ID   ALF_MAIZE               Reviewed;         355 AA.
AC   P08440;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Fructose-bisphosphate aldolase, cytoplasmic isozyme;
DE            EC=4.1.2.13;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3172237; DOI=10.1016/0022-2836(88)90556-6;
RA   Dennis E.S., Gerlach W.L., Walker J.C., Lavin M., Peacock W.J.;
RT   "Anaerobically regulated aldolase gene of maize. A chimaeric origin?";
RL   J. Mol. Biol. 202:759-767(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16665137; DOI=10.1104/pp.82.4.1076;
RA   Kelley P.M., Tolan D.R.;
RT   "The complete amino acid sequence for the anaerobically induced aldolase
RT   from maize derived from cDNA clones.";
RL   Plant Physiol. 82:1076-1080(1986).
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; X12872; CAA31366.1; -; Genomic_DNA.
DR   EMBL; M16220; AAA33435.1; -; mRNA.
DR   PIR; S07789; ADZM.
DR   RefSeq; NP_001105336.1; NM_001111866.1.
DR   AlphaFoldDB; P08440; -.
DR   SMR; P08440; -.
DR   STRING; 4577.P08440; -.
DR   PaxDb; 4577-GRMZM2G057823_P01; -.
DR   ProMEX; P08440; -.
DR   GeneID; 542261; -.
DR   KEGG; zma:542261; -.
DR   MaizeGDB; 24903; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   InParanoid; P08440; -.
DR   OrthoDB; 3595068at2759; -.
DR   SABIO-RK; P08440; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P08440; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:AgBase.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0034059; P:response to anoxia; IDA:AgBase.
DR   GO; GO:0005986; P:sucrose biosynthetic process; TAS:AgBase.
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:SF80; 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..355
FT                   /note="Fructose-bisphosphate aldolase, cytoplasmic isozyme"
FT                   /id="PRO_0000216921"
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   BINDING         52
FT                   /ligand="substrate"
FT   BINDING         142
FT                   /ligand="substrate"
FT   SITE            355
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   355 AA;  38604 MW;  54B480978ECD1470 CRC64;
     MSAYCGKYKD ELIKNAAYIG TPGKGILAAD ESTGTIGKRL SSINVENVEE NRRALRELLF
     CCPGALQYIS GVILFEETLY QKTKDGKPFV DVLKEGGVLP GIKVDKGTIE VVGTDKETTT
     QGHDDLGKRC AKYYEAGARF AKWRAVLKIG PNEPSQLAID LNAQGLARYA IICQENGLVP
     IVEPEILVDG PHDIDRCAYV TETVLAACYK ALNEHHVLLE GTLLKPNMVT PGSDSKKVTP
     EVIAEYTVRT LQRTVPAAVP AVLFLSGGQS EEEATRNLNA MNKLSTKKPW SLSFSFGRAL
     QASTLKAWAG KVENLEKARA AFLARCKANS EATLGTYKGD AAADTESLHV KDYKY
//