ID E3RHY1_PYRTT Unreviewed; 295 AA.
AC E3RHY1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 22-FEB-2023, entry version 43.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU366023};
DE Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU366023};
GN ORFNames=PTT_07562 {ECO:0000313|EMBL:EFQ94689.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ94689.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ94689.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000256|RuleBase:RU366023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000256|RuleBase:RU366023};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3,
CC ECO:0000256|RuleBase:RU366023};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3,
CC ECO:0000256|RuleBase:RU366023};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|RuleBase:RU366023}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|RuleBase:RU366023}.
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DR EMBL; GL533178; EFQ94689.1; -; Genomic_DNA.
DR RefSeq; XP_003297236.1; XM_003297188.1.
DR AlphaFoldDB; E3RHY1; -.
DR STRING; 861557.E3RHY1; -.
DR EnsemblFungi; EFQ94689; EFQ94689; PTT_07562.
DR KEGG; pte:PTT_07562; -.
DR eggNOG; KOG4153; Eukaryota.
DR HOGENOM; CLU_040088_4_0_1; -.
DR OrthoDB; 1763470at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|RuleBase:RU366023};
KW Lyase {ECO:0000256|RuleBase:RU366023};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW ECO:0000256|RuleBase:RU366023};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU366023}.
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
SQ SEQUENCE 295 AA; 32022 MW; ABA35376AC1B1FED CRC64;
MAPDLSQNKA VKLVAHAAAN KYAICATCCY NVEGILASVR AAEAKRAPLI IQLFPWAITY
ANGVLLHAAR EAADNASVPV ALHMDHAQTP EMVKRAADFE HGFDGIMVDM SHFDDNLAKT
AELVRYCNER GIITEAEPGR IDGGEDGVGD LSEMGLEAIL TTPEQAEEFV ATGINWLAPA
FGNVHGKYGP KGPQLDYPRL KNVHAKVGDR VALVLHGAGK EWFQEKLLKE CIECGVAKVN
INDAFNNDFL DVMHKHADKT PLTGLIEKAT DAMQKSIEDY IVWMGGAGMA DKIQL
//
