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Q9URB4 (ALF_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
37 kDa major allergen
Fructose-1,6-bisphosphate aldolase
IgE-binding allergen
Gene names
Name:FBA1
ORF Names:CaO19.12088, CaO19.4618
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Ref.2.

Allergenic properties

Causes an allergic reaction in human. Binds to IgE. Ref.2

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 359358Fructose-bisphosphate aldolase
PRO_0000178757

Regions

Region266 – 2683Dihydroxyacetone phosphate binding By similarity
Region287 – 2904Dihydroxyacetone phosphate binding By similarity

Sites

Active site1091Proton donor By similarity
Metal binding1101Zinc 1; catalytic By similarity
Metal binding1441Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2261Zinc 1; catalytic By similarity
Metal binding2651Zinc 1; catalytic By similarity
Binding site621Glyceraldehyde 3-phosphate By similarity
Binding site2271Dihydroxyacetone phosphate; via amide nitrogen By similarity

Experimental info

Sequence conflict161K → L AA sequence Ref.2
Sequence conflict39 – 413SSS → WSW AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9URB4 [UniParc].

Last modified March 3, 2009. Version 2.
Checksum: 030943199E4D6C28

FASTA35939,215
        10         20         30         40         50         60 
MAPPAVLSKS GVIYGKDVKD LFDYAQEKGF AIPAINVTSS STVVAALEAA RDNKAPIILQ 

        70         80         90        100        110        120 
TSQGGAAYFA GKGVDNKDQA ASIAGSIAAA HYIRAIAPTY GIPVVLHTDH CAKKLLPWFD 

       130        140        150        160        170        180 
GMLKADEEFF AKTGTPLFSS HMLDLSEETD DENIATCAKY FERMAKMGQW LEMEIGITGG 

       190        200        210        220        230        240 
EEDGVNNEHV EKDALYTSPE TVFAVYESLH KISPNFSIAA AFGNVHGVYK PGNVQLRPEI 

       250        260        270        280        290        300 
LGDHQVYAKK QIGTDAKHPL YLVFHGGSGS TQEEFNTAIK NGVVKVNLDT DCQYAYLTGI 

       310        320        330        340        350 
RDYVTNKIEY LKAPVGNPEG ADKPNKKYFD PRVWVREGEK TMSKRIAEAL DIFHTKGQL 

« Hide

References

« Hide 'large scale' references
[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[2]"Identification of Candida albicans antigens reactive with immunoglobulin E antibody of human sera."
Ishiguro A., Homma M., Torii S., Tanaka K.
Infect. Immun. 60:1550-1557(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-41, SUBCELLULAR LOCATION, ALLERGEN.
Strain: C9.
[3]"Analysis of the serologic response to systemic Candida albicans infection in a murine model."
Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C., Nombela C.
Proteomics 1:550-559(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000005 Genomic DNA. Translation: EAL04108.1.
AACQ01000006 Genomic DNA. Translation: EAL03953.1.
PIRA43853.
RefSeqXP_722690.1. XM_717597.1.
XP_722836.1. XM_717743.1.

3D structure databases

ProteinModelPortalQ9URB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0003619.

Chemistry

BindingDBQ9URB4.
ChEMBLCHEMBL1287619.

Protein family/group databases

Allergome5990. Cand a FPA.

2D gel databases

COMPLUYEAST-2DPAGEQ9URB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3635548.
3635585.
KEGGcal:CaO19.12088.
cal:CaO19.4618.

Organism-specific databases

CGDCAL0003619. FBA1.

Phylogenomic databases

eggNOGCOG0191.
KOK01624.
OrthoDBEOG7HTHSN.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_CANAL
AccessionPrimary (citable) accession number: Q9URB4
Secondary accession number(s): Q5AMM8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names