ID   ENO4_XENLA              Reviewed;         572 AA.
AC   A9UMP7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 48.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2007) 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 belongs to the enolase family, Leu-333 is present
CC       instead of the conserved Glu which is expected to be an active site
CC       residue. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI57742.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC157741; AAI57742.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; A9UMP7; -.
DR   SMR; A9UMP7; -.
DR   PRIDE; A9UMP7; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000186698; Genome assembly.
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   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..572
FT                   /note="Enolase 4"
FT                   /id="PRO_0000348457"
FT   REGION          181..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        468
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         519
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  62419 MW;  7AD4B020613C70C0 CRC64;
     MSYRVTGDAA RKARERYELK QAAAEFYRKR NVPERLEEAL NSTFCLGPED VYGHLANYFA
     QFSMPPTICQ IRGRKVLDGS GEPTVEVEVS CTVKNSDKRI CSSVISAVSE HPKASEGLEQ
     ERNHSADTAI QWLKDLSPLL KGMSPNEQHN IDQLLSDFYQ PKIEEEKARR QMEREASPMA
     IEPVPSPVTS PALGKKKGSG KGKKAVVMEK PIPPKEAPEP VVPGSPAIGA LSLAVAKASS
     VLGKTPLYLH IATLRNEKLP SEFIMPTPMI SVLSCGKSSP GKLNLMKEVL VIPPTGLTVQ
     QSLDMALMLQ NQIVKQINSI SKTGPAIKNV TPLGCMLIGG DRIEQPLDLI CEACQHVGLE
     LGRNLYLAIN CAAHELMDYN KAKYEALSGT FKSPDEMVDL YVDLINRQPA ILALLDPLRK
     EDAAQWESLT KALGSKCFLF ADAASKPVCK LLESADIHNP PCSGTVIKHT NETTVSQLLG
     SFKLIEGENR VTILGCPCEE SVDDSIADLA VGLGARFVKL GGLLRGERSS KYNRLLAIED
     ELTQAGTLGF WTKHEFPILS DVENLPGPEE VE