ALF_MAIZE
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 03-AUG-2022, entry version 121.
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.GRMZM2G057823_P01; -.
DR PaxDb; P08440; -.
DR PRIDE; P08440; -.
DR ProMEX; P08440; -.
DR GeneID; 542261; -.
DR KEGG; zma:542261; -.
DR MaizeGDB; 24903; -.
DR eggNOG; KOG1557; Eukaryota.
DR OrthoDB; 799973at2759; -.
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 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; 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
