ID ALDOB_HUMAN Reviewed; 364 AA. AC P05062; Q13741; Q13742; Q5T7D6; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 232. DE RecName: Full=Fructose-bisphosphate aldolase B; DE EC=4.1.2.13 {ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:20848650}; DE AltName: Full=Liver-type aldolase; GN Name=ALDOB {ECO:0000303|PubMed:15880727, ECO:0000312|HGNC:HGNC:417}; GN Synonyms=ALDB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6548561; DOI=10.1093/nar/12.19.7401; RA Paolella G., Santamaria R., Izzo P., Costanzo P., Salvatore F.; RT "Isolation and nucleotide sequence of a full-length cDNA coding for RT aldolase B from human liver."; RL Nucleic Acids Res. 12:7401-7410(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2410860; DOI=10.1093/nar/13.14.5055; RA Sakakibara M., Mukai T., Yatsuki H., Hori K.; RT "Human aldolase isozyme gene: the structure of multispecies aldolase B RT mRNAs."; RL Nucleic Acids Res. 13:5055-5069(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=6585824; DOI=10.1073/pnas.81.9.2738; RA Rottmann W.H., Tolan D.R., Penhoet E.E.; RT "Complete amino acid sequence for human aldolase B derived from cDNA and RT genomic clones."; RL Proc. Natl. Acad. Sci. U.S.A. 81:2738-2742(1984). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2830249; DOI=10.1093/oxfordjournals.jbchem.a122142; RA Mukai T., Yatsuki H., Arai Y., Joh K., Matsuhashi S., Hori K.; RT "Human aldolase B gene: characterization of the genomic aldolase B gene and RT analysis of sequences required for multiple polyadenylations."; RL J. Biochem. 102:1043-1051(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3016456; RA Tolan D.R., Penhoet E.E.; RT "Characterization of the human aldolase B gene."; RL Mol. Biol. Med. 3:245-264(1986). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF 2-33 AND 357-364. RX PubMed=2649152; DOI=10.1016/0167-4781(89)90156-5; RA Sakakibara M., Takahashi I., Takasaki Y., Mukai T., Hori K.; RT "Construction and expression of human aldolase A and B expression plasmids RT in Escherichia coli host."; RL Biochim. Biophys. Acta 1007:334-342(1989). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 238-364. RX PubMed=6689266; DOI=10.1016/0006-291x(83)91243-3; RA Besmond C., Dreyfus J.-C., Gregori C., Frain M., Zakin M.M., RA Sala Trepat J., Kahn A.; RT "Nucleotide sequence of a cDNA clone for human aldolase B."; RL Biochem. Biophys. Res. Commun. 117:601-609(1983). RN [10] RP INTERACTION WITH BBS1; BBS2; BBS4 AND BBS7, AND SUBCELLULAR LOCATION. RX PubMed=18000879; DOI=10.1002/cm.20250; RA Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.; RT "Novel interaction partners of Bardet-Biedl syndrome proteins."; RL Cell Motil. Cytoskeleton 65:143-155(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-89; THR-119; RP SER-132; SER-272; SER-276 AND SER-309, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH G6PD AND TP53, AND RP MUTAGENESIS OF ARG-43; ARG-46; LYS-108; LYS-147; ARG-149; LYS-230 AND RP ARG-304. RX PubMed=35122041; DOI=10.1038/s43018-020-0086-7; RA Li M., He X., Guo W., Yu H., Zhang S., Wang N., Liu G., Sa R., Shen X., RA Jiang Y., Tang Y., Zhuo Y., Yin C., Tu Q., Li N., Nie X., Li Y., Hu Z., RA Zhu H., Ding J., Li Z., Liu T., Zhang F., Zhou H., Li S., Yue J., Yan Z., RA Cheng S., Tao Y., Yin H.; RT "Aldolase B suppresses hepatocellular carcinogenesis by inhibiting G6PD and RT pentose phosphate pathways."; RL Nat. Cancer 1:735-747(2020). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=11679716; DOI=10.1107/s0907444901012719; RA Dalby A.R., Tolan D.R., Littlechild J.A.; RT "The structure of human liver fructose-1,6-bisphosphate aldolase."; RL Acta Crystallogr. D 57:1526-1533(2001). RN [14] RP REVIEW ON VARIANTS. RX PubMed=8535439; DOI=10.1002/humu.1380060303; RA Tolan D.R.; RT "Molecular basis of hereditary fructose intolerance: mutations and RT polymorphisms in the human aldolase B gene."; RL Hum. Mutat. 6:210-218(1995). RN [15] RP VARIANT HFI PRO-150. RX PubMed=3383242; DOI=10.1016/s0092-8674(88)90349-2; RA Cross N.C.P., Tolan D.R., Cox T.M.; RT "Catalytic deficiency of human aldolase B in hereditary fructose RT intolerance caused by a common missense mutation."; RL Cell 53:881-885(1988). RN [16] RP VARIANT HFI ASP-175. RX PubMed=1967768; DOI=10.1016/0140-6736(90)90603-3; RA Cross N.C.P., de Franchis R., Sebastio G., Dazzo C., Tolan D.R., RA Gregori C., Odievre M., Vidailhet M., Romano V., Mascali G., Romano C., RA Musumeci S., Steinmann B., Gitzelmann R., Cox T.M.; RT "Molecular analysis of aldolase B genes in hereditary fructose RT intolerance."; RL Lancet 335:306-309(1990). RN [17] RP VARIANT HFI ARG-135. RX PubMed=8299883; DOI=10.1096/fasebj.8.1.8299883; RA Brooks C.C., Tolan D.R.; RT "A partially active mutant aldolase B from a patient with hereditary RT fructose intolerance."; RL FASEB J. 8:107-113(1994). RN [18] RP VARIANT ARG-148. RX PubMed=7717389; RA Ali M., Cox T.M.; RT "Diverse mutations in the aldolase B gene that underlie the prevalence of RT hereditary fructose intolerance."; RL Am. J. Hum. Genet. 56:1002-1005(1995). RN [19] RP VARIANT HFI PRO-257. RX PubMed=8162030; DOI=10.1093/hmg/3.1.203; RA Ali M., Sebastio G., Cox T.M.; RT "Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B RT gene associated with hereditary fructose intolerance."; RL Hum. Mol. Genet. 3:203-204(1994). RN [20] RP VARIANT HFI LYS-335. RX PubMed=2336380; DOI=10.1093/nar/18.7.1925; RA Cross N.C.P., Stojanov L.M., Cox T.M.; RT "A new aldolase B variant, N334K, is a common cause of hereditary fructose RT intolerance in Yugoslavia."; RL Nucleic Acids Res. 18:1925-1925(1990). RN [21] RP VARIANTS HFI PRO-150; ASP-175; PRO-257; TRP-304; LYS-335 AND VAL-338. RX PubMed=10024431; DOI=10.1006/mcpr.1998.0208; RA Lau J., Tolan D.R.; RT "Screening for hereditary fructose intolerance mutations by reverse dot- RT blot."; RL Mol. Cell. Probes 13:35-40(1999). RN [22] RP VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304 RP AND TRP-304, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP AND PATHWAY. RX PubMed=10970798; DOI=10.1042/bj3500823; RA Santamaria R., Esposito G., Vitagliano L., Race V., Paglionico I., RA Zancan L., Zagari A., Salvatore F.; RT "Functional and molecular modelling studies of two hereditary fructose RT intolerance-causing mutations at arginine 303 in human liver aldolase."; RL Biochem. J. 350:823-828(2000). RN [23] RP VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335, FUNCTION, CATALYTIC RP ACTIVITY, AND PATHWAY. RX PubMed=12205126; DOI=10.1136/jmg.39.9.e56; RA Sanchez-Gutierrez J.C., Benlloch T., Leal M.A., Samper B., RA Garcia-Ripoll I., Feliu J.E.; RT "Molecular analysis of the aldolase B gene in patients with hereditary RT fructose intolerance from Spain."; RL J. Med. Genet. 39:E56-E56(2002). RN [24] RP VARIANTS HFI THR-74; 120-ASN-LYS-121 DEL; PRO-150; ASP-175; PHE-222; RP PRO-229; PRO-257; LYS-335 AND VAL-338, AND CHARACTERIZATION OF VARIANTS HFI RP THR-74; PHE-222 AND PRO-229. RX PubMed=15532022; DOI=10.1002/humu.9290; RA Esposito G., Santamaria R., Vitagliano L., Ieno L., Viola A., Fiori L., RA Parenti G., Zancan L., Zagari A., Salvatore F.; RT "Six novel alleles identified in Italian hereditary fructose intolerance RT patients enlarge the mutation spectrum of the aldolase B gene."; RL Hum. Mutat. 24:534-534(2004). RN [25] RP VARIANTS HFI PRO-150; ASP-175; ARG-178; PRO-284 AND LYS-335. RX PubMed=15880727; DOI=10.1002/humu.9343; RA Santer R., Rischewski J., von Weihe M., Niederhaus M., Schneppenheim S., RA Baerlocher K., Kohlschuetter A., Muntau A., Posselt H.-G., Steinmann B., RA Schneppenheim R.; RT "The spectrum of aldolase B (ALDOB) mutations and the prevalence of RT hereditary fructose intolerance in Central Europe."; RL Hum. Mutat. 25:594-594(2005). RN [26] RP VARIANTS HFI TRP-46; PRO-150; ASP-175 AND HIS-343, CHARACTERIZATION OF RP VARIANTS HFI TRP-46 AND HIS-343, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=20848650; DOI=10.1002/humu.21359; RA Esposito G., Imperato M.R., Ieno L., Sorvillo R., Benigno V., Parenti G., RA Parini R., Vitagliano L., Zagari A., Salvatore F.; RT "Hereditary fructose intolerance: functional study of two novel ALDOB RT natural variants and characterization of a partial gene deletion."; RL Hum. Mutat. 