[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0166-6851(89)90101-1; PubMed=2693962 [NCBI, ExPASy, EBI, Israel, Japan] Knapp B., Hundt E., Kuepper H.A.; "A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface."; Mol. Biochem. Parasitol. 37:47-56(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0166-6851(90)90074-V; PubMed=2190085 [NCBI, ExPASy, EBI, Israel, Japan] Knapp B., Hundt E., Kuepper H.A.; "Plasmodium falciparum aldolase: gene structure and localization."; Mol. Biochem. Parasitol. 40:1-12(1990).
[3]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1021/bi972233h; PubMed=9521758 [NCBI, ExPASy, EBI, Israel, Japan] Kim H., Certa U., Dobeli H., Jakob P., Hol W.G.J.; "Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum."; Biochemistry 37:4388-4396(1998).

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: Homotetramer.
SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M28881; AAA29473.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A13461; CAA01107.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A13481; CAA01117.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A44942; A44942.

3D structure databases

PDB

1A5C; X-ray; 3.00 A; A/B=2-369.	[ExPASy / RCSB / EBI]
2EPH; X-ray; 2.70 A; A/B/C/D=1-369.	[ExPASy / RCSB / EBI]
2PC4; X-ray; 2.40 A; A/B/C/D=1-369.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1A5C; -.
2EPH; -.
2PC4; -.

ModBase

P14223.

Ontologies

GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Other

P14223; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Glycolysis; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 369`	`369`	`Fructose-bisphosphate aldolase.`	`PRO_0000216930`
`ACT_SITE`	`195 195`		`Proton acceptor (By similarity).`
`ACT_SITE`	`237 237`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`62 62`		`Substrate.`
`BINDING`	`152 152`		`Substrate.`
`SITE`	`369 369`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`HELIX`	`16 29`	`14`
`STRAND`	`35 39`	`5`
`HELIX`	`43 52`	`10`
`HELIX`	`59 70`	`12`
`TURN`	`76 78`	`3`
`STRAND`	`79 84`	`6`
`HELIX`	`86 89`	`4`
`HELIX`	`99 106`	`8`
`STRAND`	`109 113`	`5`
`STRAND`	`118 120`	`3`
`STRAND`	`124 126`	`3`
`STRAND`	`128 130`	`3`
`HELIX`	`136 146`	`11`
`STRAND`	`150 157`	`8`
`HELIX`	`161 163`	`3`
`HELIX`	`168 187`	`20`
`STRAND`	`191 198`	`8`
`HELIX`	`206 226`	`21`
`HELIX`	`231 233`	`3`
`HELIX`	`253 267`	`15`
`STRAND`	`274 277`	`4`
`HELIX`	`284 296`	`13`
`STRAND`	`301 309`	`9`
`HELIX`	`310 318`	`9`
`TURN`	`319 322`	`4`
`TURN`	`324 326`	`3`
`HELIX`	`327 346`	`20`

Sequence information

Length: 369 AA [This is the length of the unprocessed precursor]

Molecular weight: 40105 Da [This is the MW of the unprocessed precursor]

CRC64: 2AE9CDED4F5C96A4 [This is a checksum on the sequence]

        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

P14223 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools