Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00884 (ALDOB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase B

EC=4.1.2.13
Alternative name(s):
Liver-type aldolase
Gene names
Name:Aldob
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7 By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity.

Miscellaneous

In vertebrates, 3 forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
Cytoskeleton
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to extracellular stimulus

Inferred from expression pattern PubMed 15770659. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern PubMed 9473304. Source: RGD

glycolytic process

Inferred from direct assay PubMed 8255543. Source: RGD

liver development

Inferred from expression pattern PubMed 8641049. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 2984252. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 2984252. Source: RGD

response to carbohydrate

Inferred from expression pattern PubMed 6689021. Source: RGD

response to copper ion

Inferred from expression pattern PubMed 11044632. Source: RGD

response to drug

Inferred from expression pattern PubMed 12387752. Source: RGD

response to fructose

Inferred from expression pattern PubMed 2984252. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 9473304. Source: RGD

response to interleukin-6

Inferred from expression pattern PubMed 7625825. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 9020521. Source: RGD

response to peptide hormone

Inferred from direct assay PubMed 10775441. Source: RGD

response to starvation

Inferred from expression pattern PubMed 9886486. Source: RGD

response to zinc ion

Inferred from direct assay PubMed 12721403. Source: RGD

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 201371. Source: RGD

cytosol

Inferred from direct assay PubMed 9886486. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 15683743. Source: RGD

lysosome

Inferred from direct assay PubMed 9886486. Source: RGD

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 10797566. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10797566. Source: RGD

plasma membrane

Inferred from direct assay PubMed 10797566. Source: RGD

rough endoplasmic reticulum membrane

Inferred from direct assay PubMed 234468. Source: RGD

smooth endoplasmic reticulum membrane

Inferred from direct assay PubMed 234468. Source: RGD

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from direct assay PubMed 8255543PubMed 9448062. Source: RGD

phosphatidylcholine binding

Inferred from physical interaction PubMed 9448062. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 364363Fructose-bisphosphate aldolase B
PRO_0000216943

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue131N6-succinyllysine By similarity
Modified residue361Phosphoserine By similarity
Modified residue391Phosphothreonine By similarity
Modified residue1211N6-succinyllysine By similarity
Modified residue3171N6-succinyllysine By similarity

Experimental info

Sequence conflict2341L → V in CAA26156. Ref.2

Secondary structure

........................................................ 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00884 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E120FC119F0180F8

FASTA36439,618
        10         20         30         40         50         60 
MAHRFPALTS EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

        70         80         90        100        110        120 
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN 

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

       190        200        210        220        230        240 
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMLTAGHAC 

       250        260        270        280        290        300 
TKKYTPEQVA MATVTALHRT VPAAVPSICF LSGGMSEEDA TLNLNAIYRC PLPRPWKLSF 

       310        320        330        340        350        360 
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAVANCQAAQ GQYVHTGSSG AASTQSLFTA 


SYTY 

« Hide

References

[1]"Nucleotide sequence of rat liver aldolase B messenger RNA."
Tsutsumi K., Mukai T., Tsutsumi R., Mori M., Daimon M., Tanaka T., Yatsuki H., Hori K., Ishikawa K.
J. Biol. Chem. 259:14572-14575(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and genomic organization of the rat aldolase B gene."
Tsutsumi K., Mukai T., Tsutsumi R., Hidaka S., Arai Y., Hori K., Ishikawa K.
J. Mol. Biol. 181:153-160(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
[3]"Rat aldolase isozyme gene."
Tsutsumi K., Mukai T., Hidaka S., Miyahara H., Tsutsumi R., Tanaka T., Hori K., Ishikawa K.
J. Biol. Chem. 258:6537-6542(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 185-364.
[4]"Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa Zn(2+)-binding protein (parathymosin)."
Brand I.A., Heinickel A.
J. Biol. Chem. 266:20984-20989(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-68.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10149 mRNA. Translation: AAA40716.1.
X02284 expand/collapse EMBL AC list , X02285, X02286, X02287, X02288, X02289, X02290, X02291 Genomic DNA. Translation: CAA26156.1.
V01223 mRNA. Translation: CAA24533.1.
PIRADRTB. A22585.
UniGeneRn.98207.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N30model-A1-364[»]
ProteinModelPortalP00884.
SMRP00884. Positions 2-360.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00884. 1 interaction.
MINTMINT-3376760.

PTM databases

PhosphoSiteP00884.

Proteomic databases

PaxDbP00884.
PRIDEP00884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2090. rat.

Organism-specific databases

RGD2090. Aldob.

Phylogenomic databases

eggNOGCOG3588.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP00884.
PhylomeDBP00884.

Enzyme and pathway databases

SABIO-RKP00884.
UniPathwayUPA00109; UER00183.

Gene expression databases

GenevestigatorP00884.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDOB_RAT
AccessionPrimary (citable) accession number: P00884
Secondary accession number(s): P70706
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways