ENO_DESVM
ID ENO_DESVM Reviewed; 434 AA.
AC O32513; B8DMB0; Q9KVZ6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=DvMF_1810;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14746912; DOI=10.1016/j.bbaexp.2003.11.008;
RA Kitamura M., Takayama Y., Kojima S., Kohno K., Ogata H., Higuchi Y.,
RA Inoue H.;
RT "Cloning and expression of the enolase gene from Desulfovibrio vulgaris
RT (Miyazaki F).";
RL Biochim. Biophys. Acta 1676:172-181(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-165.
RA Kitamura M., Konishi T., Kawanishi K., Ohashi K., Kishida M., Kohno K.,
RA Akutsu H., Kumagai I., Nakaya T.;
RL Submitted (JUL-1997) 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 ECO:0000269|PubMed:14746912}.
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, ECO:0000269|PubMed:14746912};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=136 uM for 2-phosphoglycerate (at 25 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:14746912};
CC KM=674 uM for phosphoenolpyruvate (at 25 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:14746912};
CC pH dependence:
CC Optimum pH is 7.8-8.1. {ECO:0000269|PubMed:14746912};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:14746912}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB046715; BAB07786.1; -; Genomic_DNA.
DR EMBL; CP001197; ACL08754.1; -; Genomic_DNA.
DR EMBL; AB005550; BAA21475.1; -; Genomic_DNA.
DR RefSeq; WP_012612929.1; NC_011769.1.
DR AlphaFoldDB; O32513; -.
DR SMR; O32513; -.
DR STRING; 883.DvMF_1810; -.
DR EnsemblBacteria; ACL08754; ACL08754; DvMF_1810.
DR KEGG; dvm:DvMF_1810; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_7; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 533698at2; -.
DR UniPathway; UPA00109; UER00187.
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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Secreted.
FT CHAIN 1..434
FT /note="Enolase"
FT /id="PRO_0000133881"
FT REGION 29..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 337
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 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 337
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 364..367
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT CONFLICT 34
FT /note="R -> G (in Ref. 3; BAA21475)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="D -> N (in Ref. 3; BAA21475)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="G -> A (in Ref. 3; BAA21475)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..120
FT /note="TAR -> HRA (in Ref. 3; BAA21475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 434 AA; 46689 MW; F4C0AB4AE4AEBC33 CRC64;
MSTIVSVWAR EILDSRGNPT VEVEVSLESG HTGRAAVPSG ASTGSREALE MRDGDKGRYK
GKGVEKAVDN VMGEIAEAIV GLDSLRQVQV DNTLLDLDGT DNKSRLGANA MLGVSLATAR
AASSFLGLPL YQYLGGVNAK VLPVPLMNII NGGAHAPNNL DIQEFMIMPI GAATFRDALR
MGAETFHTLK ALLAADGHVT SVGDEGGFAP NLKNHDEAFR YIMKAIEEAG YIPGAEIALA
IDAAASEFHK DGKYVLAGEG KNLSNSEMVE WLGEFTTRYP LISIEDGLAE ADWDGWRELT
YKLGDTIQLV GDDIFVTNPD ILAEGIDEGV ANSILIKLNQ IGTLTETLDT IEMAKQAAYT
TVISHRSGET EDHFISDLAV GLNAGQIKTG SLCRSDRLAK YNQLLRIEED LDDTGIYFGP
MMSSHFGFEE EGEE
