ENO_CAMHC
ID ENO_CAMHC Reviewed; 415 AA.
AC A7I455;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=CHAB381_1786;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) 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; CP000776; ABS52371.1; -; Genomic_DNA.
DR AlphaFoldDB; A7I455; -.
DR SMR; A7I455; -.
DR STRING; 360107.CHAB381_1786; -.
DR EnsemblBacteria; ABS52371; ABS52371; CHAB381_1786.
DR KEGG; cha:CHAB381_1786; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_7; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002407; 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..415
FT /note="Enolase"
FT /id="PRO_0000337613"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 333
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 360..363
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ SEQUENCE 415 AA; 45557 MW; DE600709083278A6 CRC64;
MIITDIYAQE VLDSRGNPTV RAFVALEDGT LAGATVPSGA STGKREALEL RDGDERFCGK
GVLKAVENVN TVIADEIVGM NVYEQKDIDN AMKKLDGTEN YSNLGANAVL GVSMAVARAA
AMSLGIPLYR YLGGANAQIL PVPMFNIING GAHANNSVDF QEFMVMPFGF DCFSDALRAV
AEIYQNLKKI LNELGYSTAV GDEGGFAPNL KDNEEPIKII MQAIKKAGYE PGKQIKIALD
VAASELYENG KYRLEGKTFT SEELIERYVK LCEKYPIFSI EDGLGEDDWE GWKKLTARLK
DKIQLVGDDL FVTNEKILRE GIEKGIANAI LIKPNQIGSI TQTMQTVRLA QRNGYRCIMS
HRSGESEDSF IADFAVALNT GEIKTGATSR SERNAKYNRL LEIECENTEF LGNKI