31:1294-1303(2010). CC -!- FUNCTION: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to CC form two triosephosphates dihydroxyacetone phosphate and D- CC glyceraldehyde 3-phosphate in glycolysis as well as the reverse CC stereospecific aldol addition reaction in gluconeogenesis. In CC fructolysis, metabolizes fructose 1-phosphate derived from the CC phosphorylation of dietary fructose by fructokinase into CC dihydroxyacetone phosphate and D-glyceraldehyde (PubMed:10970798, CC PubMed:12205126, PubMed:20848650). Acts as an adapter independently of CC its enzymatic activity, exerts a tumor suppressor role by stabilizing CC the ternary complex with G6PD and TP53 to inhibit G6PD activity and CC keep oxidative pentose phosphate metabolism in check (PubMed:35122041). CC {ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, CC ECO:0000269|PubMed:20848650, ECO:0000269|PubMed:35122041}. 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 Evidence={ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, CC ECO:0000269|PubMed:20848650}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; CC Evidence={ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12205126, CC ECO:0000305|PubMed:20848650}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14731; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1-phosphate = D-glyceraldehyde + CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:30851, ChEBI:CHEBI:17378, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:138881; CC Evidence={ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, CC ECO:0000269|PubMed:20848650}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30852; CC Evidence={ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12205126, CC ECO:0000305|PubMed:20848650}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30853; CC Evidence={ECO:0000305}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.6 uM for fructose 1,6-bisphosphate CC {ECO:0000269|PubMed:10970798}; CC KM=0.95 uM for fructose 1,6-bisphosphate CC {ECO:0000269|PubMed:20848650}; CC KM=2.3 mM for fructose 1-phosphate {ECO:0000269|PubMed:10970798}; CC KM=0.73 mM for fructose 1-phosphate {ECO:0000269|PubMed:20848650}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12205126, CC ECO:0000305|PubMed:20848650}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000305|PubMed:10970798, ECO:0000305|PubMed:12205126, CC ECO:0000305|PubMed:20848650}. CC -!- PATHWAY: Carbohydrate metabolism; fructose metabolism. CC {ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, CC ECO:0000269|PubMed:20848650}. CC -!- SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7 CC (PubMed:18000879). Forms a ternary complex with G6PD and TP53; this CC interaction is direct (PubMed:35122041). {ECO:0000269|PubMed:18000879, CC ECO:0000269|PubMed:35122041}. CC -!- INTERACTION: CC P05062; Q8NFJ9: BBS1; NbExp=4; IntAct=EBI-1045507, EBI-1805484; CC P05062; Q9BXC9: BBS2; NbExp=4; IntAct=EBI-1045507, EBI-748297; CC P05062; Q96RK4: BBS4; NbExp=4; IntAct=EBI-1045507, EBI-1805814; CC P05062; Q8IWZ6: BBS7; NbExp=4; IntAct=EBI-1045507, EBI-1806001; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:35122041}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, CC centriolar satellite {ECO:0000269|PubMed:18000879}. CC -!