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Q5RFA6 (ALDOB_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity. 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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-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_0000230296

Sites

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

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

Sequences

Sequence LengthMass (Da)Tools
Q5RFA6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 992D2580A7F34CB9

FASTA36439,447
        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 AAAYKALNDH HVYLEGTLLK PNMVTAGHAC 

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

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


CYTY 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857255 mRNA. Translation: CAH89551.1.
RefSeqNP_001127166.1. NM_001133694.1.

3D structure databases

ProteinModelPortalQ5RFA6.
SMRQ5RFA6. Positions 2-361.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174217.
KEGGpon:100174217.

Organism-specific databases

CTD229.

Phylogenomic databases

HOVERGENHBG002386.
InParanoidQ5RFA6.
KOK01623.

Enzyme and pathway databases

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...

Entry information

Entry nameALDOB_PONAB
AccessionPrimary (citable) accession number: Q5RFA6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 58 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

PATHWAY comments

Index of metabolic and biosynthesis pathways