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Protein

Fructose-bisphosphate aldolase A

Gene

Aldoa

Organism
Rattus norvegicus (Rat)
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)
  3. ATP-dependent 6-phosphofructokinase (Pfkm), ATP-dependent 6-phosphofructokinase, liver type (Pfkl), ATP-dependent 6-phosphofructokinase, platelet type (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkp), ATP-dependent 6-phosphofructokinase (Pfkl), ATP-dependent 6-phosphofructokinase, muscle type (Pfkm), ATP-dependent 6-phosphofructokinase (Pfkp)
  4. Fructose-bisphosphate aldolase (LOC100912010), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (Aldoart2), Fructose-bisphosphate aldolase A (Aldoa), Fructose-bisphosphate aldolase B (Aldob), Fructose-bisphosphate aldolase C (Aldoc), 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

GO - Biological processi

  • glycolytic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
  • response to estrogen Source: RGD
  • response to heat Source: RGD
  • response to hypoxia Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to nicotine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

ReactomeiREACT_288006. Platelet degranulation.
REACT_331968. Gluconeogenesis.
REACT_342181. Glycolysis.
SABIO-RKP05065.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase A (EC:4.1.2.13)
Alternative name(s):
Muscle-type aldolase
Gene namesi
Name:Aldoa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unassembled WGS sequence

Organism-specific databases

RGDi2089. Aldoa.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • I band Source: UniProtKB-SubCell
  • M band Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216939Add
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

PaxDbiP05065.
PRIDEiP05065.

2D gel databases

World-2DPAGE0004:P05065.

PTM databases

PhosphoSiteiP05065.

Expressioni

Tissue specificityi

Expressed in muscle, brain and hepatoma cells.1 Publication

Gene expression databases

GenevisibleiP05065. RN.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppm1eQ80Z302EBI-522118,EBI-7473061

Protein-protein interaction databases

BioGridi246379. 3 interactions.
IntActiP05065. 6 interactions.
MINTiMINT-4567674.
STRINGi10116.ENSRNOP00000032320.

Structurei

3D structure databases

ProteinModelPortaliP05065.
SMRiP05065. Positions 5-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05065.
KOiK01623.
OMAiPNMVIDG.
OrthoDBiEOG744T94.
PhylomeDBiP05065.

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.

P05065-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHPYPALTP EQKKELADIA 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 SLAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC TQKFSNEEIA
260 270 280 290 300
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG
360
AAASESLFIS NHAY
Length:364
Mass (Da):39,352
Last modified:January 23, 2007 - v2
Checksum:i2774497C20DCC0DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451F → S in AAA40715 (PubMed:2416636).Curated
Sequence conflicti165 – 1651M → V in AAA40715 (PubMed:2416636).Curated
Sequence conflicti330 – 3301K → Q in AAA40720 (PubMed:6086339).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA24532. ADRTA.
RefSeqiNP_001170776.1. NM_001177305.1.
NP_001258465.1. NM_001271536.1.
NP_036627.1. NM_012495.2.
XP_006230273.1. XM_006230211.1.
UniGeneiRn.1774.

Genome annotation databases

EnsembliENSRNOT00000080988; ENSRNOP00000068764; ENSRNOG00000052802.
ENSRNOT00000087928; ENSRNOP00000069507; ENSRNOG00000052802.
ENSRNOT00000088473; ENSRNOP00000069540; ENSRNOG00000052802.
GeneIDi24189.
KEGGirno:24189.
UCSCiRGD:2089. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA24532. ADRTA.
RefSeqiNP_001170776.1. NM_001177305.1.
NP_001258465.1. NM_001271536.1.
NP_036627.1. NM_012495.2.
XP_006230273.1. XM_006230211.1.
UniGeneiRn.1774.

3D structure databases

ProteinModelPortaliP05065.
SMRiP05065. Positions 5-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246379. 3 interactions.
IntActiP05065. 6 interactions.
MINTiMINT-4567674.
STRINGi10116.ENSRNOP00000032320.

PTM databases

PhosphoSiteiP05065.

2D gel databases

World-2DPAGE0004:P05065.

Proteomic databases

PaxDbiP05065.
PRIDEiP05065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000080988; ENSRNOP00000068764; ENSRNOG00000052802.
ENSRNOT00000087928; ENSRNOP00000069507; ENSRNOG00000052802.
ENSRNOT00000088473; ENSRNOP00000069540; ENSRNOG00000052802.
GeneIDi24189.
KEGGirno:24189.
UCSCiRGD:2089. rat.

Organism-specific databases

CTDi226.
RGDi2089. Aldoa.

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05065.
KOiK01623.
OMAiPNMVIDG.
OrthoDBiEOG744T94.
PhylomeDBiP05065.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
ReactomeiREACT_288006. Platelet degranulation.
REACT_331968. Gluconeogenesis.
REACT_342181. Glycolysis.
SABIO-RKP05065.

Miscellaneous databases

NextBioi602559.
PROiP05065.

Gene expression databases

GenevisibleiP05065. RN.

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. "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.

Entry informationi

Entry nameiALDOA_RAT
AccessioniPrimary (citable) accession number: P05065
Secondary accession number(s): Q63038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 139 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.