ID   ALF1_PEA                Reviewed;         357 AA.
AC   P46256;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Fructose-bisphosphate aldolase, cytoplasmic isozyme 1;
DE            EC=4.1.2.13;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Pelzer-Reith B., Schnarrenberger C.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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; X89828; CAA61946.1; -; mRNA.
DR   PIR; S58168; S58168.
DR   AlphaFoldDB; P46256; -.
DR   SMR; P46256; -.
DR   PRIDE; P46256; -.
DR   SABIO-RK; P46256; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
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                   1"
FT                   /id="PRO_0000216923"
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         52
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;  38446 MW;  BB30E70BA0401D61 CRC64;
     MSAFVGKYAD ELIKNAKYIA TPGKGILAAD ESTGTIGKRL ASINVENIEA NRQALRELLF
     TSPNALQYLS GVILFEETLY QKSSEGKPFV EILQENNVIP GIKVDKGVVE LAGTDGETTT
     QGFDSLGARC QQYYKAGARF AKWRAVLKIG PNEPSELSIQ QNAQGLARYA IICQENGLVL
     FVEPEILTDG SHDIAKCAAV TETVLAACYK ALNDQHVLLE GTLLKPNMVT PGSDSPKVSP
     EVIGEYTVNA LRRTVPAAVP GIVFLSGGQS EEQATLNLNA MNKFDVVKPW TLSFSFGRAL
     QQSTLKTWSG KKENVGKAQD VFLARCKANS EATLGKYGGG SGTGLASESL HVKDYKY