- DISEASE: Hereditary fructose intolerance (HFI) [MIM:229600]: Autosomal CC recessive disease that results in an inability to metabolize fructose CC and related sugars. Complete exclusion of fructose results in dramatic CC recovery; however, if not treated properly, HFI subjects suffer CC episodes of hypoglycemia, general ill condition, and risk of death the CC remainder of life. {ECO:0000269|PubMed:10024431, CC ECO:0000269|PubMed:10970798, ECO:0000269|PubMed:12205126, CC ECO:0000269|PubMed:15532022, ECO:0000269|PubMed:15880727, CC ECO:0000269|PubMed:1967768, ECO:0000269|PubMed:20848650, CC ECO:0000269|PubMed:2336380, ECO:0000269|PubMed:3383242, CC ECO:0000269|PubMed:8162030, ECO:0000269|PubMed:8299883}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: In vertebrates, 3 forms of this ubiquitous glycolytic CC enzyme are found, aldolase A in muscle, aldolase B in liver and CC aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44287/ALDOB"; 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; X02747; CAA26526.1; -; mRNA. DR EMBL; D00183; BAA00125.1; -; Genomic_DNA. DR EMBL; M15656; AAA51691.1; -; Genomic_DNA. DR EMBL; M15657; AAA51691.1; JOINED; Genomic_DNA. DR EMBL; AL353621; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW58951.1; -; Genomic_DNA. DR EMBL; X00270; CAA25072.1; -; mRNA. DR EMBL; X01098; CAA25572.1; -; mRNA. DR CCDS; CCDS6756.1; -. DR PIR; A41505; ADHUB. DR RefSeq; NP_000026.2; NM_000035.3. DR PDB; 1QO5; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-364. DR PDB; 1XDL; X-ray; 3.00 A; A/B/C/D/W/X/Y/Z=2-364. DR PDB; 1XDM; X-ray; 3.00 A; A/B/C/D/W/X/Y/Z=2-364. DR PDB; 8D44; EM; 2.80 A; A/B/C/D=1-364. DR PDBsum; 1QO5; -. DR PDBsum; 1XDL; -. DR PDBsum; 1XDM; -. DR PDBsum; 8D44; -. DR AlphaFoldDB; P05062; -. DR EMDB; EMD-27174; -. DR SMR; P05062; -. DR BioGRID; 106730; 42. DR IntAct; P05062; 29. DR MINT; P05062; -. DR STRING; 9606.ENSP00000497767; -. DR DrugBank; DB02512; 1,6-Fructose Diphosphate (Linear Form). DR DrugBank; DB04326; Dihydroxyacetone phosphate. DR DrugBank; DB02515; sn-glycerol 3-phosphate. DR MoonDB; P05062; Curated. DR GlyGen; P05062; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P05062; -. DR PhosphoSitePlus; P05062; -. DR BioMuta; ALDOB; -. DR DMDM; 113611; -. DR CPTAC; CPTAC-2720; -. DR EPD; P05062; -. DR jPOST; P05062; -. DR MassIVE; P05062; -. DR MaxQB; P05062; -. DR PaxDb; 9606-ENSP00000363988; -. DR PeptideAtlas; P05062; -. DR ProteomicsDB; 51773; -. DR Pumba; P05062; -. DR Antibodypedia; 1025; 473 antibodies from 33 providers. DR DNASU; 229; -. DR Ensembl; ENST00000647789.2; ENSP00000497767.1; ENSG00000136872.21. DR Ensembl; ENST00000648064.1; ENSP00000497990.1; ENSG00000136872.21. DR Ensembl; ENST00000648758.1; ENSP00000497731.1; ENSG00000136872.21. DR GeneID; 229; -. DR KEGG; hsa:229; -. DR MANE-Select; ENST00000647789.2; ENSP00000497767.1; NM_000035.4; NP_000026.2. DR UCSC; uc004bbk.3; human. DR AGR; HGNC:417; -. DR CTD; 229; -. DR DisGeNET; 229; -. DR GeneCards; ALDOB; -. DR GeneReviews; ALDOB; -. DR HGNC; HGNC:417; ALDOB. DR HPA; ENSG00000136872; Group enriched (intestine, kidney, liver). DR MalaCards; ALDOB; -. DR MIM; 229600; phenotype. DR MIM; 612724; gene. DR neXtProt; NX_P05062; -. DR OpenTargets; ENSG00000136872; -. DR Orphanet; 469; Hereditary fructose intolerance. DR PharmGKB; PA24710; -. DR VEuPathDB; HostDB:ENSG00000136872; -. DR eggNOG; KOG1557; Eukaryota. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_0_0_1; -. DR InParanoid; P05062; -. DR OMA; ANCQAAQ; -. DR OrthoDB; 3664741at2759; -. DR PhylomeDB; P05062; -. DR TreeFam; TF314203; -. DR BioCyc; MetaCyc:HS06234-MONOMER; -. DR BRENDA; 4.1.2.13; 2681. DR PathwayCommons; P05062; -. DR Reactome; R-HSA-5657560; Hereditary fructose intolerance. DR Reactome; R-HSA-70171; Glycolysis. DR Reactome; R-HSA-70263; Gluconeogenesis. DR Reactome; R-HSA-70350; Fructose catabolism. DR SABIO-RK; P05062; -. DR SignaLink; P05062; -. DR SIGNOR; P05062; -. DR UniPathway; UPA00109; UER00183. DR UniPathway; UPA00138; -. DR UniPathway; UPA00202; -. DR BioGRID-ORCS; 229; 10 hits in 1149 CRISPR screens. DR ChiTaRS; ALDOB; human. DR EvolutionaryTrace; P05062; -. DR GeneWiki; Aldolase_B; -. DR GenomeRNAi; 229; -. DR Pharos; P05062; Tbio. DR PRO; PR:P05062; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P05062; Protein. DR Bgee; ENSG00000136872; Expressed in jejunal mucosa and 142 other cell types or tissues. DR ExpressionAtlas; P05062; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005815; C:microtubule organizing center; IDA:BHF-UCL. DR GO; GO:0051117; F:ATPase binding; IDA:BHF-UCL. DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL. DR GO; GO:0070061; F:fructose binding; IMP:BHF-UCL. DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; IDA:UniProtKB. