ID ALF2_PLABA Reviewed; 369 AA. AC P49577; A0A509APH7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2024, sequence version 2. DT 02-SEP-2026, entry version 94. DE RecName: Full=Fructose-bisphosphate aldolase 2; DE Short=ALDO-2 {ECO:0000303|PubMed:1625704}; DE EC=4.1.2.13 {ECO:0000269|PubMed:1625704}; GN Name=ALDO2; OS Plasmodium berghei (strain Anka). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Vinckeia. OX NCBI_TaxID=5823; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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). RN [2] {ECO:0000312|Proteomes:UP000074855} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855}; RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0; RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B., RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A., RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G., RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M., RA Janse C.J.; RT "A comprehensive evaluation of rodent malaria parasite genomes and gene RT expression."; RL BMC Biol. 12:86-86(2014). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP DEVELOPMENTAL STAGE. RX PubMed=1625704; DOI=10.1016/0166-6851(92)90032-f; RA Meier B., Doebeli H., Certa U.; RT "Stage-specific expression of aldolase isoenzymes in the rodent malaria RT parasite Plasmodium berghei."; RL Mol. Biochem. Parasitol. 52:15-27(1992). CC -!- FUNCTION: Plays a key role in glycolysis by catalyzing the cleavage of CC fructose 1,6-bisphosphate into dihydroxyacetone phosphate and CC glyceraldehyde 3-phosphate. {ECO:0000269|PubMed:1625704}. 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 Evidence={ECO:0000269|PubMed:1625704}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5 mM for fructose-1-phosphate {ECO:0000269|PubMed:1625704}; CC KM=6 uM for fructose-1,6-bisphosphate {ECO:0000269|PubMed:1625704}; CC Note=kcat is 66 min(-1) with fructose-1-phosphate as substrate CC (PubMed:1625704). kcat is 164 min(-1) with fructose-1,6- bisphosphate CC as substrate (PubMed:1625704). {ECO:0000269|PubMed:1625704}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14223}. CC Membrane {ECO:0000250|UniProtKB:P14223}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:P14223}. Host cell membrane CC {ECO:0000250|UniProtKB:Q27744}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q27744}. CC -!- DEVELOPMENTAL STAGE: Expressed in blood stage forms (at protein level). CC {ECO:0000269|PubMed:1625704}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M81793; AAC37203.1; ALT_SEQ; Unassigned_DNA. DR EMBL; LK023128; VUC57468.1; -; Genomic_DNA. DR AlphaFoldDB; P49577; -. DR SMR; P49577; -. DR MoonProt; P49577; -. DR EnsemblProtists; PBANKA_1308600.1; PBANKA_1308600.1-p1; PBANKA_1308600. DR VEuPathDB; PlasmoDB:PBANKA_1308600; -. DR eggNOG; KOG1557; Eukaryota. DR InParanoid; A0A509APH7; -. DR OMA; WRAVITI; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000074855; Chromosome 13. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-ARBA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051289; P:protein homotetramerization; IEA:UniProtKB-ARBA. DR CDD; cd00948; FBP_aldolase_I_a; 1. DR FunFam; 3.20.20.70:FF:000187; Fructose-bisphosphate aldolase; 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 Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 1: Evidence at protein level; KW Cytoplasm; Glycolysis; Host cell membrane; Host membrane; Lyase; Membrane; KW Reference proteome; Schiff base. FT CHAIN 1..369 FT /note="Fructose-bisphosphate aldolase 2" FT /id="PRO_0000216931" FT ACT_SITE 195 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT ACT_SITE 237 FT /note="Schiff-base intermediate with dihydroxyacetone FT phosphate" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 40 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 42 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 45 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 49 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 113 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 152 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 237 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 279..281 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 279 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 280 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 307 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 309 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT BINDING 310 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 310 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q8I8I2" FT SITE 369 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT CONFLICT 18 FT /note="V -> D (in Ref. 1; AAC37203)" FT /evidence="ECO:0000305" FT CONFLICT 60 FT /note="E -> Q (in Ref. 1; AAC37203)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="L -> S (in Ref. 1; AAC37203)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="V -> A (in Ref. 1; AAC37203)" FT /evidence="ECO:0000305" FT CONFLICT 332 FT /note="A -> R (in Ref. 1; AAC37203)" FT /evidence="ECO:0000305" SQ SEQUENCE 369 AA; 39852 MW; 3A92BF2115427EDF CRC64; MVGCAEYKNA PMKLPKEVAQ ELAETAKKLV AAGKGILAAD ESTQTIKKRF DNIKIENTVE NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPLV NLLHDEGIIP GIKVDKGLVS IPCTDDEKST QGLDGLAERC KEYYKAGARF AKWRAVLVID PAKGKPTDLS IQEVSWGLAR YASICQQNKL VPIVEPEILA DGAHTIEVCA TVTQKVLASV FKALHDNGVL LEGALLKPNM VTAGYDCTEK TKTDDIGFFT VRTLRRTVPP ALPGVVFLSG GQSEEDASIN LNSINVLGPH PWALTFSYGR ALQASVLNTW QGKKENVAKA RAVLLQRAEA NSLATYGKYK GGAGGSTAGA SLYEKKYVY //