Q9URB4 (ALF_CANAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida › Candida albicans

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Disease	Allergen
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway induction by symbiont of host defense response Inferred from direct assay Ref.3. Source: CGD
Cellular_component	cell surface Inferred from direct assay PubMed 12543933. Source: CGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell hyphal cell wall Inferred from direct assay PubMed 1383159. Source: CGD plasma membrane Inferred from direct assay PubMed 19824013. Source: CGD
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2 Ref.3
	Chain	2 – 359	358	Fructose-bisphosphate aldolase		PRO_0000178757
Regions
	Region	266 – 268	3	Dihydroxyacetone phosphate binding By similarity
	Region	287 – 290	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	109	1	Proton donor By similarity
	Metal binding	110	1	Zinc 1; catalytic By similarity
	Metal binding	144	1	Zinc 2 By similarity
	Metal binding	174	1	Zinc 2 By similarity
	Metal binding	226	1	Zinc 1; catalytic By similarity
	Metal binding	265	1	Zinc 1; catalytic By similarity
	Binding site	62	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	227	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity
Experimental info
	Sequence conflict	16	1	K → L AA sequence Ref.2
	Sequence conflict	39 – 41	3	SSS → WSW AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9URB4 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: 030943199E4D6C28	FASTA	359	39,215
	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

References

	« Hide 'large scale' referencesShow '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.
PIR	A43853.
RefSeq	XP_722690.1. XM_717597.1. XP_722836.1. XM_717743.1.
3D structure databases
ProteinModelPortal	Q9URB4.
ModBase	Search...
Protein-protein interaction databases
STRING	5476.CAL0003619.
Protein family/group databases
Allergome	5990. Cand a FPA.
2D gel databases
COMPLUYEAST-2DPAGE	Q9URB4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3635548. 3635585.
KEGG	cal:CaO19.12088. cal:CaO19.4618.
Organism-specific databases
CGD	CAL0003619. FBA1.
Phylogenomic databases
eggNOG	COG0191.
KO	K01624.
Enzyme and pathway databases
UniPathway	UPA00109; UER00183.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR006411. Fruct_bisP_bact. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMs	TIGR00167. cbbA. 1 hit. TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9URB4.
ChEMBL	CHEMBL1287619.

Entry information

Entry name

ALF_CANAL

Accession

Primary (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 3, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program