ID   ENOB_HUMAN              Reviewed;         434 AA.
AC   P13929; B4DUI6; B4DUM6; D3DTL2; E7ENK8; Q96AE2;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 5.
DT   27-MAR-2024, entry version 225.
DE   RecName: Full=Beta-enolase;
DE            EC=4.2.1.11 {ECO:0000250|UniProtKB:P15429};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=Enolase 3;
DE   AltName: Full=Muscle-specific enolase;
DE            Short=MSE;
DE   AltName: Full=Skeletal muscle enolase;
GN   Name=ENO3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2587223; DOI=10.1093/nar/17.21.8862;
RA   Peshavaria M., Hinks L.J., Day I.N.M.;
RT   "Structure of human muscle (beta) enolase mRNA and protein deduced from a
RT   genomic clone.";
RL   Nucleic Acids Res. 17:8862-8862(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-85.
RX   PubMed=2336366; DOI=10.1093/nar/18.7.1893;
RA   Cali L., Feo S., Oliva D., Giallongo A.;
RT   "Nucleotide sequence of a cDNA encoding the human muscle-specific enolase
RT   (MSE).";
RL   Nucleic Acids Res. 18:1893-1893(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=1840492; DOI=10.1042/bj2750427;
RA   Peshavaria M., Day I.N.M.;
RT   "Molecular structure of the human muscle-specific enolase gene (ENO3).";
RL   Biochem. J. 275:427-433(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS SER-71 AND
RP   ALA-85.
RX   PubMed=8513787; DOI=10.1111/j.1432-1033.1993.tb17932.x;
RA   Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.;
RT   "Structural features of the human gene for muscle-specific enolase.
RT   Differential splicing in the 5'-untranslated sequence generates two forms
RT   of mRNA.";
RL   Eur. J. Biochem. 214:367-374(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP   SER-71 AND ALA-85.
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-71 AND
RP   ALA-85.
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   INTERACTION WITH PNKD.
RX   PubMed=15188056; DOI=10.1093/abbs/36.6.412;
RA   Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G.,
RA   Gong L.-M.;
RT   "Characterization of MR-1, a novel myofibrillogenesis regulator in human
RT   muscle.";
RL   Acta Biochim. Biophys. Sin. 36:412-418(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND SER-263, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   VARIANTS GSD13 ASP-156 AND GLU-374.
RX   PubMed=11506403; DOI=10.1002/ana.1095;
RA   Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S.,
RA   Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G.,
RA   Bresolin N.;
RT   "Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis.";
RL   Ann. Neurol. 50:202-207(2001).
CC   -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC       phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC       striated muscle development and regeneration.
CC       {ECO:0000250|UniProtKB:P15429}.
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         Evidence={ECO:0000250|UniProtKB:P15429};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC         Evidence={ECO:0000250|UniProtKB:P15429};
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. {ECO:0000250|UniProtKB:P15429}.
CC   -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
CC       beta and gamma, which can form homodimers or heterodimers which are
CC       cell-type and development-specific. Interacts with PNKD.
CC       {ECO:0000269|PubMed:15188056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some
CC       colocalization with CKM at M-band (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P13929-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P13929-2; Sequence=VSP_037753;
CC       Name=3;
CC         IsoId=P13929-3; Sequence=VSP_037752;
CC   -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo
CC       and in most adult tissues. The alpha/beta heterodimer and the beta/beta
CC       homodimer are found in striated muscle, and the alpha/gamma heterodimer
CC       and the gamma/gamma homodimer in neurons.
CC   -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
CC       alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
CC       cells, and to the alpha/gamma heterodimer in nerve cells.
CC   -!- DISEASE: Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic
CC       disorder that results in exercise-induced myalgias, generalized muscle
CC       weakness and fatigability. It is characterized by increased serum
CC       creatine kinase and decreased enolase 3 activity. Dramatically reduced
CC       protein levels with focal sarcoplasmic accumulation of glycogen-beta
CC       particles are detected on ultrastructural analysis.
