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Protein

Fructose-bisphosphate aldolase A

Gene

ALDOA

Organism
Oryctolagus cuniculus (Rabbit)
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.1 Publication

Catalytic activityi

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

Pathwayi: glycolysis

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 (GPI)
  3. ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM)
  4. Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA)
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)DescriptionActionsGraphical viewLength
Binding sitei43SubstrateCombined sources1 Publication1
Sitei73Essential for substrate cleavage1
Sitei108Essential for substrate cleavage1
Sitei147Alkylation inactivates the enzyme1
Active sitei188Proton acceptor1 Publication1
Active sitei230Schiff-base intermediate with dihydroxyacetone-P1 Publication1
Binding sitei304SubstrateCombined sources1 Publication1
Sitei362Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base1
Sitei364Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate1

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: UniProtKB

GO - Biological processi

  • glycolytic process Source: UniProtKB
  • protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BRENDAi4.1.2.13. 1749.
SABIO-RKP00883.
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35E → A: Reduces activity 14-fold. 1 Publication1
Mutagenesisi43R → A: Reduces activity 14-fold. 1 Publication1
Mutagenesisi129D → V: Alters protein-protein interactions, leading to a dimeric protein. 1
Mutagenesisi147K → A: Loss of activity. 1 Publication1
Mutagenesisi188E → A: Reduces activity over 100-fold. 1 Publication1
Mutagenesisi188E → Q: Reduces activity over 1000-fold. 1 Publication1
Mutagenesisi190E → Q: Reduces activity 20-fold. 1 Publication1
Mutagenesisi230K → M: Loss of activity. 1 Publication1
Mutagenesisi304R → A: Reduces activity 400-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002169382 – 364Fructose-bisphosphate aldolase AAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphothreonineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei39PhosphoserineBy similarity1
Modified residuei42N6-acetyllysine; alternateBy similarity1
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei46PhosphoserineBy similarity1
Modified residuei108N6-acetyllysineBy similarity1
Modified residuei111N6-malonyllysineBy similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei272PhosphoserineBy similarity1
Modified residuei312N6-malonyllysineBy similarity1
Modified residuei330N6-acetyllysineBy similarity1
Modified residuei361Deamidated asparagine; in form beta1 Publication1

Post-translational modificationi

Asn-361 in form alpha is deaminated to Asp in form beta.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP00883.

PTM databases

iPTMnetiP00883.

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+.6 Publications

Protein-protein interaction databases

BioGridi1172078. 2 interactors.
IntActiP00883. 1 interactor.
MINTiMINT-7995296.
STRINGi9986.ENSOCUP00000020204.

Chemistry databases

BindingDBiP00883.

Structurei

Secondary structure

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 23Combined sources14
Beta strandi29 – 33Combined sources5
Helixi37 – 45Combined sources9
Turni46 – 48Combined sources3
Helixi53 – 64Combined sources12
Helixi68 – 70Combined sources3
Turni71 – 73Combined sources3
Beta strandi74 – 79Combined sources6
Helixi81 – 84Combined sources4
Turni89 – 91Combined sources3
Helixi94 – 99Combined sources6
Turni100 – 102Combined sources3
Beta strandi104 – 108Combined sources5
Beta strandi113 – 115Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi123 – 125Combined sources3
Helixi131 – 140Combined sources10
Beta strandi145 – 152Combined sources8
Beta strandi155 – 157Combined sources3
Helixi161 – 180Combined sources20
Beta strandi184 – 191Combined sources8
Helixi199 – 219Combined sources21
Helixi224 – 226Combined sources3
Helixi246 – 258Combined sources13
Beta strandi267 – 270Combined sources4
Helixi277 – 289Combined sources13
Beta strandi290 – 292Combined sources3
Beta strandi296 – 303Combined sources8
Helixi304 – 314Combined sources11
Helixi318 – 320Combined sources3
Helixi321 – 338Combined sources18
Turni339 – 341Combined sources3
Beta strandi345 – 347Combined sources3
Helixi351 – 354Combined sources4
Beta strandi358 – 360Combined sources3
Helixi361 – 363Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ADOX-ray1.90A/B/C/D2-364[»]
1EWDX-ray2.46A/B/C/D2-364[»]
1EWEX-ray2.60A/B/C/D2-364[»]
1EX5X-ray2.20A/B/C/D2-364[»]
1J4EX-ray2.65A/B/C/D2-364[»]
1ZAHX-ray1.80A/B/C/D2-364[»]
1ZAIX-ray1.76A/B/C/D2-364[»]
1ZAJX-ray1.89A/B/C/D2-364[»]
1ZALX-ray1.89A/B/C/D2-364[»]
2OT0X-ray2.05A/B/C/D2-364[»]
2OT1X-ray2.05A/B/C/D2-364[»]
2QUTX-ray1.88A/B/C/D2-364[»]
2QUUX-ray1.98A/B/C/D2-364[»]
2QUVX-ray2.22A/B/C/D2-364[»]
3B8DX-ray2.00A/B/C/D2-364[»]
3BV4X-ray1.70A5-344[»]
3DFNX-ray1.86A/B/C/D2-364[»]
3DFOX-ray1.94A/B/C/D2-364[»]
3DFPX-ray2.05A/B/C/D2-364[»]
3DFQX-ray1.82A/B/C/D2-364[»]
3DFSX-ray2.03A/B/C/D2-364[»]
3DFTX-ray1.94A/B/C/D2-364[»]
3LGEX-ray2.20A/B/C/D2-364[»]
3TU9X-ray2.09A/B/C/D2-364[»]
6ALDX-ray2.30A/B/C/D2-364[»]
ProteinModelPortaliP00883.
SMRiP00883.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00883.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni272 – 274Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP00883.
KOiK01623.
OMAiPNMVIDG.
OrthoDBiEOG091G0A9T.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
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.

