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
//