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:BHF-UCL. DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IEA:Ensembl. DR GO; GO:0006000; P:fructose metabolic process; IMP:BHF-UCL. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006096; P:glycolytic process; IDA:UniProtKB. DR GO; GO:0006116; P:NADH oxidation; IDA:BHF-UCL. DR GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; IMP:UniProtKB. DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IGI:BHF-UCL. DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IGI:BHF-UCL. DR CDD; cd00948; FBP_aldolase_I_a; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR11627:SF2; FRUCTOSE-BISPHOSPHATE ALDOLASE B; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. DR Genevisible; P05062; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Disease variant; Glycolysis; Lyase; KW Phosphoprotein; Reference proteome; Schiff base. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q91Y97, FT ECO:0000269|PubMed:2649152" FT CHAIN 2..364 FT /note="Fructose-bisphosphate aldolase B" FT /id="PRO_0000216940" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00883" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 43 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 272..274 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 304 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250|UniProtKB:P00883" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 13 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 39 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 119 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 121 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00884" FT MOD_RES 301 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00884" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 317 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91Y97" FT VARIANT 46 FT /note="R -> W (in HFI; reduced enzymatic activity; FT dbSNP:rs41281039)" FT /evidence="ECO:0000269|PubMed:20848650" FT /id="VAR_075348" FT VARIANT 74 FT /note="I -> T (in HFI; affects proper folding; FT dbSNP:rs781023784)" FT /evidence="ECO:0000269|PubMed:15532022" FT /id="VAR_020822" FT VARIANT 120..121 FT /note="Missing (in HFI)" FT /evidence="ECO:0000269|PubMed:15532022" FT /id="VAR_020823" FT VARIANT 134 FT /note="R -> S (in dbSNP:rs10123355)" FT /id="VAR_038429" FT VARIANT 135 FT /note="C -> R (in HFI; America; partial activity)" FT /evidence="ECO:0000269|PubMed:8299883" FT /id="VAR_000551" FT VARIANT 148 FT /note="W -> R (in one subject with fructose intolerance; FT rare variant; America; dbSNP:rs118204430)" FT /evidence="ECO:0000269|PubMed:7717389" FT /id="VAR_000552" FT VARIANT 150 FT /note="A -> P (in HFI; frequent mutation; dbSNP:rs1800546)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:15532022, FT ECO:0000269|PubMed:15880727, ECO:0000269|PubMed:20848650, FT ECO:0000269|PubMed:3383242" FT /id="VAR_000553" FT VARIANT 175 FT /note="A -> D (in HFI; frequent mutation; FT dbSNP:rs76917243)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:15532022, FT ECO:0000269|PubMed:15880727, ECO:0000269|PubMed:1967768, FT ECO:0000269|PubMed:20848650" FT /id="VAR_000554" FT VARIANT 178 FT /note="C -> R (in HFI)" FT /evidence="ECO:0000269|PubMed:15880727" FT /id="VAR_058211" FT VARIANT 185 FT /note="P -> R (in HFI)" FT /evidence="ECO:0000269|PubMed:12205126" FT /id="VAR_020824" FT VARIANT 207 FT /note="E -> Q (in dbSNP:rs3739721)" FT /id="VAR_020825" FT VARIANT 222 FT /note="V -> F (in HFI; affects proper folding; FT dbSNP:rs1554702442)" FT /evidence="ECO:0000269|PubMed:15532022" FT /id="VAR_020826" FT VARIANT 229 FT /note="L -> P (in HFI; affects proper folding; FT dbSNP:rs1554702433)" FT /evidence="ECO:0000269|PubMed:15532022" FT /id="VAR_020827" FT VARIANT 257 FT /note="L -> P (in