ENO_CAMJE
ID ENO_CAMJE Reviewed; 414 AA.
AC P42448; Q0P7V7; Q9PM05;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 150.
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=Cj1672c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35768.1; -; Genomic_DNA.
DR PIR; E81264; E81264.
DR RefSeq; WP_002851519.1; NC_002163.1.
DR RefSeq; YP_002345040.1; NC_002163.1.
DR PDB; 3QN3; X-ray; 2.13 A; A/B/C/D=1-414.
DR PDBsum; 3QN3; -.
DR AlphaFoldDB; P42448; -.
DR SMR; P42448; -.
DR IntAct; P42448; 31.
DR STRING; 192222.Cj1672c; -.
DR PaxDb; P42448; -.
DR PRIDE; P42448; -.
DR EnsemblBacteria; CAL35768; CAL35768; Cj1672c.
DR GeneID; 905947; -.
DR KEGG; cje:Cj1672c; -.
DR PATRIC; fig|192222.6.peg.1647; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_7; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..414
FT /note="Enolase"
FT /id="PRO_0000133861"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 332
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 359..362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3QN3"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:3QN3"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:3QN3"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:3QN3"
FT TURN 308..312
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:3QN3"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:3QN3"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:3QN3"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3QN3"
SQ SEQUENCE 414 AA; 44939 MW; 25C132C6B631FF3D CRC64;
MLVIEDVRAY EVLDSRGNPT VKAEVTLSDG SVGAAIVPSG ASTGSKEALE LRDNDERFGG
KGVLKAVANV NETIADEILG LDAFNQTQLD DTLRELDGTN NYSNLGANAT LGVSMATARA
AAAALGMPLY RYLGGANASI LPVPMCNIIN GGAHANNNVD FQEFMIMPFG FTSFKEALRS
VCEIYAILKK ELANSGHSTA LGDEGGFAPN LANNTEPIDL LMTCIKKAGY ENRVKIALDV
ASTEFFKDGK YHMEGKAFSS EALIERYVEL CAKYPICSIE DGLAENDFEG WIKLTEKLGN
KIQLVGDDLF VTNEDILREG IIKKMANAVL IKPNQIGTIT QTMRTVRLAQ RNNYKCVMSH
RSGESEDAFI ADFAVALNTG QIKTGALARG ERTAKYNRLL EIEFESDEYL GEKL
