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Database: UniProt
Entry: A0A1Y9IVE2_9DIPT
LinkDB: A0A1Y9IVE2_9DIPT
Original site: A0A1Y9IVE2_9DIPT 
ID   A0A1Y9IVE2_9DIPT        Unreviewed;       433 AA.
AC   A0A1Y9IVE2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
OS   Anopheles minimus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN015927-PA, ECO:0000313|Proteomes:UP000075920};
RN   [1] {ECO:0000313|Proteomes:UP000075920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMIN015927-PA}
RP   IDENTIFICATION.
RC   STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN015927-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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   AlphaFoldDB; A0A1Y9IVE2; -.
DR   STRING; 112268.A0A1Y9IVE2; -.
DR   EnsemblMetazoa; AMIN015927-RA; AMIN015927-PA; AMIN015927.
DR   VEuPathDB; VectorBase:AMIN015927; -.
DR   OrthoDB; 1093250at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000075920; 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; SFLDS00001; 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}.
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;  46585 MW;  41BC7EF8D0F903AD CRC64;
     MPFKSIKARQ IFDSRGNPTV EVDLVTDLGL FRAAVPSGAS TGVHEALELR DNEKGNWHGK
     GVLKAVENIN KTIAPAVLGS NLCVTQQKEL DELMLKLDGT ENKSKLGANA ILGVSLAICK
     AGAAKKGVPL YKHIADLAGN ANIILPVPAF NVINGGSHAG NKLAMQEFMI LPTGASSFTE
     AMKIGSEVYH HLKNVIKAKF GLDATAVGDE GGFAPNILEN KEALNLIQDA IAKAGYTGKV
     EIGMDVAASE FHKEGKYDLD FKNPKSDPSA WLTPDALEQM YQGFIKDFPI VSIEDPFDQD
     HWDAWSKITA NTTIQIVGDD LTVTNPKRIA TAVEKKACNC LLLKVNQIGS VTESINAHLL
     AKKNGWGTMV SHRSGETEDT FIADLVVGLS TGQIKTGAPC RSERLAKYNQ ILRIEEELGA
     GAKFAGKSFR HPQ
//
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