ENOA_DICDI
ID ENOA_DICDI Reviewed; 434 AA.
AC Q54RK5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Enolase A;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase A;
DE AltName: Full=2-phosphoglycerate dehydratase A;
GN Name=enoA; ORFNames=DDB_G0283137;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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; AAFI02000050; EAL65898.1; -; Genomic_DNA.
DR RefSeq; XP_639231.1; XM_634139.1.
DR AlphaFoldDB; Q54RK5; -.
DR SMR; Q54RK5; -.
DR STRING; 44689.DDB0231355; -.
DR PaxDb; Q54RK5; -.
DR PRIDE; Q54RK5; -.
DR EnsemblProtists; EAL65898; EAL65898; DDB_G0283137.
DR GeneID; 8623917; -.
DR KEGG; ddi:DDB_G0283137; -.
DR dictyBase; DDB_G0283137; enoA.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q54RK5; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; Q54RK5; -.
DR Reactome; R-DDI-70171; Glycolysis.
DR Reactome; R-DDI-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00187.
DR PRO; PR:Q54RK5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
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 GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..434
FT /note="Enolase A"
FT /id="PRO_0000330350"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 46991 MW; 9AA4156D859BC896 CRC64;
MSVIKSIKAR EILNSRGNPT VEVDLYTEKD GVVSSFRAAV PSGASTGIYE AVELRDGDKS
RYLGKGVLKA IKNILEVIQP AVIGKSVSDQ AAIDKLMIDL DGTPNKGKLG ANAILAVSLA
VCRAGAADRN LPLYKYISEI AGTKMRLPVP AFNVINGGSH AGNKLAMQEF MILPVGAKDF
NEAYRMGSEV YHNLKNVISG RYGQDAINVG DEGGFAPPIQ SNKEGLELLK LAIEKAGYTG
LVKIGMDCAA SEFKVENGYD LDFKTKNNDG SAVISGEKLG DLYREFIKEY PIISIEDPFD
QDDWESYTKL TASVDIQIVG DDLLVTNPER IKTGIEKKAC NALLLKVNQI GSVTESIRAA
LDSKNASWGV MVSHRSGETE DTFIADLVVG LGTGQIKTGA PCRSERLAKY NQLVRINEEL
GENHNYAGLT FRKF
