN10455.1; -; Genomic_DNA.
EMBL; AE014134; AAN10456.1; -; Genomic_DNA.
EMBL; AE014134; AAN10457.1; -; Genomic_DNA.
EMBL; AE014134; AAN10458.1; -; Genomic_DNA.
EMBL; AY118449; AAM48478.1; -; mRNA.
EMBL; BT014924; AAT47775.1; -; mRNA.
EMBL; BT058002; ACM16712.1; -; mRNA.
EMBL; BT072929; ACN86077.1; -; mRNA.
EMBL; DQ864190; ABH06825.1; -; Genomic_DNA.
EMBL; DQ864191; ABH06826.1; -; Genomic_DNA.
EMBL; DQ864192; ABH06827.1; -; Genomic_DNA.
EMBL; DQ864193; ABH06828.1; -; Genomic_DNA.
EMBL; DQ864194; ABH06829.1; -; Genomic_DNA.
EMBL; DQ864195; ABH06830.1; -; Genomic_DNA.
EMBL; DQ864196; ABH06831.1; -; Genomic_DNA.
EMBL; DQ864197; ABH06832.1; -; Genomic_DNA.
EMBL; DQ864198; ABH06833.1; -; Genomic_DNA.
EMBL; DQ864199; ABH06834.1; -; Genomic_DNA.
EMBL; DQ864200; ABH06835.1; -; Genomic_DNA.
EMBL; DQ864201; ABH06836.1; -; Genomic_DNA.
EMBL; DQ864202; ABH06837.1; -; Genomic_DNA.
EMBL; DQ864203; ABH06838.1; -; Genomic_DNA.
EMBL; DQ864204; ABH06839.1; -; Genomic_DNA.
EMBL; DQ864205; ABH06840.1; -; Genomic_DNA.
EMBL; DQ864206; ABH06841.1; -; Genomic_DNA.
EMBL; DQ864207; ABH06842.1; -; Genomic_DNA.
EMBL; DQ864208; ABH06843.1; -; Genomic_DNA.
EMBL; DQ864209; ABH06844.1; -; Genomic_DNA.
EMBL; DQ864210; ABH06845.1; -; Genomic_DNA.
EMBL; DQ864211; ABH06846.1; -; Genomic_DNA.
EMBL; DQ864212; ABH06847.1; -; Genomic_DNA.
EMBL; DQ864213; ABH06848.1; -; Genomic_DNA.
PIR; S07586; S07586.
RefSeq; NP_001162853.1; NM_001169382.2. [P15007-2]
RefSeq; NP_477421.1; NM_058073.5. [P15007-2]
RefSeq; NP_722721.1; NM_164431.3. [P15007-1]
RefSeq; NP_722722.1; NM_164432.3. [P15007-1]
RefSeq; NP_722723.1; NM_164433.3. [P15007-1]
RefSeq; NP_722724.1; NM_164434.3. [P15007-1]
UniGene; Dm.18435; -.
PDB; 5WRO; X-ray; 2.02 A; A=69-500.
PDBsum; 5WRO; -.
ProteinModelPortal; P15007; -.
SMR; P15007; -.
BioGrid; 59591; 90.
IntAct; P15007; 5.
MINT; MINT-338625; -.
STRING; 7227.FBpp0077572; -.
PaxDb; P15007; -.
PRIDE; P15007; -.
EnsemblMetazoa; FBtr0077905; FBpp0077571; FBgn0000579. [P15007-1]
EnsemblMetazoa; FBtr0077906; FBpp0077572; FBgn0000579. [P15007-1]
EnsemblMetazoa; FBtr0077907; FBpp0077573; FBgn0000579. [P15007-1]
EnsemblMetazoa; FBtr0077908; FBpp0077574; FBgn0000579. [P15007-1]
EnsemblMetazoa; FBtr0077909; FBpp0077575; FBgn0000579. [P15007-2]
EnsemblMetazoa; FBtr0302115; FBpp0291325; FBgn0000579. [P15007-2]
GeneID; 33351; -.
KEGG; dme:Dmel_CG17654; -.
CTD; 33351; -.
FlyBase; FBgn0000579; Eno.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
GeneTree; ENSGT00900000141167; -.
InParanoid; P15007; -.
KO; K01689; -.
OMA; EFMIIPV; -.
OrthoDB; EOG091G07NH; -.
PhylomeDB; P15007; -.
Reactome; R-DME-70171; Glycolysis.
Reactome; R-DME-70263; Gluconeogenesis.
UniPathway; UPA00109; UER00187.
ChiTaRS; Eno; fly.
GenomeRNAi; 33351; -.
PRO; PR:P15007; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000579; -.
ExpressionAtlas; P15007; differential.
Genevisible; P15007; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR034390; Enolase-like_superfamily.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PRINTS; PR00148; ENOLASE.
