[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/12.19.7401; PubMed=6548561 [NCBI, ExPASy, EBI, Israel, Japan] Paolella G., Santamaria R., Izzo P., Costanzo P., Salvatore F.; "Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver."; Nucleic Acids Res. 12:7401-7410(1984).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/13.14.5055; PubMed=2410860 [NCBI, ExPASy, EBI, Israel, Japan] Sakakibara M., Mukai T., Yatsuki H., Hori K.; "Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs."; Nucleic Acids Res. 13:5055-5069(1985).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. PubMed=6585824 [NCBI, ExPASy, EBI, Israel, Japan] Rottmann W.H., Tolan D.R., Penhoet E.E.; "Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones."; Proc. Natl. Acad. Sci. U.S.A. 81:2738-2742(1984).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2830249 [NCBI, ExPASy, EBI, Israel, Japan] Mukai T., Yatsuki H., Arai Y., Joh K., Matsuhashi S., Hori K.; "Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations."; J. Biochem. 102:1043-1051(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3016456 [NCBI, ExPASy, EBI, Israel, Japan] Tolan D.R., Penhoet E.E.; "Characterization of the human aldolase B gene."; Mol. Biol. Med. 3:245-264(1986).
[6]	PROTEIN SEQUENCE OF 2-33 AND 357-364. DOI=10.1016/0167-4781(89)90156-5; PubMed=2649152 [NCBI, ExPASy, EBI, Israel, Japan] Sakakibara M., Takahashi I., Takasaki Y., Mukai T., Hori K.; "Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host."; Biochim. Biophys. Acta 1007:334-342(1989).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 238-364. DOI=10.1016/0006-291X(83)91243-3; PubMed=6689266 [NCBI, ExPASy, EBI, Israel, Japan] Besmond C., Dreyfus J.-C., Gregori C., Frain M., Zakin M.M., Sala Trepat J., Kahn A.; "Nucleotide sequence of a cDNA clone for human aldolase B."; Biochem. Biophys. Res. Commun. 117:601-609(1983).
[8]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1107/S0907444901012719; PubMed=11679716 [NCBI, ExPASy, EBI, Israel, Japan] Dalby A.R., Tolan D.R., Littlechild J.A.; "The structure of human liver fructose-1,6-bisphosphate aldolase."; Acta Crystallogr. D 57:1526-1533(2001).
[9]	REVIEW ON VARIANTS. DOI=10.1002/humu.1380060303; PubMed=8535439 [NCBI, ExPASy, EBI, Israel, Japan] Tolan D.R.; "Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene."; Hum. Mutat. 6:210-218(1995).
[10]	VARIANT HFI PRO-150. DOI=10.1016/S0092-8674(88)90349-2; PubMed=3383242 [NCBI, ExPASy, EBI, Israel, Japan] Cross N.C.P., Tolan D.R., Cox T.M.; "Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation."; Cell 53:881-885(1988).
[11]	VARIANT HFI ASP-175. DOI=10.1016/0140-6736(90)90603-3; PubMed=1967768 [NCBI, ExPASy, EBI, Israel, Japan] Cross N.C.P., de Franchis R., Sebastio G., Dazzo C., Tolan D.R., Gregori C., Odievre M., Vidailhet M., Romano V., Mascali G., Romano C., Musumeci S., Steinmann B., Gitzelmann R., Cox T.M.; "Molecular analysis of aldolase B genes in hereditary fructose intolerance."; Lancet 335:306-309(1990).
[12]	VARIANT HFI ARG-135. PubMed=8299883 [NCBI, ExPASy, EBI, Israel, Japan] Brooks C.C., Tolan D.R.; "A partially active mutant aldolase B from a patient with hereditary fructose intolerance."; FASEB J. 8:107-113(1994).
[13]	VARIANT ARG-148. PubMed=7717389 [NCBI, ExPASy, EBI, Israel, Japan] Ali M., Cox T.M.; "Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance."; Am. J. Hum. Genet. 56:1002-1005(1995).
[14]	VARIANT HFI PRO-257. DOI=10.1093/hmg/3.1.203; PubMed=8162030 [NCBI, ExPASy, EBI, Israel, Japan] Ali M., Sebastio G., Cox T.M.; "Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance."; Hum. Mol. Genet. 3:203-204(1994).
[15]	VARIANT HFI LYS-335. DOI=10.1093/nar/18.7.1925; PubMed=2336380 [NCBI, ExPASy, EBI, Israel, Japan] Cross N.C.P., Stojanov L.M., Cox T.M.; "A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia."; Nucleic Acids Res. 18:1925-1925(1990).
[16]	VARIANTS HFI PRO-150; ASP-175; PRO-257; TRP-304; LYS-335 AND VAL-338. DOI=10.1006/mcpr.1998.0208; PubMed=10024431 [NCBI, ExPASy, EBI, Israel, Japan] Lau J., Tolan D.R.; "Screening for hereditary fructose intolerance mutations by reverse dot-blot."; Mol. Cell. Probes 13:35-40(1999).
[17]	VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304 AND TRP-304, AND KINETIC PARAMETERS. DOI=10.1042/0264-6021:3500823; PubMed=10970798 [NCBI, ExPASy, EBI, Israel, Japan] Santamaria R., Esposito G., Vitagliano L., Race V., Paglionico I., Zancan L., Zagari A., Salvatore F.; "Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase."; Biochem. J. 350:823-828(2000).
[18]	VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335. DOI=10.1136/jmg.39.9.e56; PubMed=12205126 [NCBI, ExPASy, EBI, Israel, Japan] Sanchez-Gutierrez J.C., Benlloch T., Leal M.A., Samper B., Garcia-Ripoll I., Feliu J.E.; "Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain."; J. Med. Genet. 39:E56-E56(2002).
[19]	VARIANTS HFI THR-74; 120-ASN-LYS-121 DEL; PRO-150; ASP-175; PHE-222; PRO-229; PRO-257; LYS-335 AND VAL-338, AND CHARACTERIZATION OF VARIANTS HFI THR-74; PHE-222 AND PRO-229. DOI=10.1002/humu.9290; PubMed=15532022 [NCBI, ExPASy, EBI, Israel, Japan] Esposito G., Santamaria R., Vitagliano L., Ieno L., Viola A., Fiori L., Parenti G., Zancan L., Zagari A., Salvatore F.; "Six novel alleles identified in Italian hereditary fructose intolerance patients enlarge the mutation spectrum of the aldolase B gene."; Hum. Mutat. 24:534-534(2004).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=1.6 µM for fructose 1,6-bisphosphate;
K_M=2.3 mM for fructose 1-phosphate;
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4 .
SUBUNIT: Homotetramer.
DISEASE: Defects in ALDOB are the cause of hereditary fructose intolerance (HFI) [MIM:229600]. HFI is an autosomal recessive disease that results in an inability to metabolize fructose and related sugars. Complete exclusion of fructose results in dramatic recovery; however, if not treated properly, HFI subjects suffer episodes of hypoglycemia, general ill condition, and risk of death the remainder of life.
MISCELLANEOUS: In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.
SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ALDOB";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X02747; CAA26526.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X01098; CAA25572.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00183; BAA00125.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15656; AAA51691.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15657; AAA51691.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00270; CAA25072.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A41505; ADHUB.

