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Database: UniProt
Entry: Q94IG3_PHYIN
LinkDB: Q94IG3_PHYIN
Original site: Q94IG3_PHYIN 
ID   Q94IG3_PHYIN            Unreviewed;        74 AA.
AC   Q94IG3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
DE   Flags: Fragment;
OS   Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4787 {ECO:0000313|EMBL:BAB63402.1};
RN   [1] {ECO:0000313|EMBL:BAB63402.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DN101 {ECO:0000313|EMBL:BAB63402.1};
RA   Hatsugai N., Ikeda R., Matsuura T., Oikawa T., Hassan A., Furuichi N.;
RT   "Cloning and characterization of a gene encoding a protein elicitor from
RT   Phytophthora infestans causing HR and generation of active oxygen species
RT   in potato.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00002181}.
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|ARBA:ARBA00000441};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00005812}.
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DR   EMBL; AB051573; BAB63402.1; -; mRNA.
DR   AlphaFoldDB; Q94IG3; -.
DR   VEuPathDB; FungiDB:PITG_02786; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   NON_TER         74
FT                   /evidence="ECO:0000313|EMBL:BAB63402.1"
SQ   SEQUENCE   74 AA;  7762 MW;  3E1C6908E38D5D08 CRC64;
     MGLLDIVQPG VLNGEDVVKV YKYAQEHNAI FPAVNVTSSS TVNAALQAAR DIKSPIIIQT
     SNGGAFYAGK GIDN
//
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