P00883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHSHPALTP 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 HIYLEGTLLK PNMVTPGHAC TQKYSHEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
360
AAASESLFIS NHAY
Length:364
Mass (Da):39,343
Last modified:January 23, 2007 - v2
Checksum:iE61BCBC60F668324
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35E → Q AA sequence (PubMed:1122141).Curated1
Sequence conflicti274 – 276GQS → SQE AA sequence (PubMed:1122142).Curated3
Sequence conflicti276S → E AA sequence (PubMed:1122142).Curated1
Sequence conflicti294 – 296KPW → WPK AA sequence (PubMed:1122142).Curated3
Sequence conflicti354S → R in CAA24246 (PubMed:6687628).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02300 mRNA. Translation: AAA31156.1.
V00876 mRNA. Translation: CAA24245.1.
V00877 mRNA. Translation: CAA24246.1.
PIRiA92444. ADRBA.
RefSeqiNP_001075707.1. NM_001082238.1.
XP_008256151.1. XM_008257929.2.
XP_008256152.1. XM_008257930.2.
XP_017197924.1. XM_017342435.1.
UniGeneiOcu.864.

Genome annotation databases

EnsembliENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneIDi100009055.
KEGGiocu:100009055.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02300 mRNA. Translation: AAA31156.1.
V00876 mRNA. Translation: CAA24245.1.
V00877 mRNA. Translation: CAA24246.1.
PIRiA92444. ADRBA.
RefSeqiNP_001075707.1. NM_001082238.1.
XP_008256151.1. XM_008257929.2.
XP_008256152.1. XM_008257930.2.
XP_017197924.1. XM_017342435.1.
UniGeneiOcu.864.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ADOX-ray1.90A/B/C/D2-364[»]
1EWDX-ray2.46A/B/C/D2-364[»]
1EWEX-ray2.60A/B/C/D2-364[»]
1EX5X-ray2.20A/B/C/D2-364[»]
1J4EX-ray2.65A/B/C/D2-364[»]
1ZAHX-ray1.80A/B/C/D2-364[»]
1ZAIX-ray1.76A/B/C/D2-364[»]
1ZAJX-ray1.89A/B/C/D2-364[»]
1ZALX-ray1.89A/B/C/D2-364[»]
2OT0X-ray2.05A/B/C/D2-364[»]
2OT1X-ray2.05A/B/C/D2-364[»]
2QUTX-ray1.88A/B/C/D2-364[»]
2QUUX-ray1.98A/B/C/D2-364[»]
2QUVX-ray2.22A/B/C/D2-364[»]
3B8DX-ray2.00A/B/C/D2-364[»]
3BV4X-ray1.70A5-344[»]
3DFNX-ray1.86A/B/C/D2-364[»]
3DFOX-ray1.94A/B/C/D2-364[»]
3DFPX-ray2.05A/B/C/D2-364[»]
3DFQX-ray1.82A/B/C/D2-364[»]
3DFSX-ray2.03A/B/C/D2-364[»]
3DFTX-ray1.94A/B/C/D2-364[»]
3LGEX-ray2.20A/B/C/D2-364[»]
3TU9X-ray2.09A/B/C/D2-364[»]
6ALDX-ray2.30A/B/C/D2-364[»]
ProteinModelPortaliP00883.
SMRiP00883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172078. 2 interactors.
IntActiP00883. 1 interactor.
MINTiMINT-7995296.
STRINGi9986.ENSOCUP00000020204.

Chemistry databases

BindingDBiP00883.
ChEMBLiCHEMBL4695.

PTM databases

iPTMnetiP00883.

Proteomic databases

PRIDEiP00883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneIDi100009055.
KEGGiocu:100009055.

Organism-specific databases

CTDi226.

Phylogenomic databases

eggNOGiKOG1557. Eukaryota.
COG3588. LUCA.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP00883.
KOiK01623.
OMAiPNMVIDG.
OrthoDBiEOG091G0A9T.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BRENDAi4.1.2.13. 1749.
SABIO-RKP00883.

Miscellaneous databases

EvolutionaryTraceiP00883.
PROiP00883.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDOA_RABIT
AccessioniPrimary (citable) accession number: P00883
Secondary accession number(s): Q28671
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 151 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.
Alkylation of Arg-43 inactivates the enzyme.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.