ID   ALF2_PLABA              Reviewed;         358 AA.
AC   P49577;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Fructose-bisphosphate aldolase 2;
DE            Short=ALDO-2;
DE            EC=4.1.2.13;
GN   Name=ALDO2;
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8008025; DOI=10.1016/0166-6851(94)90065-5;
RA   Certa U.;
RT   "Regular initiation of translation of Plasmodium berghei aldolase-2 after
RT   pre-mRNA splicing.";
RL   Mol. Biochem. Parasitol. 63:291-297(1994).
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   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; M81793; AAC37203.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P49577; -.
DR   SMR; P49577; -.
DR   STRING; 5821.PBANKA_130860; -.
DR   MoonProt; P49577; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   UniPathway; UPA00109; UER00183.
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   Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..358
FT                   /note="Fructose-bisphosphate aldolase 2"
FT                   /id="PRO_0000216931"
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         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            358
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   358 AA;  38733 MW;  44D82D283FE4C47F CRC64;
     MKLPKEDAQE LAETAKKLVA AGKGILAADE STQTIKKRFD NIKIENTVQN RASYRDLLFG
     TKGLGKFISG AILFEETLFQ KNEAGVPLVN LLHDEGIIPG IKVDKGLVSI PCTDDEKSTQ
     GLDGLAERCK EYYKAGARFA KWRAVLVIDP AKGKPTDLSI QEVSWGLARY ASICQQNKLV
     PIVEPEILAD GAHTIEVCAT VTQKVLASVF KALHDNGVLL EGASLKPNMV TAGYDCTEKT
     KTDDIGFFTV RTLRRTVPPA LPGVAFLSGG QSEEDASINL NSINVLGPHP WALTFSYGRA
     LQASVLNTWQ GKKENVAKAR RVLLQRAEAN SLATYGKYKG GAGGSTAGAS LYEKKYVY