ID Q10P35_ORYSJ Unreviewed; 445 AA.
AC Q10P35;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN OrderedLocusNames=LOC_Os03g14450 {ECO:0000313|EMBL:ABF94968.1},
GN Os03g0248600 {ECO:0000313|EMBL:BAS83270.1};
GN ORFNames=OSNPB_030248600 {ECO:0000313|EMBL:BAS83270.1};
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 {ECO:0000313|EMBL:ABF94968.1};
RN [1] {ECO:0000313|EMBL:BAG93549.1}
RP NUCLEOTIDE SEQUENCE.
RA Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N.,
RA Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., Namiki T.,
RA Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., Shishiki T., Otomo Y.,
RA Murakami K., Iida Y., Sugano S., Fujimura T., Suzuki Y., Tsunoda Y.,
RA Kurosaki T., Kodama T., Masuda H., Kobayashi M., Xie Q., Lu M.,
RA Narikawa R., Sugiyama A., Mizuno K., Yokomizo S., Niikura J., Ikeda R.,
RA Ishibiki J., Kawamata M., Yoshimura A., Miura J., Kusumegi T., Oka M.,
RA Ryu R., Ueda M., Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K.,
RA Arakawa T., Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N.,
RA Ota Y., Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T.,
RA Yoshino M., Hayashizaki Y.;
RT "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from
RT japonica Rice.";
RL Science 301:376-379(2003).
RN [2] {ECO:0000313|EMBL:ABF94968.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG Rice Chromosome 3 Sequencing Consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S., Luo M.,
RA Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G.,
RA Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3] {ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4] {ECO:0000313|EMBL:ABF94968.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R., Wing R.A., McCombie W.A., Ouyang S.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BAS83270.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23299411; DOI=10.1093/pcp/pcs183;
RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H.,
RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T.,
RA Matsumoto T., Sasaki T., Itoh T.;
RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive
RT database for rice genomics.";
RL Plant Cell Physiol. 54:E6-E6(2013).
RN [6] {ECO:0000313|EMBL:BAS83270.1, ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
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] {ECO:0000313|EMBL:BAS83270.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000009; ABF94968.1; -; Genomic_DNA.
DR EMBL; AK073611; BAG93549.1; -; mRNA.
DR EMBL; AK099342; BAG94076.1; -; mRNA.
DR EMBL; AP014959; BAS83270.1; -; Genomic_DNA.
DR RefSeq; XP_015632611.1; XM_015777125.1.
DR AlphaFoldDB; Q10P35; -.
DR SMR; Q10P35; -.
DR STRING; 39947.Q10P35; -.
DR PaxDb; 39947-Q10P35; -.
DR EnsemblPlants; Os03t0248600-01; Os03t0248600-01; Os03g0248600.
DR EnsemblPlants; Os03t0248600-02; Os03t0248600-02; Os03g0248600.
DR GeneID; 4332253; -.
DR Gramene; Os03t0248600-01; Os03t0248600-01; Os03g0248600.
DR Gramene; Os03t0248600-02; Os03t0248600-02; Os03g0248600.
DR KEGG; osa:4332253; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR OMA; VDICCSD; -.
DR OrthoDB; 1093250at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000059680; Chromosome 3.
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; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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 NCBIfam; TIGR01060; eno; 1.
DR PANTHER; PTHR11902; ENOLASE; 1.
DR PANTHER; PTHR11902:SF1; ENOLASE; 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 SFLD; SFLDG00178; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Proteomics identification {ECO:0007829|ProteomicsDB:Q10P35};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680}.
FT DOMAIN 5..140
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 148..441
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 380..383
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 445 AA; 47973 MW; E03EF302CD580423 CRC64;
MAATIQSVKA RQIFDSRGNP TVEVDICCSD GTFARAAVPS GASTGVYEAL ELRDGGSDYL
GKGVLKAVDN VNSIIGPALI GKDPTEQTVI DNFMVQQLDG TKNEWGWCKQ KLGANAILAV
SLALCKAGAI IKKIPLYQHI ANLAGNKQLV LPVPAFNVIN GGSHAGNKLA MQEFMILPTG
ASSFKEAMKM GVEVYHNLKS VIKKKYGQDA TNVGDEGGFA PNIQENKEGL ELLKTAIEKA
GYTGKVVIGM DVAASEFYTE DQTYDLNFKE ENNDGSQKIS GDSLKNVYKS FVSEYPIVSI
EDPFDQDDWV HYAKMTEEIG DQVQIVGDDL LVTNPTRVAK AIKDKACNAL LLKVNQIGSV
TESIEAVKMS KRAGWGVMTS HRSGETEDTF IADLAVGLST GQIKTGAPCR SERLAKYNQL
LRIEEELGAA AVYAGAKFRA PVEPY
//
