ENO_HOMGA
ID ENO_HOMGA Reviewed; 433 AA.
AC P56252;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
OS Homarus gammarus (European lobster) (Homarus vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Nephropoidea; Nephropidae; Homarus.
OX NCBI_TaxID=6707;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP SUBSTRATE ANALOG AND MAGNESIUM IONS, AND ACETYLATION AT SER-1.
RC TISSUE=Muscle;
RX PubMed=7547999; DOI=10.1021/bi00039a005;
RA Duquerroy S., Camus C., Janin J.;
RT "X-ray structure and catalytic mechanism of lobster enolase.";
RL Biochemistry 34:12513-12523(1995).
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7547999}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR PDB; 1PDY; X-ray; 2.40 A; A=1-433.
DR PDB; 1PDZ; X-ray; 2.20 A; A=1-433.
DR PDBsum; 1PDY; -.
DR PDBsum; 1PDZ; -.
DR AlphaFoldDB; P56252; -.
DR SMR; P56252; -.
DR iPTMnet; P56252; -.
DR UniPathway; UPA00109; UER00187.
DR EvolutionaryTrace; P56252; -.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; Acetylation; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..433
FT /note="Enolase"
FT /id="PRO_0000134085"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT BINDING 157
FT /ligand="substrate"
FT BINDING 166
FT /ligand="substrate"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 294
FT /ligand="substrate"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 319
FT /ligand="substrate"
FT BINDING 344
FT /ligand="substrate"
FT BINDING 371..374
FT /ligand="substrate"
FT BINDING 374
FT /ligand="substrate"
FT BINDING 395
FT /ligand="substrate"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:7547999"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1PDZ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 177..199
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1PDZ"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1PDY"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:1PDZ"
FT TURN 320..324
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:1PDZ"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 402..418
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:1PDZ"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:1PDZ"
SQ SEQUENCE 433 AA; 47042 MW; CC7DA44B67E9DE3D CRC64;
SITKVFARTI FDSRGNPTVE VDLYTSKGLF RAAVPSGAST GVHEALEMRD GDKSKYHGKS
VFNAVKNVND VIVPEIIKSG LKVTQQKECD EFMCKLDGTE NKSSLGANAI LGVSLAICKA
GAAELGIPLY RHIANLANYD EVILPVPAFN VINGGSHAGN KLAMQEFMIL PTGATSFTEA
MRMGTEVYHH LKAVIKARFG LDATAVGDEG GFAPNILNNK DALDLIQEAI KKAGYTGKIE
IGMDVAASEF YKQNNIYDLD FKTANNDGSQ KISGDQLRDM YMEFCKDFPI VSIEDPFDQD
DWETWSKMTS GTTIQIVGDD LTVTNPKRIT TAVEKKACKC LLLKVNQIGS VTESIDAHLL
AKKNGWGTMV SHRSGETEDC FIADLVVGLC TGQIKTGAPC RSERLAKYNQ ILRIEEELGS
GAKFAGKNFR APS
