ID   ALF_ANASL               Reviewed;          16 AA.
AC   P83155;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE   Flags: Fragment;
OS   Anabaena sp. (strain L31).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC   unclassified Anabaena.
OX   NCBI_TaxID=29412;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Apte S.K., Uhlemann E., Schmid R., Altendorf K.;
RL   Submitted (OCT-2001) to UniProtKB.
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:0000250}.
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:0000250|UniProtKB:P29271};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC       provides a structural contribution. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29271}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P83155; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..>16
FT                   /note="Fructose-bisphosphate aldolase"
FT                   /id="PRO_0000262929"
FT   NON_TER         16
SQ   SEQUENCE   16 AA;  1702 MW;  5D2670D9E4833A8B CRC64;
     ALVPLRLLLD HAAENG