ENO4_XENTR
ID ENO4_XENTR Reviewed; 574 AA.
AC B0BM20;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2008) 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-332 is present
CC instead of the conserved Glu which is expected to be an active site
CC residue. {ECO:0000305}.
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DR EMBL; BC158253; AAI58254.1; -; mRNA.
DR RefSeq; NP_001119992.1; NM_001126520.1.
DR AlphaFoldDB; B0BM20; -.
DR SMR; B0BM20; -.
DR STRING; 8364.ENSXETP00000031321; -.
DR GeneID; 100144948; -.
DR KEGG; xtr:100144948; -.
DR CTD; 387712; -.
DR Xenbase; XB-GENE-1009720; eno4.
DR eggNOG; KOG2670; Eukaryota.
DR InParanoid; B0BM20; -.
DR OrthoDB; 1097401at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; 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..574
FT /note="Enolase 4"
FT /id="PRO_0000348458"
FT REGION 165..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 62651 MW; 67D536E7B27C74C2 CRC64;
MSYRAGDAAR RARERYELKQ AAAEFYRKLS VTERLEEALN STFCLGPEDV YGHLANYFAQ
FSKPPTICQI RGRKVLDGTG EPTVEAEVFC TVKNMDKRIC SSVISAASEH PKASKGPEQE
SNHSADIAIQ WLNDLSPKLR GMSPDEQNKI DQLLSDFYQP KIEEEKERRQ MEREASPMPL
QPEPSPVTSP APGKKKGSGK GKKAAVVEKP IPPEETPEAV VPGSPAIGAL SLAVAKASSV
LSKTPLYLHI RALRNEKLPT EFFMPTPMIS ILSCGTSSPG KLNLMKEVLI IPQTGLTVQQ
SLDMALMLQN QIVKQINAAS KTGPAIKNVS PLGCMLIGGD RIEQPLDLIC EACQHVGLEL
GTNLYLAINC AAHELMDYNK GKYEVLSGTF KSPDEMIDLY VDLINRQPAI LALLDPLRKE
DTVQWESLAK ALGSKCYLFA DAASKPVCKL LESGSMNSPP CSGTVIKHTN EITISQLLGV
FKLIEGENRV AVLGCPYKES VGDSTADLAV GLGARFVKLG GLLRGERTTK YNRLLAIEDE
LTQAGALGFW TKNEFPVLCE VQNQPGPQET PETQ