ID   ALF_CICAR               Reviewed;         359 AA.
AC   O65735;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Fructose-bisphosphate aldolase, cytoplasmic isozyme;
DE            EC=4.1.2.13;
GN   Name=ALDC;
OS   Cicer arietinum (Chickpea) (Garbanzo).
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; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Castellana; TISSUE=Etiolated epicotyl;
RA   Dopico B., Munoz F.J., Labrador E.;
RT   "cDNA and deduced amino-acid sequence of a cytosolic aldolase from Cicer
RT   arietinum L. epicotyls.";
RL   (er) Plant Gene Register PGR98-110(1998).
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; AJ005041; CAA06308.1; -; mRNA.
DR   RefSeq; NP_001265896.1; NM_001278967.1.
DR   AlphaFoldDB; O65735; -.
DR   SMR; O65735; -.
DR   STRING; 3827.O65735; -.
DR   PaxDb; 3827-XP_004514022-1; -.
DR   GeneID; 101501462; -.
DR   KEGG; cam:101501462; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   OrthoDB; 3595068at2759; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000087171; Unplaced.
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   CDD; cd00948; FBP_aldolase_I_a; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR029768; Aldolase_I_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   NCBIfam; NF033379; FrucBisAld_I; 1.
DR   PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF83; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..359
FT                   /note="Fructose-bisphosphate aldolase, cytoplasmic isozyme"
FT                   /id="PRO_0000216920"
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   BINDING         52
FT                   /ligand="substrate"
FT   BINDING         142
FT                   /ligand="substrate"
FT   SITE            359
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   359 AA;  38452 MW;  DD68864B745A5195 CRC64;
     MSNFKSKYHD ELIANAAYIG TPGKGILAAD ESTGTIGKRL ASINVENVET NRRALRELLF
     TAPNVLQYLS GVILFEETLY QSTAAGKPFV DVLNEAGVLP GIKVDKGTVE LAGTDGETTT
     QGLDGLGARC AKYYEAGARF AKWRAVLKIG PNEPSLSILS IENAYGLARY AVICQENGLV
     PIVELEILVD GSHDIHKCAA ITERVLAATY KALSDHHVLL EGTLLKPNMV TPGSDSPKVA
     PEVVAEHTVR ALQRTVPAAV PAVVFLSGGQ SEEEATVNLN AINQVKGKKP WTLSFSFGRA
     LQQSTLKAWS GKEENVKNAQ DALLTRAKAN SEATLGTYKG NSQLGEGASE SLHVKDYKY
//