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

Q8JH70 (ALDCB_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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 C-B

EC=4.1.2.13
Alternative name(s):
Brain-type aldolase-B
Gene names
Name:aldocb
Synonyms:aldoc
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length363 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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 363362Fructose-bisphosphate aldolase C-B
PRO_0000291612

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site561Substrate By similarity
Binding site1471Substrate By similarity
Site3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8JH70 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 84D269B36579E6A0

FASTA36339,259
        10         20         30         40         50         60 
MTHQYPALTA EQKKELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QLLFSADERI DKCIGGVIFF HETLYQNTDD GTNFAQLIKD RGIVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRS VLKISDTTPS ELAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGEHDLK RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC 

       250        260        270        280        290        300 
PTKYSSEEIA MATVTALRRT VPPAVSGVTF LSGGQSEEEA SVNLNSINNC PLAKPWPLTF 

       310        320        330        340        350        360 
SYGRALQASA LSAWRGAKSN EKAATEEFIK RAEANGLAAQ GKYVSSGTCG AAGQSLYVAN 


HAY 

« Hide

References

« Hide 'large scale' references
[1]"Negative charge correlates with neural expression in vertebrate aldolase isozymes."
Merritt T.J.S., Quattro J.M.
J. Mol. Evol. 55:674-683(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF533647 mRNA. Translation: AAN04478.1.
BC053192 mRNA. Translation: AAH53192.1.
RefSeqNP_919365.1. NM_194384.1.
UniGeneDr.19223.

3D structure databases

ProteinModelPortalQ8JH70.
SMRQ8JH70. Positions 3-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000024492.

Proteomic databases

PRIDEQ8JH70.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000026766; ENSDARP00000024492; ENSDARG00000019702.
GeneID369193.
KEGGdre:369193.

Organism-specific databases

CTD369193.
ZFINZDB-GENE-030821-1. aldocb.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidQ8JH70.
KOK01623.
OMARGQQDNA.
OrthoDBEOG744T94.
PhylomeDBQ8JH70.
TreeFamTF314203.

Enzyme and pathway databases

UniPathwayUPA00109; UER00183.

Gene expression databases

BgeeQ8JH70.

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

NextBio20813343.
PROQ8JH70.

Entry information

Entry nameALDCB_DANRE
AccessionPrimary (citable) accession number: Q8JH70
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 78 of the entry and version 1 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