ENO_GEMAT
ID ENO_GEMAT Reviewed; 426 AA.
AC C1A7Y3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GAU_1301;
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC Gemmatimonas.
OX NCBI_TaxID=379066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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; AP009153; BAH38343.1; -; Genomic_DNA.
DR RefSeq; WP_012682790.1; NC_012489.1.
DR AlphaFoldDB; C1A7Y3; -.
DR SMR; C1A7Y3; -.
DR STRING; 379066.GAU_1301; -.
DR PRIDE; C1A7Y3; -.
DR EnsemblBacteria; BAH38343; BAH38343; GAU_1301.
DR KEGG; gau:GAU_1301; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_0; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 533698at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002209; 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..426
FT /note="Enolase"
FT /id="PRO_1000205095"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 338
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 365..368
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ SEQUENCE 426 AA; 45331 MW; 911D0703294B5FF2 CRC64;
MASIVAVSAR EILDSRGNPT VEVDVVLETG AAGRAAVPSG ASTGEREAVE LRDGDPARYG
GKGVLNAVNN VNTEIAEALE DMDATDQIAV DRALLDLDGT ENKGRLGANA MLGVSMAVAR
AAAFEVGLPL YRYLGGPMAR TLPVPMMNIL NGGAHATNTV DFQEFMIIPV GADSFADGLR
MGTQVFHQLK KVLVSRKLST GVGDEGGFAP NLASDEEALK VIIEAIEAAG FRPGQDIALA
LDVAASELFQ NGQYHFKKSG APSRSPKDMA EMYAGWLEQY PIVSIEDGMS ENDWDGWKLL
TEKIGDRCQL VGDDLFCTNS EILAKGIEND VANAILIKVN QIGTLTETFE AIELARSAGY
NSVISHRSGE TEDTFIADLA VATQAGQIKT GAPSRSDRVA KYNQLLRIEE QLEGYAEYPG
GAIFGI
