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Database: UniProt
Entry: A0A2P6RBH1_ROSCH
LinkDB: A0A2P6RBH1_ROSCH
Original site: A0A2P6RBH1_ROSCH 
ID   A0A2P6RBH1_ROSCH        Unreviewed;       444 AA.
AC   A0A2P6RBH1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN   ORFNames=RchiOBHm_Chr3g0472001 {ECO:0000313|EMBL:PRQ43774.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ43774.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ43774.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRQ43774.1}.
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DR   EMBL; PDCK01000041; PRQ43774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6RBH1; -.
DR   STRING; 74649.A0A2P6RBH1; -.
DR   EnsemblPlants; PRQ43774; PRQ43774; RchiOBHm_Chr3g0472001.
DR   Gramene; PRQ43774; PRQ43774; RchiOBHm_Chr3g0472001.
DR   OMA; MIMEATE; -.
DR   OrthoDB; 1093250at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000238479; Chromosome 3.
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; 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:SF41; PHOSPHOPYRUVATE HYDRATASE; 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; SFLDS00001; 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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PRQ43774.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:PRQ43774.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238479}.
FT   DOMAIN          4..139
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          147..440
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         379..382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         403
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   444 AA;  47798 MW;  8BA13DA455920348 CRC64;
     MATIQSVKAR QIFDSRGNPT VEVDIVLSDG FLARAAVPSG ASTGVYEALE LRDGGKEYLG
     KGVSKAVNNV NSIIGPALIG KDPSEQTAID NFMVQQLDGT VNEWGWCKQK LGANAILAVS
     LAVCKAGASV KKIPLYKHIA NLAGNKNLVL PVPAFNVING GSHAGNKLAM QEFMILPVGA
     SSFKEAMKMG VEVYHNLKSV IKKKYGQDAT NVGDEGGFAP NIQENKEGLE LLKTAIEKAG
     YTGKVVIGMD VAASEFYGTD KTYDLNFKEE KNDGSSKISG NALKDLYKSF ASEYPIVSIE
     DPFDQDDWEH YSKMTAECGE QVQIVGDDLL VTNPKRVEKA IKEKSCNALL LKVNQIGSVT
     ESIEAVRMSK KAGWGVMASH RSGETEDTFI ADLSVGLATG QIKTGAPCRS ERLAKYNQLL
     RIEEELGSAA VYAGAKFRVP VEPY
//
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