NP_000026.2; -.

3D structure databases

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.	[ExPASy / RCSB / EBI]
1XDL; X-ray; 3.00 A; A/B/C/D/W/X/Y/Z=1-364.	[ExPASy / RCSB / EBI]
1XDM; X-ray; 3.00 A; A/B/C/D/W/X/Y/Z=1-364.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QO5; -.
1XDL; -.
1XDM; -.

ModBase

P05062.

Protein-protein interaction databases

IntAct

P05062; -.

PTM databases

PhosphoSite

P05062; -.

Enzyme and pathway databases

Reactome

REACT_1709; Metabolism of small molecules.

Organism-specific databases

H-InvDB

HIX0008244; -.
HIX0025826; -.

HGNC:417; ALDOB.

HPA002198; -.

229600; gene+phenotype. [NCBI / EBI]

Orphanet

469; Fructose intolerance.

PharmGKB

PA24710; -.

GeneCards

P05062.

Gene expression databases

ArrayExpress

P05062; -.

CleanEx

HS_ALDOB; -.

GermOnline

ENSG00000136872; Homo sapiens.

Ontologies

GO:0034451;	Cellular component: centriolar satellite (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0051117;	Molecular function: ATPase binding (inferred from direct assay from UniProtKB).
GO:0008092;	Molecular function: cytoskeletal protein binding (inferred from direct assay from UniProtKB).
GO:0070061;	Molecular function: fructose binding (inferred from mutant phenotype from UniProtKB).
GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from direct assay from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from UniProtKB).
GO:0043623;	Biological process: cellular protein complex assembly (inferred from genetic interaction from UniProtKB).
GO:0030388;	Biological process: fructose 1,6-bisphosphate metabolic process (inferred from direct assay from UniProtKB).
GO:0006096;	Biological process: glycolysis (inferred from direct assay from UniProtKB).
GO:0006116;	Biological process: NADH oxidation (inferred from direct assay from UniProtKB).
GO:0032781;	Biological process: positive regulation of ATPase activity (inferred from genetic interaction from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Proteomic databases

P05062; -.

Genome annotation databases

Ensembl

ENSG00000136872; Homo sapiens. [Contig view]

GeneID

229; -.

KEGG

hsa:229; -.

Phylogenomic databases

HOGENOM

P05062; -.

HOVERGEN

P05062; -.

Other

NextBio

930; -.

