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P14223

- ALF_PLAFA

UniProt

P14223 - ALF_PLAFA

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Protein

Fructose-bisphosphate aldolase

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Substrate
Binding sitei152 – 1521Substrate
Active sitei195 – 1951Proton acceptorBy similarity
Active sitei237 – 2371Schiff-base intermediate with dihydroxyacetone-P
Sitei369 – 3691Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Alternative name(s):
41 kDa antigen
OrganismiPlasmodium falciparum
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Fructose-bisphosphate aldolasePRO_0000216930Add
BLAST

Proteomic databases

PRIDEiP14223.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-60915N.

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2914
Beta strandi35 – 395
Helixi43 – 5210
Helixi59 – 7012
Turni76 – 783
Beta strandi79 – 846
Helixi86 – 894
Helixi99 – 1068
Beta strandi109 – 1135
Beta strandi118 – 1203
Beta strandi124 – 1263
Beta strandi128 – 1303
Turni133 – 1353
Helixi136 – 14611
Beta strandi150 – 1578
Helixi161 – 1633
Helixi168 – 18720
Beta strandi191 – 1988
Helixi206 – 22621
Helixi231 – 2333
Helixi253 – 26715
Beta strandi274 – 2774
Helixi284 – 29613
Beta strandi301 – 3099
Helixi310 – 3189
Turni319 – 3224
Turni324 – 3263
Helixi327 – 34620

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5CX-ray3.00A/B2-369[»]
2EPHX-ray2.70A/B/C/D1-369[»]
2PC4X-ray2.40A/B/C/D1-369[»]
ProteinModelPortaliP14223.
SMRiP14223. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14223.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14223-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF
60 70 80 90 100
DNIKLENTIE NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV
110 120 130 140 150
NLLHNENIIP GIKVDKGLVN IPCTDEEKST QGLDGLAERC KEYYKAGARF
160 170 180 190 200
AKWRTVLVID TAKGKPTDLS IHETAWGLAR YASICQQNRL VPIVEPEILA
210 220 230 240 250
DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM VTAGYECTAK
260 270 280 290 300
TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH
310 320 330 340 350
PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK
360
GGAGGENAGA SLYEKKYVY
Length:369
Mass (Da):40,105
Last modified:January 1, 1990 - v1
Checksum:i2AE9CDED4F5C96A4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28881 Genomic DNA. Translation: AAA29473.1.
A13461 Unassigned DNA. Translation: CAA01107.1.
A13481 Unassigned DNA. Translation: CAA01117.1.
PIRiA44942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28881 Genomic DNA. Translation: AAA29473.1 .
A13461 Unassigned DNA. Translation: CAA01107.1 .
A13481 Unassigned DNA. Translation: CAA01117.1 .
PIRi A44942.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P14223.
SMRi P14223. Positions 4-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60915N.

Proteomic databases

PRIDEi P14223.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3588.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .

Miscellaneous databases

EvolutionaryTracei P14223.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view ]
PANTHERi PTHR11627. PTHR11627. 1 hit.
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiALF_PLAFA
AccessioniPrimary (citable) accession number: P14223
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3