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Protein

Fructose-bisphosphate aldolase A

Gene

Aldoa

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (Gpi), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gpi1), Glucose-6-phosphate isomerase (Gm1840)
  3. ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm)
  4. Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoart1), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldoa), Fructose-bisphosphate aldolase (Aldob), Fructose-bisphosphate aldolase C (Aldoc), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase (Aldob)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: UniProtKB
  • protease binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_307071. Platelet degranulation.
REACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP05064.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase A (EC:4.1.2.13)
Alternative name(s):
Aldolase 1
Muscle-type aldolase
Gene namesi
Name:Aldoa
Synonyms:Aldo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:87994. Aldoa.

Subcellular locationi

GO - Cellular componenti

  • M band Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • myelin sheath Source: UniProtKB
  • protein complex Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei111 – 1111N6-malonyllysineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei312 – 3121N6-malonyllysineBy similarity
Modified residuei330 – 3301N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05064.
PaxDbiP05064.
PRIDEiP05064.

2D gel databases

COMPLUYEAST-2DPAGEP05064.
REPRODUCTION-2DPAGEIPI00221402.
P05064.
SWISS-2DPAGEP05064.

PTM databases

PhosphoSiteiP05064.

Expressioni

Gene expression databases

BgeeiP05064.
CleanExiMM_ALDOA.
ExpressionAtlasiP05064. baseline and differential.
GenevisibleiP05064. MM.

Interactioni

Subunit structurei

Homotetramer. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+ (By similarity).By similarity

Protein-protein interaction databases

BioGridi198067. 9 interactions.
IntActiP05064. 22 interactions.
MINTiMINT-1581489.
STRINGi10090.ENSMUSP00000084846.

Structurei

3D structure databases

ProteinModelPortaliP05064.
SMRiP05064. Positions 5-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05064.
OrthoDBiEOG744T94.
PhylomeDBiP05064.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05064-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHPYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
60 70 80 90 100
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS
110 120 130 140 150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC TQKFSNEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG
360
AAASESLFIS NHAY
Length:364
Mass (Da):39,356
Last modified:January 23, 2007 - v2
Checksum:i0D067F7E4C63E216
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811S → C in CAA27423 (PubMed:3009179).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03797 mRNA. Translation: CAA27423.1.
BC043026 mRNA. Translation: AAH43026.1.
BC050896 mRNA. Translation: AAH50896.1.
J05517 Genomic DNA. Translation: AAA37210.2.
Y00516 mRNA. Translation: CAA68571.1.
CCDSiCCDS21845.1.
PIRiS06323. ADMSA.
RefSeqiNP_001170779.1. NM_001177308.1.
NP_031464.1. NM_007438.4.
XP_006507273.1. XM_006507210.2.
XP_006507274.1. XM_006507211.2.
UniGeneiMm.275831.

Genome annotation databases

EnsembliENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695.
ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
GeneIDi11674.
UCSCiuc009jsu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03797 mRNA. Translation: CAA27423.1.
BC043026 mRNA. Translation: AAH43026.1.
BC050896 mRNA. Translation: AAH50896.1.
J05517 Genomic DNA. Translation: AAA37210.2.
Y00516 mRNA. Translation: CAA68571.1.
CCDSiCCDS21845.1.
PIRiS06323. ADMSA.
RefSeqiNP_001170779.1. NM_001177308.1.
NP_031464.1. NM_007438.4.
XP_006507273.1. XM_006507210.2.
XP_006507274.1. XM_006507211.2.
UniGeneiMm.275831.

3D structure databases

ProteinModelPortaliP05064.
SMRiP05064. Positions 5-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198067. 9 interactions.
IntActiP05064. 22 interactions.
MINTiMINT-1581489.
STRINGi10090.ENSMUSP00000084846.

PTM databases

PhosphoSiteiP05064.

2D gel databases

COMPLUYEAST-2DPAGEP05064.
REPRODUCTION-2DPAGEIPI00221402.
P05064.
SWISS-2DPAGEP05064.

Proteomic databases

MaxQBiP05064.
PaxDbiP05064.
PRIDEiP05064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695.
ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
GeneIDi11674.
UCSCiuc009jsu.2. mouse.

Organism-specific databases

CTDi226.
MGIiMGI:87994. Aldoa.

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05064.
OrthoDBiEOG744T94.
PhylomeDBiP05064.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiREACT_307071. Platelet degranulation.
REACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP05064.

Miscellaneous databases

ChiTaRSiAldoa. mouse.
NextBioi279303.
PROiP05064.
SOURCEiSearch...

Gene expression databases

BgeeiP05064.
CleanExiMM_ALDOA.
ExpressionAtlasiP05064. baseline and differential.
GenevisibleiP05064. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  3. "Nonconservative utilization of aldolase A alternative promoters."
    Stauffer J.K., Colbert M.C., Ciejek-Baez E.
    J. Biol. Chem. 265:11773-11782(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266 AND 295-364.
  4. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-22; 29-57; 61-109; 112-134; 154-258; 260-312 AND 323-364, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Structure and expression of mouse aldolase genes. Brain-specific aldolase C amino acid sequence is closely related to aldolase A."
    Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.
    Eur. J. Biochem. 156:229-235(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-355.

Entry informationi

Entry nameiALDOA_MOUSE
AccessioniPrimary (citable) accession number: P05064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.