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Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (37 kDa major allergen) (Fructose-1,6-bisphosphate aldolase) (IgE-binding allergen)

 ALF_CANAL               Reviewed;         359 AA.
Q9URB4; A0A1D8PLC4; Q5AMM8;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 2.
07-JUN-2017, entry version 100.
RecName: Full=Fructose-bisphosphate aldolase;
Short=FBP aldolase;
Short=FBPA;
EC=4.1.2.13;
AltName: Full=37 kDa major allergen;
AltName: Full=Fructose-1,6-bisphosphate aldolase;
AltName: Full=IgE-binding allergen;
Name=FBA1; OrderedLocusNames=CAALFM_C401750CA;
ORFNames=CaO19.12088, CaO19.4618;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
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.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
PROTEIN SEQUENCE OF 2-41, SUBCELLULAR LOCATION, AND ALLERGEN.
STRAIN=C9;
PubMed=1548078;
Ishiguro A., Homma M., Torii S., Tanaka K.;
"Identification of Candida albicans antigens reactive with
immunoglobulin E antibody of human sera.";
Infect. Immun. 60:1550-1557(1992).
[5]
PROTEIN SEQUENCE OF 2-21.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=11681208;
DOI=10.1002/1615-9861(200104)1:4<550::AID-PROT550>3.0.CO;2-W;
Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C.,
Nombela C.;
"Analysis of the serologic response to systemic Candida albicans
infection in a murine model.";
Proteomics 1:550-559(2001).
-!- 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.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
phosphate + D-glyceraldehyde 3-phosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the
other provides a structural contribution. {ECO:0000250};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 4/4.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1548078}.
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
{ECO:0000269|PubMed:1548078}.
-!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017626; AOW28947.1; -; Genomic_DNA.
PIR; A43853; A43853.
RefSeq; XP_722690.1; XM_717597.2.
ProteinModelPortal; Q9URB4; -.
SMR; Q9URB4; -.
BindingDB; Q9URB4; -.
ChEMBL; CHEMBL1287619; -.
Allergome; 5990; Cand a FPA.
COMPLUYEAST-2DPAGE; Q9URB4; -.
PRIDE; Q9URB4; -.
GeneID; 3635585; -.
KEGG; cal:CAALFM_C401750CA; -.
CGD; CAL0000186998; FBA1.
InParanoid; Q9URB4; -.
KO; K01624; -.
OrthoDB; EOG092C385G; -.
UniPathway; UPA00109; UER00183.
PRO; PR:Q9URB4; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0005886; C:plasma membrane; IDA:CGD.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
GO; GO:0051701; P:interaction with host; IPI:CGD.
CDD; cd00946; FBP_aldolase_IIA; 1.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000771; FBA_II.
InterPro; IPR006411; Fruct_bisP_bact.
Pfam; PF01116; F_bP_aldolase; 1.
PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
TIGRFAMs; TIGR00167; cbbA; 1.
TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
1: Evidence at protein level;
Allergen; Complete proteome; Cytoplasm; Direct protein sequencing;
Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11681208,
ECO:0000269|PubMed:1548078}.
CHAIN 2 359 Fructose-bisphosphate aldolase.
/FTId=PRO_0000178757.
REGION 266 268 Dihydroxyacetone phosphate binding.
{ECO:0000250}.
REGION 287 290 Dihydroxyacetone phosphate binding.
{ECO:0000250}.
ACT_SITE 109 109 Proton donor. {ECO:0000250}.
METAL 110 110 Zinc 1; catalytic. {ECO:0000250}.
METAL 144 144 Zinc 2. {ECO:0000250}.
METAL 174 174 Zinc 2. {ECO:0000250}.
METAL 226 226 Zinc 1; catalytic. {ECO:0000250}.
METAL 265 265 Zinc 1; catalytic. {ECO:0000250}.
BINDING 62 62 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 227 227 Dihydroxyacetone phosphate; via amide
nitrogen. {ECO:0000250}.
CONFLICT 16 16 K -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 39 41 SSS -> WSW (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 359 AA; 39215 MW; 030943199E4D6C28 CRC64;
MAPPAVLSKS GVIYGKDVKD LFDYAQEKGF AIPAINVTSS STVVAALEAA RDNKAPIILQ
TSQGGAAYFA GKGVDNKDQA ASIAGSIAAA HYIRAIAPTY GIPVVLHTDH CAKKLLPWFD
GMLKADEEFF AKTGTPLFSS HMLDLSEETD DENIATCAKY FERMAKMGQW LEMEIGITGG
EEDGVNNEHV EKDALYTSPE TVFAVYESLH KISPNFSIAA AFGNVHGVYK PGNVQLRPEI
LGDHQVYAKK QIGTDAKHPL YLVFHGGSGS TQEEFNTAIK NGVVKVNLDT DCQYAYLTGI
RDYVTNKIEY LKAPVGNPEG ADKPNKKYFD PRVWVREGEK TMSKRIAEAL DIFHTKGQL


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