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Database: UniProt
Entry: A0A2B7Y3R1_9EURO
LinkDB: A0A2B7Y3R1_9EURO
Original site: A0A2B7Y3R1_9EURO 
ID   A0A2B7Y3R1_9EURO        Unreviewed;       438 AA.
AC   A0A2B7Y3R1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Enolase {ECO:0000256|ARBA:ARBA00017068};
DE            EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058};
DE   AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|ARBA:ARBA00032132};
GN   ORFNames=AJ80_05411 {ECO:0000313|EMBL:PGH15880.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH15880.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH15880.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH15880.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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:0000256|ARBA:ARBA00000767};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGH15880.1}.
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DR   EMBL; PDNA01000079; PGH15880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7Y3R1; -.
DR   STRING; 1447883.A0A2B7Y3R1; -.
DR   OrthoDB; 1093250at2759; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000224634; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224634}.
FT   DOMAIN          3..134
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          143..435
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         374..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   438 AA;  47404 MW;  3B663CA9E91E258F CRC64;
     MAITKIHARS VYDSRGNPTV EVDVVTETGL HRAIVPSGAS TGLHEACELR DGDKDKWLGK
     GVLKAVKNVN DVIGPAIIKE NVDVKDQSKV DEFLNKLDGT ANKSNLGANA ILGVSLAIAK
     AGAAEKGVPL YAHVSDLAGT KKPYVLPVPF QNVLNGGSHA GGRMAFQEFM IVPDTAPSFS
     EALRQGAEVY HKLKSLAKKK YGQSAGNVGD EGGVAPDIQT PEEALDLITD AIEQAGYTGK
     IKIALDVASS EFYKAEEKKY DLDFKNPESD KSKWLTYEQL SDLYKSLAAK YPIVSIEDPF
     AEDDWEAWSY FFKTSDFQIV GDDLTVTNPI RIKKAIELKS CNALLLKVNQ IGTLTESIQA
     AKDSYAAGWG VMVSHRSGET EDVTIADIVV GLRSGQIKTG APARSERLAK LNQILRIEEE
     LGDNAVYAGE KFRDAVNI
//
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