CC       {ECO:0000269|PubMed:11506403}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; X16504; CAA34513.1; -; mRNA.
DR   EMBL; X51957; CAA36216.1; -; mRNA.
DR   EMBL; X55976; CAA39446.1; -; Genomic_DNA.
DR   EMBL; X56832; CAA40163.1; -; Genomic_DNA.
DR   EMBL; AK300662; BAG62348.1; -; mRNA.
DR   EMBL; AK300709; BAG62388.1; -; mRNA.
DR   EMBL; AC004771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90375.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90379.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90380.1; -; Genomic_DNA.
DR   EMBL; BC017249; AAH17249.1; -; mRNA.
DR   CCDS; CCDS11062.1; -. [P13929-1]
DR   CCDS; CCDS54070.1; -. [P13929-3]
DR   PIR; S06756; S06756.
DR   RefSeq; NP_001180432.1; NM_001193503.1. [P13929-3]
DR   RefSeq; NP_001967.3; NM_001976.4. [P13929-1]
DR   RefSeq; NP_443739.3; NM_053013.3. [P13929-1]
DR   RefSeq; XP_011522031.1; XM_011523729.1. [P13929-1]
DR   RefSeq; XP_016879835.1; XM_017024346.1.
DR   PDB; 2XSX; X-ray; 1.70 A; A/B=1-434.
DR   PDBsum; 2XSX; -.
DR   AlphaFoldDB; P13929; -.
DR   SMR; P13929; -.
DR   BioGRID; 108341; 93.
DR   IntAct; P13929; 30.
DR   STRING; 9606.ENSP00000324105; -.
DR   DrugBank; DB01709; 2-phospho-D-glyceric acid.
DR   DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR   DrugBank; DB01819; Phosphoenolpyruvate.
DR   DrugBank; DB03645; Phosphonoacetohydroxamic Acid.
DR   GlyGen; P13929; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P13929; -.
DR   PhosphoSitePlus; P13929; -.
DR   SwissPalm; P13929; -.
DR   BioMuta; ENO3; -.
DR   DMDM; 425906077; -.
DR   EPD; P13929; -.
DR   jPOST; P13929; -.
DR   MassIVE; P13929; -.
DR   MaxQB; P13929; -.
DR   PaxDb; 9606-ENSP00000324105; -.
DR   PeptideAtlas; P13929; -.
DR   PRIDE; P13929; -.
DR   ProteomicsDB; 12760; -.
DR   ProteomicsDB; 52999; -. [P13929-1]
DR   ProteomicsDB; 53000; -. [P13929-2]
DR   ProteomicsDB; 53001; -. [P13929-3]
DR   Pumba; P13929; -.
DR   Antibodypedia; 630; 480 antibodies from 34 providers.
DR   DNASU; 2027; -.
DR   Ensembl; ENST00000323997.10; ENSP00000324105.6; ENSG00000108515.18. [P13929-1]
DR   Ensembl; ENST00000518175.1; ENSP00000431087.1; ENSG00000108515.18. [P13929-1]
DR   Ensembl; ENST00000519584.5; ENSP00000430636.1; ENSG00000108515.18. [P13929-3]
DR   Ensembl; ENST00000519602.6; ENSP00000430055.2; ENSG00000108515.18. [P13929-1]
DR   GeneID; 2027; -.
DR   KEGG; hsa:2027; -.
DR   MANE-Select; ENST00000519602.6; ENSP00000430055.2; NM_053013.4; NP_443739.3.
DR   UCSC; uc002gac.5; human. [P13929-1]
DR   AGR; HGNC:3354; -.
DR   CTD; 2027; -.
DR   DisGeNET; 2027; -.
DR   GeneCards; ENO3; -.
DR   HGNC; HGNC:3354; ENO3.
DR   HPA; ENSG00000108515; Group enriched (skeletal muscle, tongue).
