ENO_DAVTA
ID ENO_DAVTA Reviewed; 440 AA.
AC P42040; Q6LC77;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 Cla h VI;
DE AltName: Allergen=Cla h 6;
GN Name=ENO; Synonyms=CLAH6;
OS Davidiella tassiana (Mycosphaerella tassiana) (Cladosporium herbarum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Cladosporium.
OX NCBI_TaxID=29918;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RC STRAIN=280202-Berlin;
RX PubMed=7898496; DOI=10.1016/0161-5890(94)00108-d;
RA Achatz G., Oberkofler H., Lechenauer E., Simon-Nobbe B., Unger A.,
RA Kandler D., Ebner C., Prillinger H., Kraft D., Breitenbach M.;
RT "Molecular cloning of major and minor allergens of Alternaria alternata and
RT Cladosporium herbarum.";
RL Mol. Immunol. 32:213-227(1995).
RN [2]
RP SEQUENCE REVISION TO 38; 285; 286; 427 AND 428.
RA Simon B.;
RL Submitted (OCT-1998) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=280202-Berlin; TISSUE=Hyphae;
RA Simon-Nobbe B., Oberkofler H., Probst G., Breitenbach M., Achatz G.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IGE-BINDING, AND MUTAGENESIS OF LYS-141.
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 [6]
RP IGE-BINDING.
RX DOI=10.1159/000053679;
RA Simon-Nobbe B., Kodzius R., Kajava A., Ferreira F., Kungl A., Achatz G.,
RA Crameri R., Ebner C., Breitenbach M.;
RT "Structure of an IgE-binding peptide from fungal enolases.";
RL Int. Arch. Allergy Immunol. 124:93-94(2001).
RN [7]
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).
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. Second
CC most important allergen of C.herbarum in terms of frequency of
CC sensitization. {ECO:0000269|PubMed:7898496,
CC ECO:0000269|PubMed:9130497}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; X78226; CAA55070.1; -; mRNA.
DR EMBL; U82438; AAR00929.2; -; Genomic_DNA.
DR PIR; S43113; S43113.
DR AlphaFoldDB; P42040; -.
DR SMR; P42040; -.
DR Allergome; 221; Cla h 6.
DR Allergome; 3205; Cla h 6.0101.
DR PRIDE; P42040; -.
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..440
FT /note="Enolase"
FT /id="PRO_0000134046"
FT REGION 120..189
FT /note="IgE-binding determinant"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
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 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376..379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 141
FT /note="K->A,Q: No effect on IgE-binding."
FT /evidence="ECO:0000269|PubMed:11080711"
FT CONFLICT 175
FT /note="G -> A (in Ref. 3; AAR00929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 47519 MW; FF43316D94740DFB CRC64;
MPISKIHSRY VYDSRGNPTV EVDIVTETGL HRAIVPSGAS TGSHEACELR DGDKSKWAGK
GVTKAVANVN EIIAPALIKE NLDVKDQAAV DAFLNKLDGT TNKTKIGANA ILGVSMAVAK
AAAAEKRVPL YAHISDLSGT KKPFVLPVPF MNVVNGGSHA GGRLAFQEFM IVPSGAPSFT
EAMRQGAEVY QKLKSLTKKR YGQSAGNVGD EGGVAPDIQT AEEALDLITD AIEEAGYTGQ
IKIAMDVASS EFYKADEKKY DLDFKNPDSD KSKWITYEQL ADQYKQLAAK YPIVSIEDPF
AEDDWEAWSY FYKTSGSDFQ IVGDDLTVTN PEFIKKAIET KACNALLLKV NQIGTITEAI
NAAKDSFAAG WGVMVSHRSG ETEDVTIADI VVGLRAGQIK TGAPARSERL AKLNQILRIE
EELGDKAVYA GDNFRTAINL
