ENO_ALTAL
ID ENO_ALTAL Reviewed; 438 AA.
AC Q9HDT3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 101.
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;
DE AltName: Full=Allergen Alt a 11;
DE AltName: Full=Allergen Alt a 5;
DE AltName: Full=Allergen Alt a XI;
DE AltName: Allergen=Alt a 6;
GN Name=ENO; Synonyms=ALTA11, ALTA6;
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC STRAIN=08-0203-Berlin;
RX PubMed=11080711; DOI=10.1067/mai.2000.110799;
RA Simon-Nobbe B., Probst G., Kajava A.V., Oberkofler H., Susani M.,
RA Crameri R., Ferreira F., Ebner C., Breitenbach M.;
RT "IgE-binding epitopes of enolases, a class of highly conserved fungal
RT allergens.";
RL J. Allergy Clin. Immunol. 106:887-895(2000).
RN [2]
RP ALLERGEN.
RX PubMed=9130497; DOI=10.1159/000237521;
RA Breitenbach M., Simon B., Probst G., Oberkofler H., Ferreira F., Briza P.,
RA Achatz G., Unger A., Ebner C., Kraft D., Hirschwehr R.;
RT "Enolases are highly conserved fungal allergens.";
RL Int. Arch. Allergy Immunol. 113:114-117(1997).
RN [3]
RP REVIEW.
RX PubMed=12102004; DOI=10.1159/000058862;
RA Breitenbach M., Simon-Nobbe B.;
RT "The allergens of Cladosporium herbarum and Alternaria alternata.";
RL Chem. Immunol. 81:48-72(2002).
RN [4]
RP REVIEW.
RX PubMed=17709917; DOI=10.1159/000107578;
RA Simon-Nobbe B., Denk U., Poell V., Rid R., Breitenbach M.;
RT "The spectrum of fungal allergy.";
RL Int. Arch. Allergy Immunol. 145:58-86(2008).
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 Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:11080711, ECO:0000269|PubMed:9130497}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; U82437; AAG42022.2; -; mRNA.
DR RefSeq; XP_018379265.1; XM_018535292.1.
DR AlphaFoldDB; Q9HDT3; -.
DR SMR; Q9HDT3; -.
DR Allergome; 14; Alt a 6.
DR Allergome; 3063; Alt a 6.0101.
DR PRIDE; Q9HDT3; -.
DR GeneID; 29120886; -.
DR KEGG; aalt:CC77DRAFT_949988; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Allergen; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..438
FT /note="Enolase"
FT /id="PRO_0000134039"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374..377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 47205 MW; D60900100A72AF83 CRC64;
MTITKIHARS VYDSRGNPTV EVDIVTETGL HRAIVPSGAS TGSHEACELR DGDKSKWGGK
GVTKAVANVN DTIAPALIKE KLDVKDQSAV DAFLNKLDGT TNKTNLGANA ILGVSMAIAK
AAAAEKGVPL YAHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPCEAPTFS
EAMRQGAEVY QKLKALAKKT YGQSAGNVGD EGGVAPDIQT AEEALDLITK AIEEAGYTGK
IKIAMDVASS EFYKADEKKY DLDFKNPDSD KSKWLTYEQL AEMYKSLAEK YPIVSIEDPF
AEDDWEAWSY FFKTYDGQIV GDDLTVTNPE FIKKAIELKS CNALLLKVNQ IGTITEAIQA
AKDAFGAGWG VMVSHRSGET EDVTIADIVV GLRSGQIKTG APARSERLAK LNQILRIEEE
LGDNAVYAGN NFRTAVNL
