ID   ALF_SPIOL               Reviewed;         357 AA.
AC   P29356;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Fructose-bisphosphate aldolase, cytoplasmic isozyme;
DE            EC=4.1.2.13;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8425060; DOI=10.1007/bf00019948;
RA   Pelzer-Reith B., Penger A., Schnarrenberger C.;
RT   "Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast
RT   and cytosol enzyme from spinach.";
RL   Plant Mol. Biol. 21:331-340(1993).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; X65742; CAA46649.1; -; mRNA.
DR   PIR; S31091; ADSPAC.
DR   AlphaFoldDB; P29356; -.
DR   SMR; P29356; -.
DR   BioCyc; MetaCyc:MON-12898; -.
DR   SABIO-RK; P29356; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:AgBase.
DR   GO; GO:0043621; F:protein self-association; IDA:AgBase.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; TAS:AgBase.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   PANTHER; PTHR11627; PTHR11627; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..357
FT                   /note="Fructose-bisphosphate aldolase, cytoplasmic isozyme"
FT                   /id="PRO_0000216925"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            357
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  38471 MW;  33150E3D80B1C6DE CRC64;
     MTAYRGKYAD ELIANASYIA TPGKVILAAD ESTGTIGKRF PSINVENVES NRRALRELLF
     TTPGALPYLS GVILFEETLY QKTADGKPFV DAMKDGGVLP GIKVDKGTVE LAGTNGETTT
     QGLDGLAQRC AQYYTAGARF AKWRAVLKIG PTEPSPLAIL ENANGLARYG IICQENGLVP
     IVEPEILVDG THDIDRCAEV SERVLAACYK ALNDHHVLLE GTSLKPNIVT PGSESKKVTP
     EVIAEYTVRT LQRTVPQAVP GVMFLSGGQS EEEATLNLNA MNKLETKKPW TLSFSYGRAL
     QQSTLKAWQG KEENVAKAQE VFLARAKGNS EATLGKYQGG AGGADASESL HVKDYKY