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Database: UniProt
Entry: A0A3L6RCE3_PANMI
LinkDB: A0A3L6RCE3_PANMI
Original site: A0A3L6RCE3_PANMI 
ID   A0A3L6RCE3_PANMI        Unreviewed;       445 AA.
AC   A0A3L6RCE3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
GN   ORFNames=C2845_PM06G27660 {ECO:0000313|EMBL:RLM99920.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM99920.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
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:RLM99920.1}.
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DR   EMBL; PQIB02000009; RLM99920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6RCE3; -.
DR   STRING; 4540.A0A3L6RCE3; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000275267; Chromosome 6.
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: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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267}.
FT   DOMAIN          4..139
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          147..441
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        353
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         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;  47897 MW;  005337840AD79A9D CRC64;
     MATIQSVKAR QIFDSRGNPT VEVDVCCSDG TFARAAVPSG ASTGVYEALE LRDGGSDYLG
     KGVSKAVNNV NSIIGPALVG KDPTAQTEID NFMVQQLDGT KNEWGWCKQK LGANAILAVS
     LAVCKAGASI KKIPLYQHIA NLAGNKQLVL PVPAFNVING GSHAGNKLAM QEFMILPTGA
     ASFKEAMKMG VEVYHNLKSV IKKKYGQDAT NVGDEGGFAP NIQENKEGLE LLKTAIEKAG
     YTGKVVIGMD VAASEFYNDK DKTYDLNFKE ENNDGSQKIS GDSLKNVYKS FVSEYPIVSI
     EDPFDQDDWV HYAKMTEEIG EQVQIVGDDL LVTNPTRVAK AIKEKSCNAL LLKVNQIGSV
     TESIQAVKMS KHAGWGVMTS HRSGETEDTF IADLAVGLAT GQIKTGAPCR SERLAKYNQL
     LRIEEELGAA AVYAGAKFRA PVEPY
//
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