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1A5C

FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0020002cellular_componenthost cell plasma membrane
A0030388biological_processfructose 1,6-bisphosphate metabolic process
B0003779molecular_functionactin binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0020002cellular_componenthost cell plasma membrane
B0030388biological_processfructose 1,6-bisphosphate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00158
Number of Residues11
DetailsALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. VlLEGaLLKPN
ChainResidueDetails
AVAL228-ASN238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
AGLU194
BGLU194

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
ALYS236
BLYS236

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
AARG61
ALYS151
BARG61
BLYS151

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate => ECO:0000250|UniProtKB:P00883
ChainResidueDetails
ATYR368
BTYR368

220472

PDB entries from 2024-05-29

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