ID   ALF_KLULA               Reviewed;         361 AA.
AC   Q9C2U0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN   Name=FBA1; OrderedLocusNames=KLLA0E07546g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15467790; DOI=10.1139/w04-038;
RA   Diaz Prado S.M., Cerdan M.E., Gonzalez Siso M.I.;
RT   "Isolation and transcriptional regulation of the Kluyveromyces lactis FBA1
RT   (fructose-1,6-bisphosphate aldolase) gene.";
RL   Can. J. Microbiol. 50:645-652(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ272114; CAC29023.2; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99377.1; -; Genomic_DNA.
DR   RefSeq; XP_454290.1; XM_454290.1.
DR   AlphaFoldDB; Q9C2U0; -.
DR   SMR; Q9C2U0; -.
DR   STRING; 284590.Q9C2U0; -.
DR   PaxDb; 284590-Q9C2U0; -.
DR   GeneID; 2894094; -.
DR   KEGG; kla:KLLA0_E07569g; -.
DR   eggNOG; KOG4153; Eukaryota.
DR   HOGENOM; CLU_036923_0_0_1; -.
DR   InParanoid; Q9C2U0; -.
DR   OMA; PRTWGKL; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..361
FT                   /note="Fructose-bisphosphate aldolase"
FT                   /id="PRO_0000178758"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         267..269
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         288..291
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39600 MW;  DCF0BEC26FF953D5 CRC64;
     MPAQDVLTRK TGVIVGDDVK ALFDYAKEHK FAIPAINVTS SSTVVAALEA ARDNKSPIIL
     QTSNGGAAYF AGKGVSNEGQ NASIRGSIAA AHYIRSIAPA YGIPVVLHTD HCAKKLLPWF
     DGMLKADEEY FAKHGEPLFS SHMLDLSEET DEENIGLCVK YFTRMAKIHQ WLEMEIGITG
     GEEDGVNNEG TSNDKLYTTP ETVFSVHEAL SKISPNFSIA SAFGNVHGVY KIAAALKPEL
     LGTFQDYAAK QLNKKAEDKP LYLVFHGGSG SSTKDFHTAI DFGVVKVNLD TDCQFAYLSG
     IRDYVLNKKD YLMTPVGNPT GEDSPNKKYY DPRVWVREGE KTMSKRITQA LEIFRTKGAL
     E
//