SFLD; SFLDG00178; enolase; 1.
SFLD; SFLDS00001; Enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycolysis; Lyase; Magnesium;
Metal-binding; Polymorphism; Reference proteome.
CHAIN 1 500 Enolase.
/FTId=PRO_0000134081.
REGION 438 441 Substrate binding. {ECO:0000250}.
ACT_SITE 277 277 Proton donor. {ECO:0000250}.
ACT_SITE 411 411 Proton acceptor. {ECO:0000250}.
METAL 312 312 Magnesium. {ECO:0000250}.
METAL 361 361 Magnesium. {ECO:0000250}.
METAL 386 386 Magnesium. {ECO:0000250}.
BINDING 225 225 Substrate. {ECO:0000250}.
BINDING 234 234 Substrate. {ECO:0000250}.
BINDING 361 361 Substrate. {ECO:0000250}.
BINDING 386 386 Substrate. {ECO:0000250}.
BINDING 462 462 Substrate. {ECO:0000250}.
VAR_SEQ 1 67 Missing (in isoform A).
{ECO:0000303|PubMed:12537569,
ECO:0000303|Ref.5}.
/FTId=VSP_014147.
VARIANT 380 380 D -> A (in strain: SC96_47).
{ECO:0000269|PubMed:17379620}.
CONFLICT 335 335 K -> R (in Ref. 4; AAM48478 and 5;
AAT47775). {ECO:0000305}.
CONFLICT 349 349 Q -> K (in Ref. 1; CAA34895).
{ECO:0000305}.
CONFLICT 497 497 R -> G (in Ref. 1; CAA34895).
{ECO:0000305}.
STRAND 72 79 {ECO:0000244|PDB:5WRO}.
STRAND 85 93 {ECO:0000244|PDB:5WRO}.
STRAND 96 101 {ECO:0000244|PDB:5WRO}.
STRAND 110 112 {ECO:0000244|PDB:5WRO}.
HELIX 124 126 {ECO:0000244|PDB:5WRO}.
HELIX 130 138 {ECO:0000244|PDB:5WRO}.
HELIX 140 147 {ECO:0000244|PDB:5WRO}.
HELIX 154 165 {ECO:0000244|PDB:5WRO}.
TURN 171 173 {ECO:0000244|PDB:5WRO}.
HELIX 175 193 {ECO:0000244|PDB:5WRO}.
HELIX 197 204 {ECO:0000244|PDB:5WRO}.
STRAND 217 221 {ECO:0000244|PDB:5WRO}.
HELIX 223 225 {ECO:0000244|PDB:5WRO}.
STRAND 226 229 {ECO:0000244|PDB:5WRO}.
STRAND 234 238 {ECO:0000244|PDB:5WRO}.
HELIX 245 267 {ECO:0000244|PDB:5WRO}.
HELIX 269 272 {ECO:0000244|PDB:5WRO}.
HELIX 287 301 {ECO:0000244|PDB:5WRO}.
TURN 304 306 {ECO:0000244|PDB:5WRO}.
STRAND 308 312 {ECO:0000244|PDB:5WRO}.
HELIX 315 318 {ECO:0000244|PDB:5WRO}.
TURN 326 329 {ECO:0000244|PDB:5WRO}.
HELIX 335 337 {ECO:0000244|PDB:5WRO}.
HELIX 341 354 {ECO:0000244|PDB:5WRO}.
STRAND 357 361 {ECO:0000244|PDB:5WRO}.
HELIX 369 378 {ECO:0000244|PDB:5WRO}.
STRAND 381 386 {ECO:0000244|PDB:5WRO}.
TURN 387 391 {ECO:0000244|PDB:5WRO}.
HELIX 393 402 {ECO:0000244|PDB:5WRO}.
STRAND 406 410 {ECO:0000244|PDB:5WRO}.
HELIX 412 415 {ECO:0000244|PDB:5WRO}.
HELIX 418 430 {ECO:0000244|PDB:5WRO}.
STRAND 434 438 {ECO:0000244|PDB:5WRO}.
HELIX 448 456 {ECO:0000244|PDB:5WRO}.
STRAND 459 462 {ECO:0000244|PDB:5WRO}.
HELIX 469 485 {ECO:0000244|PDB:5WRO}.
HELIX 493 495 {ECO:0000244|PDB:5WRO}.
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


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EIAAB12965 2-phospho-D-glycerate hydro-lyase,Beta-enolase,ENO3,Enolase 3,MSE,Muscle-specific enolase,Pig,Skeletal muscle enolase,Sus scrofa
U1449h CLIA 2-phospho-D-glycerate hydro-lyase,Alpha-enolase,C-myc promoter-binding protein,ENO1,ENO1L1,Enolase 1,Homo sapiens,Human,MBP-1,MBPB1,MPB1,MPB-1,NNE,Non-neural enolase,Phosphopyruvate hydratase,Pla 96T


 

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