SOURCE

ALDOB; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Disease mutation; Glycolysis; Lyase; Phosphoprotein; Polymorphism; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase B.`	`PRO_0000216940`
`ACT_SITE`	`188 188`		`Proton acceptor (By similarity).`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`56 56`		`Substrate.`
`BINDING`	`147 147`		`Substrate.`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`36 36`		`Phosphoserine (By similarity).`
`VARIANT`	`74 74`	`1`	`I -> T (in HFI; affects proper folding).`	`VAR_020822 [3D]`
`VARIANT`	`120 121`	`2`	`Missing (in HFI).`	`VAR_020823`
`VARIANT`	`134 134`	`1`	`R -> S (in dbSNP:rs10123355 [NCBI]).`	`VAR_038429 [3D]`
`VARIANT`	`135 135`	`1`	`C -> R (in HFI; America; partial activity).`	`VAR_000551 [3D]`
`VARIANT`	`148 148`	`1`	`W -> R (in one subject with fructose intolerance; rare variant; America).`	`VAR_000552 [3D]`
`VARIANT`	`150 150`	`1`	`A -> P (in HFI; frequent mutation; dbSNP:rs1800546 [NCBI]).`	`VAR_000553 [3D]`
`VARIANT`	`175 175`	`1`	`A -> D (in HFI; frequent mutation).`	`VAR_000554 [3D]`
`VARIANT`	`185 185`	`1`	`P -> R (in HFI).`	`VAR_020824 [3D]`
`VARIANT`	`207 207`	`1`	`E -> Q (in dbSNP:rs3739721 [NCBI]).`	`VAR_020825 [3D]`
`VARIANT`	`222 222`	`1`	`V -> F (in HFI; affects proper folding).`	`VAR_020826 [3D]`
`VARIANT`	`229 229`	`1`	`L -> P (in HFI; affects proper folding).`	`VAR_020827 [3D]`
`VARIANT`	`257 257`	`1`	`L -> P (in HFI; Italy).`	`VAR_000555 [3D]`
`VARIANT`	`268 268`	`1`	`I -> N (in dbSNP:rs10989495 [NCBI]).`	`VAR_038430 [3D]`
`VARIANT`	`304 304`	`1`	`R -> Q (in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P).`	`VAR_020828 [3D]`
`VARIANT`	`304 304`	`1`	`R -> W (in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P).`	`VAR_000556 [3D]`
`VARIANT`	`335 335`	`1`	`N -> K (in HFI; frequent mutation).`	`VAR_000557 [3D]`
`VARIANT`	`338 338`	`1`	`A -> V (in HFI; Turkey and South Europe).`	`VAR_000558 [3D]`
`CONFLICT`	`54 54`		`E -> D (in Ref. 5; AAA51691).`
`CONFLICT`	`250 250`		`A -> D (in Ref. 7; CAA25072).`
`CONFLICT`	`278 278`		`E -> D (in Ref. 4; BAA00125).`
`CONFLICT`	`309 309`		`S -> V (in Ref. 3).`
`CONFLICT`	`348 348`		`S -> C (in Ref. 4; BAA00125).`
`HELIX`	`10 23`	`14`
`STRAND`	`29 33`	`5`
`HELIX`	`37 46`	`10`
`HELIX`	`53 64`	`12`
`HELIX`	`68 72`	`5`
`STRAND`	`74 79`	`6`
`HELIX`	`83 85`	`3`
`HELIX`	`94 100`	`7`
`STRAND`	`104 108`	`5`
`STRAND`	`113 115`	`3`
`STRAND`	`119 121`	`3`
`STRAND`	`123 125`	`3`
`HELIX`	`131 140`	`10`
`STRAND`	`145 152`	`8`
`HELIX`	`161 179`	`19`
`TURN`	`180 182`	`3`
`STRAND`	`184 191`	`8`
`HELIX`	`199 219`	`21`
`HELIX`	`224 226`	`3`
`HELIX`	`246 260`	`15`
`STRAND`	`267 271`	`5`
`HELIX`	`277 289`	`13`
`STRAND`	`296 303`	`8`
`HELIX`	`304 306`	`3`
`HELIX`	`308 314`	`7`
`HELIX`	`318 320`	`3`
`HELIX`	`321 338`	`18`
`TURN`	`339 341`	`3`
`HELIX`	`351 354`	`4`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39473 Da [This is the MW of the unprocessed precursor]

CRC64: DCE314E7AC5586CA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

        70         80         90        100        110        120 
EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN 

       130        140        150        160        170        180 
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ 

       190        200        210        220        230        240 
NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 

       250        260        270        280        290        300 
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF 

       310        320        330        340        350        360 
SYGRALQASA LAAWGGKAAN KEATQEAFMK RAMANCQAAK GQYVHTGSSG AASTQSLFTA 


CYTY

P05062 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools