ID G2X006_VERDV Unreviewed; 438 AA.
AC G2X006;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=VDAG_03029 {ECO:0000313|EMBL:EGY21589.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21589.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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 -!- SIMILARITY: Belongs to the enolase family.
CC {ECO:0000256|ARBA:ARBA00009604}.
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DR EMBL; DS572699; EGY21589.1; -; Genomic_DNA.
DR RefSeq; XP_009655189.1; XM_009656894.1.
DR AlphaFoldDB; G2X006; -.
DR STRING; 498257.G2X006; -.
DR EnsemblFungi; EGY21589; EGY21589; VDAG_03029.
DR GeneID; 20704492; -.
DR KEGG; vda:VDAG_03029; -.
DR eggNOG; KOG2670; Eukaryota.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; G2X006; -.
DR OMA; RCMMSHR; -.
DR OrthoDB; 1093250at2759; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001611; Chromosome 6.
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; IPR018247; EF_Hand_1_Ca_BS.
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; PS00018; EF_HAND_1; 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:UP000001611}.
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; 47518 MW; 4819FA12DB7AB054 CRC64;
MAIKKIHARY VYDSRGNPTV EVDVLTETGL HRAIVPSGAS TGQHEACELR DGDKAKWAGK
GVLKAVENVN TVIGPALIKE NIDVKDQTKI DEFLIKLDGT PNKNKLGANA ILGVSLAIAK
AATAEKGVPL FAHISDLAGT KKPYVLPVPF MNVLNGGSHA GGRLAFQEFM IVPSAAPSFS
EALRQGAEVY QILKSLAKKK YGQSAGNVGD EGGVAPDIQT ADEALELITD AIEKAGYTGK
MNIAMDVASS EFYKEDAKKY DLDFKNPDSD QSKWLTYEEL ANLYSELCKK YPIVSIEDPF
AEDDWEAWSY FYKAQDIQLV ADDLTVTNPI RIKKAIELKA ANALLLKVNQ IGTLTESIQA
AKDSFADGWG VMVSHRSGET EDVTIADIAV GLRAGQIKTG APARSERLAK LNQILRIEEE
LGDQAIYAGE NFRKSVNL
//
