Fructose-bisphosphate aldolase A - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

P05065 (ALDOA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 120. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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):
Muscle-type aldolase

Gene names

Name:

Aldoa

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation 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 response to estrogen stimulus Inferred from expression pattern PubMed 16339744. Source: RGD response to heat Inferred from expression pattern PubMed 10395295. Source: RGD response to hypoxia Inferred from expression pattern PubMed 16930621. Source: RGD response to lipopolysaccharide Inferred from expression pattern PubMed 16930621. Source: RGD response to nicotine Inferred from expression pattern PubMed 16622831. Source: RGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 18384645. Source: RGD
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 By similarity

Chain

2 – 364

363

Fructose-bisphosphate aldolase A

PRO_0000216939

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 By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

108

N6-acetyllysine By similarity

Modified residue

111

N6-malonyllysine By similarity

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

145

F → S in AAA40715. Ref.2

Sequence conflict

165

M → V in AAA40715. Ref.2

Sequence conflict

330

K → Q in AAA40720. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P05065 [UniParc].

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

FASTA

364

39,352

        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' referencesShow '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, 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 , X04262, X04263, X04264 Genomic DNA. Translation: CAA27815.1. BC064440 mRNA. Translation: AAH64440.1. M28282 mRNA. Translation: AAA40720.1.
IPI	IPI00231734.
PIR	ADRTA. A24532.
RefSeq	NP_001170776.1. NM_001177305.1. NP_001258465.1. NM_001271536.1. NP_036627.1. NM_012495.2.
UniGene	Rn.1774.
3D structure databases
ProteinModelPortal	P05065.
SMR	P05065. Positions 5-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05065. 3 interactions.
MINT	MINT-4567674.
STRING	10116.ENSRNOP00000031940.
PTM databases
PhosphoSite	P05065.
2D gel databases
World-2DPAGE	0004:P05065.
Proteomic databases
PaxDb	P05065.
PRIDE	P05065.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000032362; ENSRNOP00000032320; ENSRNOG00000023647.
GeneID	24189.
KEGG	rno:24189.
UCSC	RGD:2089. rat.
Organism-specific databases
CTD	226.
RGD	2089. Aldoa.
Phylogenomic databases
eggNOG	COG3588.
GeneTree	ENSGT00390000010235.
HOGENOM	HOG000220876.
HOVERGEN	HBG002386.
InParanoid	P05065.
KO	K01623.
OMA	AHLSAMN.
OrthoDB	EOG4X3H1J.
Enzyme and pathway databases
SABIO-RK	P05065.
UniPathway	UPA00109; UER00183.
Gene expression databases
Genevestigator	P05065.
GermOnline	ENSRNOG00000023647. Rattus norvegicus.
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
NextBio	602559.

Entry information

Entry name

ALDOA_RAT

Accession

Primary (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:	May 29, 2013
This is version 120 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

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