ALF_CANAL
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 03-AUG-2022, entry version 126.
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}.
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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 PDBsum; 6LNK; -.
DR PDBsum; 7V6F; -.
DR PDBsum; 7V6G; -.
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 COMPLUYEAST-2DPAGE; Q9URB4; -.
DR PRIDE; Q9URB4; -.
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; 773537at2759; -.
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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
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:6LNK"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:6LNK"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:6LNK"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:6LNK"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6LNK"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:6LNK"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:6LNK"
FT HELIX 331..352
FT /evidence="ECO:0007829|PDB:6LNK"
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
