ID A0A2Y9L2U6_ENHLU Unreviewed; 440 AA.
AC A0A2Y9L2U6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-enolase {ECO:0000256|ARBA:ARBA00040232};
DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125};
DE AltName: Full=Enolase 3 {ECO:0000256|ARBA:ARBA00041942};
DE AltName: Full=Muscle-specific enolase {ECO:0000256|ARBA:ARBA00042698};
DE AltName: Full=Skeletal muscle enolase {ECO:0000256|ARBA:ARBA00042657};
GN Name=LOC111161065 {ECO:0000313|RefSeq:XP_022380236.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022380236.1};
RN [1] {ECO:0000313|RefSeq:XP_022380236.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022380236.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate. Appears to have a function in
CC striated muscle development and regeneration.
CC {ECO:0000256|ARBA:ARBA00037209}.
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 Evidence={ECO:0000256|ARBA:ARBA00036172};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165;
CC Evidence={ECO:0000256|ARBA:ARBA00036172};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}.
CC -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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DR RefSeq; XP_022380236.1; XM_022524528.1.
DR AlphaFoldDB; A0A2Y9L2U6; -.
DR STRING; 391180.A0A2Y9L2U6; -.
DR KEGG; elk:111161065; -.
DR OrthoDB; 1093250at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000248482; Unplaced.
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; Enolase-like C-terminal domain; 1.
DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 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 NCBIfam; TIGR01060; eno; 1.
DR PANTHER; PTHR11902:SF5; BETA-ENOLASE; 1.
DR PANTHER; PTHR11902; ENOLASE; 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 SFLD; SFLDS00001; Enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482}.
FT DOMAIN 9..140
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 148..437
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 216
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 376..379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 440 AA; 47783 MW; D8ABFB3FEC3FE821 CRC64;
MRTLRAMAMQ KIFAREILDS RGNPTVEVDL HTAKGRFRAA VPSGASTGIY EALELRDGDK
SRYLGKGVLK AVEHINKTLG PALLEKKLSV VDQEKVDKFM IELDGTENKS KFGANAILGV
SLAVCKAGAA EKGVPLYRHI ADLAGNPDLV LPVPAFNVIN GGSHAGNKLA MQEFMILPVG
ASSFKEAMRI GAEVYHHLKG VIKAKYGKDA TNVGDEGGFA PNILENNEAL ELLKTAIQAA
GYPDKVVIGM DVAASEFYRN GKYDLDFKSP DDPARHITGE KLGELYKNFI KNYPVVSIED
PFDQDDWATW TSFLSGVNIQ IVGDDLTVTN PKRIAQAVEK KACNCLLLKV NQIGSVTESI
QACKLAQSNG WGVMVSHRSG ETEDTFIADL VVGLCTGQIK TGAPCRSERL AKYNQLMRIE
EALGDKAVFA GRKFRNPKAK
//