DR   MalaCards; ENO3; -.
DR   MIM; 131370; gene.
DR   MIM; 612932; phenotype.
DR   neXtProt; NX_P13929; -.
DR   OpenTargets; ENSG00000108515; -.
DR   Orphanet; 99849; Glycogen storage disease due to muscle beta-enolase deficiency.
DR   PharmGKB; PA27789; -.
DR   VEuPathDB; HostDB:ENSG00000108515; -.
DR   eggNOG; KOG2670; Eukaryota.
DR   GeneTree; ENSGT00950000182805; -.
DR   HOGENOM; CLU_031223_0_0_1; -.
DR   InParanoid; P13929; -.
DR   OMA; RHIADIS; -.
DR   OrthoDB; 1093250at2759; -.
DR   PhylomeDB; P13929; -.
DR   TreeFam; TF300391; -.
DR   BioCyc; MetaCyc:ENSG00000108515-MONOMER; -.
DR   PathwayCommons; P13929; -.
DR   Reactome; R-HSA-70171; Glycolysis.
DR   Reactome; R-HSA-70263; Gluconeogenesis.
DR   SABIO-RK; P13929; -.
DR   SignaLink; P13929; -.
DR   SIGNOR; P13929; -.
DR   UniPathway; UPA00109; UER00187.
DR   BioGRID-ORCS; 2027; 17 hits in 1164 CRISPR screens.
DR   ChiTaRS; ENO3; human.
DR   GeneWiki; ENO3; -.
DR   GenomeRNAi; 2027; -.
DR   Pharos; P13929; Tbio.
DR   PRO; PR:P13929; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P13929; Protein.
DR   Bgee; ENSG00000108515; Expressed in skeletal muscle tissue of rectus abdominis and 129 other cell types or tissues.
DR   ExpressionAtlas; P13929; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:CAFA.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
DR   GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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   NCBIfam; TIGR01060; eno; 1.
DR   PANTHER; PTHR11902:SF5; BETA-ENOLASE; 1.
DR   PANTHER; PTHR11902; ENOLASE; 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   SFLD; SFLDG00178; enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
DR   UCD-2DPAGE; P13929; -.
DR   Genevisible; P13929; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Disease variant; Glycogen storage disease; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..434
FT                   /note="Beta-enolase"
FT                   /id="PRO_0000134107"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         370..373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         229
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         236
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P15429"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         61..104
FT                   /note="GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS -> A
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_037752"
FT   VAR_SEQ         150..177
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_037753"
FT   VARIANT         71
FT                   /note="N -> S (in dbSNP:rs238238)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8513787"
FT                   /id="VAR_020618"
FT   VARIANT         85
FT                   /note="V -> A (in dbSNP:rs238239)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2336366,
FT                   ECO:0000269|PubMed:8513787"
FT                   /id="VAR_020619"
FT   VARIANT         156
FT                   /note="G -> D (in GSD13; dbSNP:rs121918403)"
FT                   /evidence="ECO:0000269|PubMed:11506403"
FT                   /id="VAR_020620"
FT   VARIANT         374
FT                   /note="G -> E (in GSD13; dbSNP:rs121918404)"
FT                   /evidence="ECO:0000269|PubMed:11506403"
FT                   /id="VAR_020621"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          18..26
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           87..98
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           108..125
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           130..138
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           178..200
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           220..234
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           273..286
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           301..309
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   TURN            319..323
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           325..334
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          338..342
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           344..347
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           350..362
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           380..388
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   STRAND          391..394
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           401..417
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           418..420
FT                   /evidence="ECO:0007829|PDB:2XSX"
FT   HELIX           425..427
FT                   /evidence="ECO:0007829|PDB:2XSX"
SQ   SEQUENCE   434 AA;  46987 MW;  4D9D8DCF32CF153F CRC64;
     MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK
     GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
     AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE
     AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
     VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD
     WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
     QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
     AIFAGRKFRN PKAK
//