ENO_DESPS
ID ENO_DESPS Reviewed; 423 AA.
AC Q6AM97;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=DP1799;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36528.1; -; Genomic_DNA.
DR RefSeq; WP_011189040.1; NC_006138.1.
DR AlphaFoldDB; Q6AM97; -.
DR SMR; Q6AM97; -.
DR STRING; 177439.DP1799; -.
DR EnsemblBacteria; CAG36528; CAG36528; DP1799.
DR KEGG; dps:DP1799; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_7; -.
DR OMA; QHLGGAF; -.
DR OrthoDB; 533698at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000602; 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..423
FT /note="Enolase"
FT /id="PRO_0000133879"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 341
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ SEQUENCE 423 AA; 45218 MW; A7D349038A6E2734 CRC64;
MSDIISAVDA MEVLDSRGNP TVRVFVTLDN GTTCAASVPS GASTGENEAI ELRDGDASRY
LGKGVLKAVD NVKNIIAPAV IGKKITHQAA IDNLMIELDG TETKSSLGAN AILGVSMAVA
RAGARSSRLP LYQYLGGPGA RRIPVPAMNI INGGEHADNS VDIQEFMAVP VGAPSFGEGL
RYIAETFHNL KKILKSRGLA TSVGDEGGFA PNLESNEAAM DIIIEAIEAS GYTPGKDIAF
ALDSAASSFS PDLCGSYDLK WSGGGKKDSA DMIAMAQKWI EKYPIVSWED PLAENDWAGF
QKLTAAVGDK IDVVGDDLFV TNTKYIARGI EEKSANSVLI KLNQIGTVTE SIDAVRMCRE
AGWRYFISHR SGETEDTFLA DFAVAMDGGQ LKTGSASRSE RIAKYNRLLE IERELGANAL
YYW
