ENO_NOSP7
ID ENO_NOSP7 Reviewed; 429 AA.
AC B2J1R2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=Npun_R3508;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate causes
CC inactivation of the enzyme, and possibly serves as a signal for the
CC export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC present in both the cytoplasm and on the cell surface. The export of
CC enolase possibly depends on the covalent binding to the substrate; once
CC secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; CP001037; ACC81914.1; -; Genomic_DNA.
DR RefSeq; WP_012409888.1; NC_010628.1.
DR AlphaFoldDB; B2J1R2; -.
DR SMR; B2J1R2; -.
DR STRING; 63737.Npun_R3508; -.
DR EnsemblBacteria; ACC81914; ACC81914; Npun_R3508.
DR KEGG; npu:Npun_R3508; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_3; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 533698at2; -.
DR PhylomeDB; B2J1R2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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;
KW Secreted.
FT CHAIN 1..429
FT /note="Enolase"
FT /id="PRO_1000115892"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 340
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 367..370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ SEQUENCE 429 AA; 45755 MW; A9518FDF4FC4CA67 CRC64;
MSKFLDTAIE AIAAREILDS RGRPTIEAEV HLANGVVGLA QVPSGASTGS FEAHELRDGD
KSRYGGKGVL KAVKNVKEAL APKLLGLDAL NQELLDRTMI AIDGSPNKSS LGANAILGVS
LAAAKAGAES LDIPLYRYLG GPLANLLPVP LMNVINGGAH ASNNVDFQEF MIVPIGATSF
REALRWGAEV FATLSQVLDE KGLLTGVGDE GGFAPNLESN QVALELLVAA IKKAGYKPGE
EVALALDVAA SEFYKNGQYV YDGKPHAPAE FIDYLGQLVD QYPIVSIEDG LHEEDWQSWQ
LLTQKLGSQV QLVGDDLFVT NATRLQRGIE EKAANAILIK LNQIGSLTET LETIDLATRN
SIRSVISHRS GETEDTTIAD LAVATRAGQI KTGSLCRSER VAKYNRLLRI EDELGDRAVY
AGAVGLGPK
