ENO_METJA
ID ENO_METJA Reviewed; 423 AA.
AC Q60173;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=MJ0232;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98220.1; ALT_INIT; Genomic_DNA.
DR PIR; A64329; A64329.
DR RefSeq; WP_064496902.1; NC_000909.1.
DR PDB; 2PA6; X-ray; 1.85 A; A/B=1-423.
DR PDBsum; 2PA6; -.
DR AlphaFoldDB; Q60173; -.
DR SMR; Q60173; -.
DR STRING; 243232.MJ_0232; -.
DR PRIDE; Q60173; -.
DR EnsemblBacteria; AAB98220; AAB98220; MJ_0232.
DR GeneID; 1451085; -.
DR KEGG; mja:MJ_0232; -.
DR eggNOG; arCOG01169; Archaea.
DR HOGENOM; CLU_031223_2_1_2; -.
DR InParanoid; Q60173; -.
DR OMA; EFMIIPV; -.
DR OrthoDB; 23221at2157; -.
DR PhylomeDB; Q60173; -.
DR UniPathway; UPA00109; UER00187.
DR EvolutionaryTrace; Q60173; -.
DR Proteomes; UP000000805; 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..423
FT /note="Enolase"
FT /id="PRO_0000134024"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 244
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 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 335
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 362..365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 6..16
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:2PA6"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2PA6"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 177..199
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:2PA6"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:2PA6"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:2PA6"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:2PA6"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2PA6"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:2PA6"
SQ SEQUENCE 423 AA; 46298 MW; 9C9BB163E64BF577 CRC64;
MDERFEIKDI VAREVIDSRG NPTVEVEVIT KGNGYGSAIV PSGASTGTHE ALELRDKEKR
FGGKGVLMAV ENVNSIIRPE ILGYDARMQR EIDTIMIELD GTPNKSRLGA NAILAVSLAV
AKAAAATAKI PLYKYLGGFN SYVMPVPMMN VINGGKHAGN DLDLQEFMIM PVGATSISEA
VRMGSEVYHV LKNVILEKYG KNAVNVGDEG GFAPPLKTSR EALDLLTESV KKAGYEDEVV
FALDAAASEF YKDGYYYVEG KKLTREELLD YYKALVDEYP IVSIEDPFHE EDFEGFAMIT
KELDIQIVGD DLFVTNVERL RKGIEMKAAN ALLLKVNQIG TLSEAVDAAQ LAFRNGYGVV
VSHRSGETED TTIADLSVAL NSGQIKTGAP ARGERTAKYN QLIRIEQELG LSKYAGRNFR
CPF
