ID   ALF_ECHMU               Reviewed;         363 AA.
AC   Q9GP32;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   13-SEP-2023, entry version 73.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            EC=4.1.2.13;
GN   Name=FBPA;
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=H-95;
RX   PubMed=10973970; DOI=10.1074/jbc.m006091200;
RA   Brehm K., Jensen K., Frosch M.;
RT   "mRNA trans-splicing in the human parasitic cestode Echinococcus
RT   multilocularis.";
RL   J. Biol. Chem. 275:38311-38318(2000).
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; AJ292376; CAC18550.1; -; mRNA.
DR   AlphaFoldDB; Q9GP32; -.
DR   SMR; Q9GP32; -.
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   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   Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..363
FT                   /note="Fructose-bisphosphate aldolase"
FT                   /id="PRO_0000216933"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        230
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            363
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   363 AA;  39727 MW;  37862DEC55BA2B70 CRC64;
     MSRFVPYLCA EKMKELRENA SAIVAPGKGL LAADESTNTI GKRFAAINLE NTEENRRAYR
     ELLFTTDPEF AKHISGVILF HETVYQKTKD GKPFVELLRE RGVLPGIKVD LGVVPLGGTA
     DECTTQGLDN LAQRCAQYYN DGCRFAKWRC VLKISSHNPS YLAMLENANV LARYAFICQQ
     NGLVPIVEPE VLPDGDHDLE TAQRVTEQVL SFVYKALADH HVYLEGTLLK PNMVTCGQSC
     TKKYSVEDNA RATVEALQRT VPVAVPGVVF LSGGQSELDA TRNLNAINKY PGKKPWALSF
     SFGRALQASA IAAWQGKPEN VKAGQAEFLQ LAKANGAASL GKFEGELKTA AGQKSLFVAN
     HAY
//