ENO_ASPOR
ID ENO_ASPOR Reviewed; 438 AA.
AC Q12560; Q2UMC4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
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;
GN Name=enoA; ORFNames=AO090003000055;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=8824839; DOI=10.1271/bbb.60.161;
RA Machida M., Gonzalez T.V., Boon L.K., Gomi K., Jigami Y.;
RT "Molecular cloning of a genomic DNA for enolase from Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 60:161-163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=8929395; DOI=10.1007/s002940050152;
RA Machida M., Chang Y., Manabe M., Yasukawa M., Kunihiro S., Jigami Y.;
RT "Molecular cloning of a cDNA encoding enolase from the filamentous fungus,
RT Aspergillus oryzae.";
RL Curr. Genet. 30:423-431(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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 -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; D63941; BAA09973.1; -; Genomic_DNA.
DR EMBL; D64113; BAA23760.1; -; mRNA.
DR EMBL; AP007155; BAE57291.1; -; Genomic_DNA.
DR PIR; JC4542; JC4542.
DR RefSeq; XP_001819293.1; XM_001819241.2.
DR AlphaFoldDB; Q12560; -.
DR SMR; Q12560; -.
DR STRING; 510516.Q12560; -.
DR PRIDE; Q12560; -.
DR EnsemblFungi; BAE57291; BAE57291; AO090003000055.
DR GeneID; 5991276; -.
DR KEGG; aor:AO090003000055; -.
DR VEuPathDB; FungiDB:AO090003000055; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000006564; Chromosome 2.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..438
FT /note="Enolase"
FT /id="PRO_0000134042"
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; 47406 MW; 1333325EEAEABBE0 CRC64;
MPITKIHARS VYDSRGNPTV EVDVVTETGL HRAIVPSGAS TGQHEAHELR DGDKTHWGGK
GVLKAVENVN KTIAPAVIEE NLDVKDQSKV DEFLKKLDGS ANKSNLGANA ILGVSLAIAK
AGAAEKGVPL YAHISDLAGT KKPYVLPVPF QNVLNGGSHA GGRLAFQEFM IVPSAAPSFS
EALRQGAEVY QKLKTLAKKK YGQSAGNVGD EGGVAPDIQT AEEALDLITE AIEQAGYTGK
MKIAMDVASS EFYKADVKKY DLDFKNPDSD SSKWLTYEQL ADLYKTLASK YPIVSIEDPF
AEDDWEAWSY FYKTSDFQIV GDDLTVTNPL RIKKAIETKA CNALLLKVNQ IGTLTESIQA
AKDSYADNWG VMVSHRSGET EDVTIADIAV GLRSGQIKTG APARSERLAK LNQILRIEEE
LGNNAIYAGE KFRTSVNL
