ID   ALF2_PEA                Reviewed;         359 AA.
AC   P46257;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Fructose-bisphosphate aldolase, cytoplasmic isozyme 2;
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 [GENOMIC DNA].
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; X89829; CAA61947.1; -; Genomic_DNA.
DR   PIR; S58167; S58167.
DR   AlphaFoldDB; P46257; -.
DR   SMR; P46257; -.
DR   PRIDE; P46257; -.
DR   SABIO-RK; P46257; -.
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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..359
FT                   /note="Fructose-bisphosphate aldolase, cytoplasmic isozyme
FT                   2"
FT                   /id="PRO_0000216924"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            359
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  38491 MW;  C0CAB16E9CC1B9EF CRC64;
     MSHFKSKYHD ELIANAAYIG TPGKGILAAD ESTGTIGKRL SSINVENVES NRQALRELLF
     TASWLFLQYL SGVILFEETL YQKTAAGKPF VDVLNEAGVL PGIKVDKGTV ELAGTDGETT
     TQGLDGLGAR CRKYYEAGAR FAKWRAVLKI GANEPSEHSI HENAYGLARY AVICQENGLV
     PIVEPEILVD GSHDILKCAA ITERVLAATY KALSDHHVIL EGTLLKPNMV TPGSDAPKVA
     PEVIAEHTVR ALQRTVPAAV PAVVFLSGGQ SEEEASVNLN AINQIKGKKP WTLSFSFGRA
     LQQSTLKAWG GKTENVKAAQ DALLTRAKAN SEATLGTYKG ASNLGAGASE SLHVKDYKY