ID   ENO_PENCH               Reviewed;         438 AA.
AC   Q76KF9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
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;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 10002 / CBS 277.47 / NBRC 4626 / Wis. Q-176;
RX   PubMed=14734176; DOI=10.1016/s0378-1097(03)00886-3;
RA   Sugimoto M., Saiki Y., Zhang D., Kawai F.;
RT   "Cloning and characterization of preferentially expressed genes in an
RT   aluminum-tolerant mutant derived from Penicillium chrysogenum IFO4626.";
RL   FEMS Microbiol. Lett. 230:137-142(2004).
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; AB091508; BAC82549.1; -; mRNA.
DR   AlphaFoldDB; Q76KF9; -.
DR   SMR; Q76KF9; -.
DR   PRIDE; Q76KF9; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..438
FT                   /note="Enolase"
FT                   /id="PRO_0000134055"
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;  47236 MW;  31F6D922CCDA2473 CRC64;
     MPISKIHARS VYDSRGNPTV EVDVVTETGL HRAIVPSGAS TGLHEVVELR DGDKTKWGGK
     GVLNAVKNVN DVIGPALIKE NIDVKDQAKV DEFLNKLDGT PNKGKLGANA ILGVSLAVAK
     AAAAEKGVPL YAHISDLAGT KKPFVLPVPF QNVLNGGSHA GGRLAFQEFM IVPDTAPTFS
     EGLRQGAEVY QELKALAKKK YGQSAGNVGD EGGVAPDIQT AEEALDLITE AIEQAGYTGQ
     IKIAMDVASS EFYKEDAKKY DLDFKNPESD PTKWLTYEQL ADLYKSLAAK YPIVSIEDPF
     AEDDWEAWSY FYKTSDFQIV GDDLTVTNPL RIKKAIELKS CNALLLKVNQ IGTLTESIQA
     AKDSYADGWG VMVSHRSGET EDVTIADIAV GLRAGQIKTG APARSERLAK LNQILRIEEE
     LGANAVYAGE KFRTAVNL