ENO_ASPFU
ID ENO_ASPFU Reviewed; 438 AA.
AC Q96X30; Q4WND2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
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: Allergen=Asp f 22;
GN Name=enoA; ORFNames=AFUA_6G06770;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22, AND ALLERGEN.
RC STRAIN=CCRC 33476;
RX PubMed=11979043; DOI=10.1159/000053862;
RA Lai H.-Y., Tam M.F., Tang R.-B., Chou H., Chang C.-Y., Tsai J.-J.,
RA Shen H.-D.;
RT "cDNA cloning and immunological characterization of a newly identified
RT enolase allergen from Penicillium citrinum and Aspergillus fumigatus.";
RL Int. Arch. Allergy Immunol. 127:181-190(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:11979043}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; AF284645; AAK49451.1; -; mRNA.
DR EMBL; AAHF01000006; EAL88532.1; -; Genomic_DNA.
DR RefSeq; XP_750570.1; XM_745477.1.
DR PDB; 7RHV; X-ray; 2.00 A; A/B=1-438.
DR PDB; 7RHW; X-ray; 1.90 A; A/B=1-438.
DR PDB; 7RI0; X-ray; 2.30 A; A/B=1-438.
DR PDBsum; 7RHV; -.
DR PDBsum; 7RHW; -.
DR PDBsum; 7RI0; -.
DR AlphaFoldDB; Q96X30; -.
DR SMR; Q96X30; -.
DR STRING; 746128.CADAFUBP00007078; -.
DR Allergome; 3116; Asp f 22.0101.
DR Allergome; 72; Asp f 22.
DR SwissPalm; Q96X30; -.
DR PRIDE; Q96X30; -.
DR EnsemblFungi; EAL88532; EAL88532; AFUA_6G06770.
DR GeneID; 3508747; -.
DR KEGG; afm:AFUA_6G06770; -.
DR VEuPathDB; FungiDB:Afu6g06770; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q96X30; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 773373at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0019863; F:IgE binding; IDA:AspGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
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 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 3D-structure; Allergen; Cytoplasm; Direct protein sequencing; Glycolysis;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11979043"
FT CHAIN 2..438
FT /note="Enolase"
FT /id="PRO_0000134041"
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"
FT CONFLICT 25
FT /note="V -> A (in Ref. 1; AAK49451)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="A -> T (in Ref. 1; AAK49451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 47305 MW; 821212CBDCBAEA2A CRC64;
MPISKIHARS VYDSRGNPTV EVDVVTETGL HRAIVPSGAS TGQHEAHELR DGDKTQWGGK
GVLKAVKNVN ETIGPALIKE NIDVKDQSKV DEFLNKLDGT ANKSNLGANA ILGVSLAVAK
AGAAEKGVPL YAHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPDSAPSFS
EALRQGAEVY QKLKALAKKK YGQSAGNVGD EGGVAPDIQT AEEALDLITE AIEQAGYTGK
IKIAMDVASS EFYKADVKKY DLDFKNPESD PSKWLTYEQL ADLYKSLAAK YPIVSIEDPF
AEDDWEAWSY FYKTSDFQIV GDDLTVTNPG RIKKAIELKS CNALLLKVNQ IGTLTESIQA
AKDSYADNWG VMVSHRSGET EDVTIADIAV GLRSGQIKTG APCRSERLAK LNQILRIEEE
LGENAVYAGS KFRTAVNL
