ALDOB_HUMAN
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 03-AUG-2022, entry version 225.
DE RecName: Full=Fructose-bisphosphate aldolase B;
DE EC=4.1.2.13;
DE AltName: Full=Liver-type aldolase;
GN Name=ALDOB; 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 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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
RP VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304
RP AND TRP-304, AND KINETIC PARAMETERS.
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 [22]
RP VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335.
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 [23]
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 [24]
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 [25]
RP VARIANTS HFI TRP-46; PRO-150; ASP-175 AND HIS-343, AND CHARACTERIZATION OF
RP VARIANT HFI TRP-46.
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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:10970798};
CC KM=2.3 mM for fructose 1-phosphate {ECO:0000269|PubMed:10970798};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7.
CC {ECO:0000269|PubMed:18000879}.
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, cytoskeleton, microtubule organizing
CC center, centrosome, 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="http://atlasgeneticsoncology.org/Genes/ALDOBID44287ch9q31.html";
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 PDBsum; 1QO5; -.
DR PDBsum; 1XDL; -.
DR PDBsum; 1XDM; -.
DR AlphaFoldDB; P05062; -.
DR SMR; P05062; -.
DR BioGRID; 106730; 38.
DR IntAct; P05062; 29.
DR MINT; P05062; -.
DR STRING; 9606.ENSP00000363988; -.
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 EPD; P05062; -.
DR jPOST; P05062; -.
DR MassIVE; P05062; -.
DR MaxQB; P05062; -.
DR PaxDb; P05062; -.
DR PeptideAtlas; P05062; -.
DR PRIDE; P05062; -.
DR ProteomicsDB; 51773; -.
DR Antibodypedia; 1025; 416 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 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; 799973at2759; -.
DR PhylomeDB; P05062; -.
DR TreeFam; TF314203; -.
DR BioCyc; MetaCyc:HS06234-MON; -.
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 BioGRID-ORCS; 229; 10 hits in 1069 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 tissues.
DR ExpressionAtlas; P05062; baseline and differential.
DR Genevisible; P05062; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:MGI.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
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:0006096; P:glycolytic process; IDA:BHF-UCL.
DR GO; GO:0006116; P:NADH oxidation; IDA:BHF-UCL.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
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"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
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 FBP and F1P; 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 FBP 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 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
