ENO_SCHMA
ID ENO_SCHMA Reviewed; 434 AA.
AC Q27877;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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;
GN Name=ENO;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=7665603; DOI=10.1074/jbc.270.37.21813;
RA Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.;
RT "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes
RT in the human parasite, Schistosoma mansoni.";
RL J. Biol. Chem. 270:21813-21819(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; Evidence={ECO:0000250};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR EMBL; U33177; AAC46884.1; -; Genomic_DNA.
DR EMBL; U30177; AAC46884.1; JOINED; Genomic_DNA.
DR EMBL; U30175; AAC46886.1; -; mRNA.
DR AlphaFoldDB; Q27877; -.
DR SMR; Q27877; -.
DR STRING; 6183.Smp_024110.1; -.
DR EnsemblMetazoa; Smp_024110.1; Smp_024110.1; Smp_024110.
DR WBParaSite; Smp_024110.1; Smp_024110.1; Smp_024110.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; Q27877; baseline and differential.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..434
FT /note="Enolase"
FT /id="PRO_0000134084"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 371..374
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 46995 MW; 5318C52F7EDFE5EE CRC64;
MSILTIHARQ IFDSRGNPTV EVDLKTSKGL FRAAVPSGAS TGVHEALELR DTNSKAYMKK
GVLTAVSNVN KIIAPALINK NIPVTNQAAI DKYMIDLDGT ENKEKLGANA ILGVSLAVCK
AGAAEAGLPL YRYIARLAGH EDVIMPVPAF NVINGGSHAG NKLAMQEFMI LPTGASSFTE
AMQIGTEVYH NLKAVIKREY GLDACNVGDE GGFAPNIQDN MKGLQLLEEA IKIAGYTGKV
EIGMDCAASE FHKNGKYDLD FKNPHSAEST WLSPDAMANM YKQMISKFPI VSIEDPFDQD
DWETWPKLTS STNIQIVGDD LTVTNPKRIK QAIASKACNC LLLKVNQIGS LTESIEACKL
AQDSGWGVMV SHRSGETEDT FIADLVVGLC TGQIKTGAPC RSDRLAKYNQ LLRIEEELGT
AAKYAGKNFR HPKV
