Fructose-bisphosphate aldolase A - Mus musculus (Mouse)

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P05064 (ALDOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase A
EC=4.1.2.13

Alternative name(s):
Aldolase 1
Muscle-type aldolase

Gene names

Name:	Aldoa
Synonyms:	Aldo1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Nitration Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from sequence or structural similarity. Source: UniProtKB protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Z disc Inferred from direct assay PubMed 18676612. Source: UniProtKB membrane Inferred from direct assay PubMed 18676612. Source: UniProtKB protein complex Inferred from direct assay PubMed 18676612. Source: UniProtKB
Molecular_function	fructose-bisphosphate aldolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 364

363

Fructose-bisphosphate aldolase A

PRO_0000216937

Sites

Active site

188

Proton acceptor By similarity

Active site

230

Schiff-base intermediate with dihydroxyacetone-P

Binding site

Substrate

Binding site

147

Substrate

Site

364

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine Ref.6 Ref.8

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine Ref.8

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphothreonine By similarity

Modified residue

108

N6-acetyllysine By similarity

Modified residue

111

N6-malonyllysine By similarity

Modified residue

174

Nitrated tyrosine Ref.7

Modified residue

204

Phosphotyrosine By similarity

Modified residue

223

Phosphotyrosine By similarity

Modified residue

235

Phosphothreonine By similarity

Modified residue

241

Phosphothreonine By similarity

Modified residue

312

N6-malonyllysine By similarity

Modified residue

330

N6-acetyllysine By similarity

Modified residue

354

Phosphoserine By similarity

Modified residue

356

Phosphoserine By similarity

Modified residue

364

Phosphotyrosine By similarity

Experimental info

Sequence conflict

281

S → C in CAA27423. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P05064 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0D067F7E4C63E216
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FASTA

364

39,356

        10         20         30         40         50         60 
MPHPYPALTP EQKKELSDIA 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 ALAIMENANV LARYASICQQ 

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

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

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


NHAY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of a mouse brain aldolase A cDNA." Mestek A., Stauffer J., Tolan D.R., Ciejek-Baez E. Nucleic Acids Res. 15:10595-10595(1987) [PubMed] [Europe PMC] [Abstract] 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, 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.
[6]	"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[7]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-174, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Melanoma.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00221402.
PIR	ADMSA. S06323.
RefSeq	NP_001170779.1. NM_001177308.1. NP_031464.1. NM_007438.4.
UniGene	Mm.275831.
3D structure databases
ProteinModelPortal	P05064.
SMR	P05064. Positions 5-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05064. 17 interactions.
PTM databases
PhosphoSite	P05064.
2D gel databases
COMPLUYEAST-2DPAGE	P05064.
REPRODUCTION-2DPAGE	IPI00221402. P05064.
SWISS-2DPAGE	P05064.
Proteomic databases
PaxDb	P05064.
PRIDE	P05064.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695. ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
GeneID	11674.
KEGG	mmu:11674.
Organism-specific databases
CTD	226.
MGI	MGI:87994. Aldoa.
Phylogenomic databases
eggNOG	COG3588.
HOGENOM	HOG000220876.
HOVERGEN	HBG002386.
InParanoid	P05064.
KO	K01623.
OrthoDB	EOG4X3H1J.
Enzyme and pathway databases
SABIO-RK	P05064.
UniPathway	UPA00109; UER00183.
Gene expression databases
ArrayExpress	P05064.
Bgee	P05064.
CleanEx	MM_ALDOA.
Genevestigator	P05064.
GermOnline	ENSMUSG00000030695. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
PANTHER	PTHR11627. PTHR11627. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ALDOA. mouse.
NextBio	279303.
SOURCE	Search...

Entry information

Entry name

ALDOA_MOUSE

Accession

Primary (citable) accession number: P05064

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents