ID   ENO4_DANRE              Reviewed;         576 AA.
AC   Q08BC6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Enolase 4;
DE            EC=4.2.1.11 {ECO:0000250|UniProtKB:Q8C042};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=eno4; ORFNames=zgc:153973;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q8C042};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000250|UniProtKB:Q8C042}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC   -!- CAUTION: Although it is highly related to enolase enzyme family, lacks
CC       the conserved Glu active site. {ECO:0000305}.
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DR   EMBL; BC124782; AAI24783.1; -; mRNA.
DR   RefSeq; NP_001071015.1; NM_001077547.1.
DR   AlphaFoldDB; Q08BC6; -.
DR   SMR; Q08BC6; -.
DR   STRING; 7955.ENSDARP00000094621; -.
DR   PaxDb; Q08BC6; -.
DR   GeneID; 558487; -.
DR   KEGG; dre:558487; -.
DR   CTD; 387712; -.
DR   ZFIN; ZDB-GENE-061013-677; eno4.
DR   eggNOG; KOG2670; Eukaryota.
DR   InParanoid; Q08BC6; -.
DR   OrthoDB; 1097401at2759; -.
DR   PhylomeDB; Q08BC6; -.
DR   UniPathway; UPA00109; UER00187.
DR   PRO; PR:Q08BC6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 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; IPR020811; Enolase_N.
DR   PANTHER; PTHR11902; PTHR11902; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Lyase; Reference proteome.
FT   CHAIN           1..576
FT                   /note="Enolase 4"
FT                   /id="PRO_0000348456"
FT   REGION          187..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         524
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   576 AA;  62768 MW;  B3FDEAA48C6F1612 CRC64;
     MSYKGFPSHS KVSKEDQEFY DLKNKAAEYY RSNGVPQKIE SVLNEMFWQK PDDIYGYLAN
     YFSGLSYTPV ISKITGKEVF DGRGLTAVQA EVHCIIRNEE KMVCGAVMDG SFDGLPDGVE
     SGEMLSNGDL QHLSITMALK WIRENFSPVL RGFNPTDQTN VDKILSDFAM ARYLEHKDSL
     IREKEEELRN EAMSEAPPQA TPTSAPAKDK KGNDKGKKGN ITENPLPPAE PPVPRLPGAT
     AVGAVSLAVA KTAAELLGTP LYRHITAVRD PQAQKEMQLP VPIITIMSCG KNSAGKLNLL
     EEIILMPSSS LRVREVIGMG LDLQCEMRRI LNGSTYKALP VGVSDEGALQ VGFDRPEQAL
     DLLAEACANL ALPLGSDLHL AVNCAAHSLM DYSRGKYEVM SGCHKSPDEL VDIYEGLINK
     YPAIRSLIDP FRKEDVGQWE RLASVIGQSC CLLADAASNL CPRWREAKPL PPGATKAIIR
     HHSDMTISDL IQSIAEHKET ILAAGSGDAS MVDLAVGSGV SFLKLGGLRG AKRMDKYNRL
     MAIEEEQEGI AGAGEINQPV SFESESGWNS LTVSAK