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Database: UniProt
Entry: A0A0R3VXB0_TAEAS
LinkDB: A0A0R3VXB0_TAEAS
Original site: A0A0R3VXB0_TAEAS 
ID   A0A0R3VXB0_TAEAS        Unreviewed;       433 AA.
AC   A0A0R3VXB0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Enolase {ECO:0000256|ARBA:ARBA00017068};
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=2-phosphoglycerate dehydratase {ECO:0000256|ARBA:ARBA00032132};
GN   ORFNames=TASK_LOCUS2055 {ECO:0000313|EMBL:VDK24227.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000205401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000205401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK24227.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; UYRS01000922; VDK24227.1; -; Genomic_DNA.
DR   STRING; 60517.A0A0R3VXB0; -.
DR   WBParaSite; TASK_0000205401-mRNA-1; TASK_0000205401-mRNA-1; TASK_0000205401.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; Unassembled WGS sequence.
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; ENOLASE; 1.
DR   PANTHER; PTHR11902:SF1; 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; SFLDG00178; 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:UP000282613}.
FT   DOMAIN          3..134
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          142..432
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         371..374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   433 AA;  46528 MW;  D312FB12965F0D90 CRC64;
     MSIQKIHARQ IFDSRGNPTV EVDLTTAKGM FRAAVPSGAS TGVHEAVELR DGDKNAYMGK
     GVLNAVKNVN EVIAPALLKE KFIVTDQEKI DEFMIKLDGS PNKGKLGANA ILGVSLAVCK
     AGAAEKGVPL YRHIADLAGN KDVVLPVPSF NVLNGGSHAG NKLAMQEFMI LPTGAKNFTE
     AMKMGTEVYH HLKSVIKGKY GLDACNVGDE GGFAPNIQDN MEGLELLKTA IDRAGYTGKV
     KIGMDVAASE FYQNGKYNLD FKNPAAAASS IVPGSKLAEI YLEMLSKYPI VSIEDPFDQD
     DWAAWTAFNA KAGIQIVGDD LTVTNPERVQ QAIDKKACNA LLLKVNQIGS VTESIKACKM
     SRAAGWGVMV SHRSGETEDS TIADIVVGLR TGQIKTGAPC RSERLAKYNQ LLRIEEELGS
     KAVYAGEHFR NPL
//
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