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Reviewed, UniProtKB/Swiss-Prot P79226 (ALDOB_RABIT)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Synonyms: ALDB
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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.

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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 364363Fructose-bisphosphate aldolase B
PRO_0000216942

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 residue361Phosphoserine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P79226-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 65A58A50906EA954

FASTA36439,605
        10         20         30         40         50         60 
MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

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

       130        140        150        160        170        180 
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANT 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 LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG AASTQSLFTA 


SYTY 

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References

[1]"Identification of conserved promoter elements for aldB and isozyme specific residues in aldolase B."
Berardini T.Z., Amsden A.B., Penhoet E.E., Tolan D.R.
Comp. Biochem. Physiol. 122B:53-61(1999) [PubMed: 10327593] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Enhanced electron-density envelopes by extended solvent definition."
Blom N., Sygush J.
Acta Crystallogr. D 54:461-466(1998) [PubMed: 9761929] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

U85645 Genomic DNA. Translation: AAB42087.1.
PIRA28856.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FDJX-ray2.10A/B/C/D2-363[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSOCUG00000014944. Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGENP79226.

Enzyme and pathway databases

BRENDA4.1.2.13. 255.

Family and domain databases

InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11627. Aldolase_I. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
ProDomPD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDOB_RABIT
AccessionPrimary (citable) accession number: P79226
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents