ENO_CHLAA
ID ENO_CHLAA Reviewed; 426 AA.
AC A9WCM4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Caur_3808;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY36986.1; -; Genomic_DNA.
DR RefSeq; WP_012259639.1; NC_010175.1.
DR RefSeq; YP_001637375.1; NC_010175.1.
DR PDB; 4YWS; X-ray; 2.45 A; A/B=1-426.
DR PDB; 4Z17; X-ray; 2.65 A; A/B=1-426.
DR PDB; 4Z1Y; X-ray; 2.53 A; A/B=1-426.
DR PDBsum; 4YWS; -.
DR PDBsum; 4Z17; -.
DR PDBsum; 4Z1Y; -.
DR AlphaFoldDB; A9WCM4; -.
DR SMR; A9WCM4; -.
DR STRING; 324602.Caur_3808; -.
DR PRIDE; A9WCM4; -.
DR EnsemblBacteria; ABY36986; ABY36986; Caur_3808.
DR KEGG; cau:Caur_3808; -.
DR PATRIC; fig|324602.8.peg.4274; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_0; -.
DR InParanoid; A9WCM4; -.
DR OMA; EFMIIPV; -.
DR BRENDA; 4.2.1.11; 1352.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000002008; 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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..426
FT /note="Enolase"
FT /id="PRO_1000079126"
FT ACT_SITE 206
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 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 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"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4Z17"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4Z1Y"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 176..195
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4Z1Y"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:4Z1Y"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4Z17"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 314..318
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:4YWS"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:4Z1Y"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:4YWS"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:4YWS"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:4YWS"
SQ SEQUENCE 426 AA; 45897 MW; 1EAF451AA599E19D CRC64;
MSTLIEAIVA REVLDSRGNP TIEVDVRLES GDVGRAIVPS GASTGAHEAL ELRDGDKSRY
NGKGVLKAVQ AVNEDIAEAL IGFDAADQIA LDQELIALDG TPNKSKLGAN AILGVSLAAA
KAAAAAFGLP LYRYLGGVYA HVLPVPMMNI MNGGQHATNS TDFQEFMIMP VGAESFREGL
RWGAEIYHML KKVIHDRGFS TTVGDEGGFA PSLPTNDAPL QLIMEAIEKA GYRPGEQIVI
ALDPATTEIF EDGKYHLKRE GRSLSSAEMV DYWVDLVNRY PIISLEDGLA EDDWEGWALL
RAKLGDRVQL VGDDFLVTNV QRLQRAIEAK AANSILIKLN QIGSLTETLS AIQLAQRSGW
TAVVSHRSGE SEDVTIADLV VATNAGQIKT GAPARTDRIA KYNQLLRIEE ELGSAARYAG
RSAFKV
