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

P05065 (ALDOA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase A

EC=4.1.2.13
Alternative name(s):
Muscle-type aldolase
Gene names
Name:Aldoa
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)

Function

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein By similarity.

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 SNX9 and WAS By similarity.

Tissue specificity

Expressed in muscle, brain and hepatoma cells. Ref.6

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ppm1eQ80Z302EBI-522118,EBI-7473061

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 364363Fructose-bisphosphate aldolase A
PRO_0000216939

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 residue361Phosphoserine By similarity
Modified residue391Phosphoserine By similarity
Modified residue421N6-acetyllysine By similarity
Modified residue461Phosphoserine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1111N6-malonyllysine By similarity
Modified residue3121N6-malonyllysine By similarity
Modified residue3301N6-acetyllysine By similarity

Experimental info

Sequence conflict1451F → S in AAA40715. Ref.2
Sequence conflict1651M → V in AAA40715. Ref.2
Sequence conflict3301K → Q in AAA40720. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P05065 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2774497C20DCC0DA

FASTA36439,352
        10         20         30         40         50         60 
MPHPYPALTP EQKKELADIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR 

        70         80         90        100        110        120 
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS SLAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
TQKFSNEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG AAASESLFIS 


NHAY 

« Hide

References

« Hide 'large scale' references
[1]"Tissue-specific expression of rat aldolase A mRNAs. Three molecular species differing only in the 5'-terminal sequences."
Mukai T., Joh K., Arai Y., Yatsuki H., Hori K.
J. Biol. Chem. 261:3347-3354(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat aldolase A messenger RNA: the nucleotide sequence and multiple mRNA species with different 5'-terminal regions."
Joh K., Mukai T., Yatsuki H., Hori K.
Gene 39:17-24(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Expression of three mRNA species from a single rat aldolase A gene, differing in their 5' non-coding regions."
Joh K., Arai Y., Mukai T., Hori K.
J. Mol. Biol. 190:401-410(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[5]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 15-22; 29-42; 70-99; 154-173; 209-215; 244-258; 290-312 AND 332-364, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[6]"Two different aldolase A mRNA species in rat tissues."
Tsutsumi R., Tsutsumi K., Numazaki M., Ishikawa K.
Eur. J. Biochem. 142:161-164(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 324-356, TISSUE SPECIFICITY.
Strain: Donryu.
Tissue: Hepatoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12919 mRNA. Translation: AAA40714.1.
M14420 mRNA. Translation: AAA40715.1.
X04261 expand/collapse EMBL AC list , X04262, X04263, X04264 Genomic DNA. Translation: CAA27815.1.
BC064440 mRNA. Translation: AAH64440.1.
M28282 mRNA. Translation: AAA40720.1.
PIRADRTA. A24532.
RefSeqNP_001170776.1. NM_001177305.1.
NP_001258465.1. NM_001271536.1.
NP_036627.1. NM_012495.2.
XP_006230273.1. XM_006230211.1.
UniGeneRn.1774.

3D structure databases

ProteinModelPortalP05065.
SMRP05065. Positions 5-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246379. 3 interactions.
IntActP05065. 6 interactions.
MINTMINT-4567674.
STRING10116.ENSRNOP00000031940.

PTM databases

PhosphoSiteP05065.

2D gel databases

World-2DPAGE0004:P05065.

Proteomic databases

PaxDbP05065.
PRIDEP05065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000032362; ENSRNOP00000032320; ENSRNOG00000023647.
GeneID24189.
KEGGrno:24189.
UCSCRGD:2089. rat.

Organism-specific databases

CTD226.
RGD2089. Aldoa.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.
InParanoidP05065.
KOK01623.
OMAPNMVIDG.
OrthoDBEOG744T94.
PhylomeDBP05065.

Enzyme and pathway databases

SABIO-RKP05065.
UniPathwayUPA00109; UER00183.

Gene expression databases

ArrayExpressP05065.
GenevestigatorP05065.

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

NextBio602559.
PROP05065.

Entry information

Entry nameALDOA_RAT
AccessionPrimary (citable) accession number: P05065
Secondary accession number(s): Q63038
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 128 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

PATHWAY comments

Index of metabolic and biosynthesis pathways