HFI; Italy; dbSNP:rs764701775)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:15532022, ECO:0000269|PubMed:8162030" FT /id="VAR_000555" FT VARIANT 268 FT /note="I -> N (in dbSNP:rs10989495)" FT /id="VAR_038430" FT VARIANT 284 FT /note="L -> P (in HFI)" FT /evidence="ECO:0000269|PubMed:15880727" FT /id="VAR_058212" FT VARIANT 304 FT /note="R -> Q (in HFI; 100-fold decrease in catalytic FT efficiency for substrates F1,6BP and F1P; FT dbSNP:rs145078268)" FT /evidence="ECO:0000269|PubMed:10970798" FT /id="VAR_020828" FT VARIANT 304 FT /note="R -> W (in HFI; Turkey; 4800-fold decrease in FT catalytic efficiency for F1,6BP and inactive with F1P; FT dbSNP:rs555935217)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:10970798" FT /id="VAR_000556" FT VARIANT 335 FT /note="N -> K (in HFI; frequent mutation; FT dbSNP:rs78340951)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:12205126, ECO:0000269|PubMed:15532022, FT ECO:0000269|PubMed:15880727, ECO:0000269|PubMed:2336380" FT /id="VAR_000557" FT VARIANT 338 FT /note="A -> V (in HFI; Turkey and South Europe; FT dbSNP:rs77718928)" FT /evidence="ECO:0000269|PubMed:10024431, FT ECO:0000269|PubMed:15532022" FT /id="VAR_000558" FT VARIANT 343 FT /note="Y -> H (in HFI; almost no effect on enzymatic FT activity at 30 degrees Celsius, but reduced activity at FT higher temperatures; dbSNP:rs369586696)" FT /evidence="ECO:0000269|PubMed:20848650" FT /id="VAR_075349" FT MUTAGEN 43 FT /note="R->A: Loss of enzymatic activity. Retains the FT ability to interact with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 46 FT /note="R->A: Decreases enzymatic activity. Retains the FT ability to interact with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 108 FT /note="K->A: Decreases enzymatic activity. Retains the FT ability to interact with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 147 FT /note="K->A: Loss of enzymatic activity. Impairs the FT interaction with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 149 FT /note="R->A: Loss of enzymatic activity. Impairs the FT interaction with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 230 FT /note="K->A: Loss of enzymatic activity. Impairs the FT interaction with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT MUTAGEN 304 FT /note="R->A: Decreases enzymatic activity. Impairs the FT interaction with G6PD." FT /evidence="ECO:0000269|PubMed:35122041" FT CONFLICT 54 FT /note="E -> D (in Ref. 5; AAA51691)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="A -> D (in Ref. 9; CAA25072)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="E -> D (in Ref. 4; BAA00125)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="S -> V (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="S -> C (in Ref. 4; BAA00125)" FT /evidence="ECO:0000305" FT HELIX 10..23 FT /evidence="ECO:0007829|PDB:1QO5" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:1XDL" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 37..46 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 68..72 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:1QO5" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:1XDM" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 131..140 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 161..179 FT /evidence="ECO:0007829|PDB:1QO5" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 199..219 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 246..260 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:1QO5" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1XDM" FT STRAND 296..303 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 308..314 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 321..338 FT /evidence="ECO:0007829|PDB:1QO5" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:1QO5" FT HELIX 351..354 FT /evidence="ECO:0007829|PDB:1QO5" SQ SEQUENCE 364 AA; 39473 MW; DCE314E7AC5586CA CRC64; MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF SYGRALQASA LAAWGGKAAN KEATQEAFMK RAMANCQAAK GQYVHTGSSG AASTQSLFTA CYTY //