ID ALF_CANAL Reviewed; 359 AA. AC Q9URB4; A0A1D8PLC4; Q5AMM8; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 2. DT 24-JAN-2024, entry version 131. DE RecName: Full=Fructose-bisphosphate aldolase; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=37 kDa major allergen; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; DE AltName: Full=IgE-binding allergen; GN Name=FBA1; OrderedLocusNames=CAALFM_C401750CA; GN ORFNames=CaO19.12088, CaO19.4618; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP PROTEIN SEQUENCE OF 2-41, SUBCELLULAR LOCATION, AND ALLERGEN. RC STRAIN=C9; RX PubMed=1548078; DOI=10.1128/iai.60.4.1550-1557.1992; RA Ishiguro A., Homma M., Torii S., Tanaka K.; RT "Identification of Candida albicans antigens reactive with immunoglobulin E RT antibody of human sera."; RL Infect. Immun. 60:1550-1557(1992). RN [5] RP PROTEIN SEQUENCE OF 2-21. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=11681208; RX DOI=10.1002/1615-9861(200104)1:4<550::aid-prot550>3.0.co;2-w; RA Pitarch A., Diez-Orejas R., Molero G., Pardo M., Sanchez M., Gil C., RA Nombela C.; RT "Analysis of the serologic response to systemic Candida albicans infection RT in a murine model."; RL Proteomics 1:550-559(2001). CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and CC the reverse reaction in glycolysis. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other CC provides a structural contribution. {ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1548078}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. CC {ECO:0000269|PubMed:1548078}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP017626; AOW28947.1; -; Genomic_DNA. DR PIR; A43853; A43853. DR RefSeq; XP_722690.1; XM_717597.2. DR PDB; 6LNK; X-ray; 2.64 A; A/B=1-359. DR PDB; 7V6F; X-ray; 2.98 A; A/B=1-359. DR PDB; 7V6G; X-ray; 2.34 A; A/B=1-359. DR PDB; 7YVA; X-ray; 2.93 A; A/B=1-359. DR PDBsum; 6LNK; -. DR PDBsum; 7V6F; -. DR PDBsum; 7V6G; -. DR PDBsum; 7YVA; -. DR AlphaFoldDB; Q9URB4; -. DR SMR; Q9URB4; -. DR BioGRID; 1218642; 1. DR STRING; 237561.Q9URB4; -. DR BindingDB; Q9URB4; -. DR ChEMBL; CHEMBL1287619; -. DR Allergome; 5990; Cand a FPA. DR MoonProt; Q9URB4; -. DR EnsemblFungi; C4_01750C_A-T; C4_01750C_A-T-p1; C4_01750C_A. DR GeneID; 3635585; -. DR KEGG; cal:CAALFM_C401750CA; -. DR CGD; CAL0000186998; FBA1. DR VEuPathDB; FungiDB:C4_01750C_A; -. DR eggNOG; KOG4153; Eukaryota. DR HOGENOM; CLU_036923_0_0_1; -. DR InParanoid; Q9URB4; -. DR OMA; PRTWGKL; -. DR OrthoDB; 275443at2759; -. DR BRENDA; 4.1.2.13; 1096. DR UniPathway; UPA00109; UER00183. DR PRO; PR:Q9URB4; -. DR Proteomes; UP000000559; Chromosome 4. DR GO; GO:0009986; C:cell surface; IDA:CGD. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD. DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD. DR GO; GO:0005886; C:plasma membrane; IDA:CGD. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0051701; P:biological process involved in interaction with host; IPI:CGD. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD. DR CDD; cd00946; FBP_aldolase_IIA; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR006411; Fruct_bisP_bact. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1. DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1. DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1. DR COMPLUYEAST-2DPAGE; Q9URB4; -. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Cytoplasm; Direct protein sequencing; Glycolysis; KW Lyase; Metal-binding; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11681208, FT ECO:0000269|PubMed:1548078" FT CHAIN 2..359 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178757" FT ACT_SITE 109 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 62 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 265 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 266..268 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 287..290 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT CONFLICT 16 FT /note="K -> L (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 39..41 FT /note="SSS -> WSW (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 5..8 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 40..52 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 63..70 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 80..96 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 102..108 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 116..133 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 150..165 FT /evidence="ECO:0007829|PDB:7V6G" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 238..252 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 272..280 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 289..302 FT /evidence="ECO:0007829|PDB:7V6G" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 307..309 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:7V6G" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7V6G" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:6LNK" FT HELIX 326..329 FT /evidence="ECO:0007829|PDB:7V6G" FT HELIX 331..352 FT /evidence="ECO:0007829|PDB:7V6G" SQ 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 //