P14223 (ALF_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Fructose-bisphosphate aldolase EC=4.1.2.13 Alternative name(s): 41 kDa antigen
Organism	Plasmodium falciparum
Taxonomic identifier	5833 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
Pathway	Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

Fructose-bisphosphate aldolase

PRO_0000216930

Sites

Active site

195

1

Proton acceptor By similarity

Active site

237

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

62

1

Substrate

Binding site

152

1

Substrate

Site

369

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Secondary structure

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369

Helix Strand Turn

Details...

Helix

16 – 29

14

Beta strand

35 – 39

5

Helix

43 – 52

10

Helix

59 – 70

12

Turn

76 – 78

3

Beta strand

79 – 84

6

Helix

86 – 89

4

Helix

99 – 106

8

Beta strand

109 – 113

5

Beta strand

118 – 120

3

Beta strand

124 – 126

3

Beta strand

128 – 130

3

Turn

133 – 135

3

Helix

136 – 146

11

Beta strand

150 – 157

8

Helix

161 – 163

3

Helix

168 – 187

20

Beta strand

191 – 198

8

Helix

206 – 226

21

Helix

231 – 233

3

Helix

253 – 267

15

Beta strand

274 – 277

4

Helix

284 – 296

13

Beta strand

301 – 309

9

Helix

310 – 318

9

Turn

319 – 322

4

Turn

324 – 326

3

Helix

327 – 346

20

Sequences

	Sequence		Length	Mass (Da)
	P14223 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 2AE9CDED4F5C96A4	FASTA	369	40,105
	10 20 30 40 50 60 MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF DNIKLENTIE 70 80 90 100 110 120 NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV NLLHNENIIP GIKVDKGLVN 130 140 150 160 170 180 IPCTDEEKST QGLDGLAERC KEYYKAGARF AKWRTVLVID TAKGKPTDLS IHETAWGLAR 190 200 210 220 230 240 YASICQQNRL VPIVEPEILA DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM 250 260 270 280 290 300 VTAGYECTAK TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH 310 320 330 340 350 360 PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK GGAGGENAGA SLYEKKYVY

References

[1]	"A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface." Knapp B., Hundt E., Kuepper H.A. Mol. Biochem. Parasitol. 37:47-56(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Plasmodium falciparum aldolase: gene structure and localization." Knapp B., Hundt E., Kuepper H.A. Mol. Biochem. Parasitol. 40:1-12(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum." Kim H., Certa U., Dobeli H., Jakob P., Hol W.G.J. Biochemistry 37:4388-4396(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M28881 Genomic DNA. Translation: AAA29473.1.
A13461 Unassigned DNA. Translation: CAA01107.1.
A13481 Unassigned DNA. Translation: CAA01117.1.

PIR

A44942.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A5C	X-ray	3.00	A/B	2-369	[»]
2EPH	X-ray	2.70	A/B/C/D	1-369	[»]
2PC4	X-ray	2.40	A/B/C/D	1-369	[»]

ProteinModelPortal

P14223.

SMR

P14223. Positions 3-367.

ModBase

Search...

Proteomic databases

PRIDE

P14223.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG3588.

Enzyme and pathway databases

UniPathway

UPA00109; UER00183.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

PANTHER

PTHR11627. PTHR11627. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14223.

Entry information

Entry name

ALF_PLAFA

Accession

Primary (citable) accession number: P14223

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)