ALF_SCHMA
ID ALF_SCHMA Reviewed; 363 AA.
AC P53442;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE EC=4.1.2.13;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=9794637; DOI=10.2307/3284627;
RA El-Dabaa E., Mei H., El-Sayed A., Karim A.M., Eldesoky H.M., Fahim F.A.,
RA Loverde P.T., Saber M.A.;
RT "Cloning and characterization of Schistosoma mansoni fructose-1,6-
RT bisphosphate aldolase isoenzyme.";
RL J. Parasitol. 84:954-960(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RA Harrison R.A., Culpepper J.C., Newport G.R., Doenhoff M.J.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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; L38658; AAA57567.1; -; mRNA.
DR EMBL; AF026805; AAB84014.1; -; mRNA.
DR RefSeq; XP_018652294.1; XM_018797232.1.
DR AlphaFoldDB; P53442; -.
DR SMR; P53442; -.
DR STRING; 6183.Smp_042160.2; -.
DR EnsemblMetazoa; Smp_042160.1; Smp_042160.1; Smp_042160.
DR GeneID; 8354313; -.
DR KEGG; smm:Smp_042160.1; -.
DR WBParaSite; Smp_042160.1; Smp_042160.1; Smp_042160.
DR CTD; 8354313; -.
DR eggNOG; KOG1557; Eukaryota.
DR OMA; QKDNAGA; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P53442; -.
DR BRENDA; 4.1.2.13; 5608.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; P53442; differential.
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 2: Evidence at transcript level;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..363
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000216934"
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; 39645 MW; AE16BBC2BD05C0B4 CRC64;
MSRFQPYLTE AQENDLRRIA QAICAPGKGI LAADESTATM GKRLQQIGVE NNEENRRLYR
QLLFSADHKL AENISGVILF EETLHQKSDD GKTLPTLLAE RNIIPGIKVD KGVVPLAGTD
NETTTQGLDD LASRCAEYWR LGCRFAKWRC VLKISSHTPS YLAMLENANV LARYASICQQ
NGLVPIVEPE VLPDGDHDLL TAQRVTEQVL AFVYKALADH HVYLEGTLLK PNMVTAGQAC
KKAYTPQENA LATVRALQRT VPPAVPGITF LSGGQSELDA TKNLNEINKI PGPKPWALTF
SFGRALQASV LATWKGKKEN VHAAQEELLK LAKANGAAAV GKFEGNMGTT LGDKSLFVAN
HAY
