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

P79226 (ALDOB_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 92. 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
Synonyms:ALDB
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
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. 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.

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P79226 [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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85645 Genomic DNA. Translation: AAB42087.1.
PIRA28856.
RefSeqNP_001164585.1. NM_001171114.1.
UniGeneOcu.4530.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FDJX-ray2.10A/B/C/D2-363[»]
ProteinModelPortalP79226.
SMRP79226. Positions 2-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000012843.

Proteomic databases

PRIDEP79226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000014943; ENSOCUP00000012843; ENSOCUG00000014944.
GeneID100328925.

Organism-specific databases

CTD229.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
OMADMEHCQY.
OrthoDBEOG744T94.
TreeFamTF314203.

Enzyme and pathway databases

SABIO-RKP79226.
UniPathwayUPA00109; UER00183.

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...

Other

EvolutionaryTraceP79226.

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: March 19, 2014
This is version 92 of the entry and version 3 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