ENO_ORYSJ
ID ENO_ORYSJ Reviewed; 446 AA.
AC Q42971; Q0IYS8; Q10A26; Q33AR3; Q33AR4; Q42987; Q7XBE4; Q8LM12;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
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=OSE1;
GN Name=ENO1; Synonyms=AD709; OrderedLocusNames=Os10g0167300, LOC_Os10g08550;
GN ORFNames=OSJNAb0015J03.9;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Tainung 67; TISSUE=Seed;
RA Hsing Y.-I.C., Tsao C.-W., Hsieh J.-S., Chen Z.-Y., Shu T.-F., Chow T.-Y.;
RT "A rice early embryogenesis-specific enolase cDNA.";
RL (er) Plant Gene Register PGR95-084(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Akiyama T.;
RT "Molecular characterization of a rice enolase gene up-regulated by moderate
RT low-temperature, low-oxygen, and salt stresses.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 110-188.
RC TISSUE=Callus;
RA Uchimiya H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 174-183; 208-215; 284-293 AND 320-329.
RC STRAIN=cv. Nipponbare; TISSUE=Anther, Callus, Leaf, Panicle, and Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(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;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed during early embryogenesis.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN04181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABB46861.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABB46862.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABG65935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U09450; AAC49173.1; -; mRNA.
DR EMBL; AY335488; AAP94211.1; -; mRNA.
DR EMBL; AC131375; AAN04181.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000086; ABB46861.2; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000086; ABB46862.2; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000086; ABG65935.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008216; BAF26137.1; -; Genomic_DNA.
DR EMBL; AP014966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D17767; BAA04612.1; -; mRNA.
DR PIR; T03267; T03267.
DR RefSeq; XP_015614256.1; XM_015758770.1.
DR AlphaFoldDB; Q42971; -.
DR SMR; Q42971; -.
DR STRING; 4530.OS10T0167300-01; -.
DR PaxDb; Q42971; -.
DR PRIDE; Q42971; -.
DR GeneID; 4348176; -.
DR KEGG; osa:4348176; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; Q42971; -.
DR OrthoDB; 773373at2759; -.
DR PlantReactome; R-OSA-8879007; Response to cold temperature.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q42971; OS.
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 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 Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..446
FT /note="Enolase"
FT /id="PRO_0000134076"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 381..384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 394
FT /note="D -> E (in Ref. 1; AAC49173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 47973 MW; BFCD813193800F1B CRC64;
MAATIVSVKA RQIFDSRGNP TVEVDVCCSD GTFARAAVPS GASTGVYEAL ELRDGGSDYL
GKGVSKAVDN VNSVIAPALI GKDPTSQAEL DNFMVQQLDG TKNEWGWCKQ KLGANAILAV
SLAICKAGAI IKKIPLYQHI ANLAGNKQLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG
AASFKEAMKM GVEVYHNLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIEKA
GYTGKVVIGM DVAASEFYND KDKTYDLNFK EENNDGSQKI SGDSLKNVYK SFVSEYPIVS
IEDPFDQDDW EHYAKMTAEI GEQVQIVGDD LLVTNPTRVA KAIQEKSCNA LLLKVNQIGS
VTESIEAVKM SKRAGWGVMT SHRSGETEDT FIADLAVGLA TGQIKTGAPC RSERLAKYNQ
LLRIEEELGA AAVYAGAKFR APVEPY
