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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

Pathway: 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, Fructose-bisphosphate aldolase (ALDOC), 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431Substrate1 Publication
Sitei73 – 731Essential for substrate cleavage
Sitei108 – 1081Essential for substrate cleavage
Sitei147 – 1471Alkylation inactivates the enzyme
Active sitei188 – 1881Proton acceptor
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Binding sitei304 – 3041Substrate1 Publication
Sitei362 – 3621Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

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
ProteomesiUP000001811 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351E → A: Reduces activity 14-fold. 1 Publication
Mutagenesisi43 – 431R → A: Reduces activity 14-fold. 1 Publication
Mutagenesisi129 – 1291D → V: Alters protein-protein interactions, leading to a dimeric protein.
Mutagenesisi147 – 1471K → A: Loss of activity. 1 Publication
Mutagenesisi188 – 1881E → A: Reduces activity over 100-fold. 1 Publication
Mutagenesisi188 – 1881E → Q: Reduces activity over 1000-fold. 1 Publication
Mutagenesisi190 – 1901E → Q: Reduces activity 20-fold. 1 Publication
Mutagenesisi230 – 2301K → M: Loss of activity. 1 Publication
Mutagenesisi304 – 3041R → A: Reduces activity 400-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216938Add
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
Modified residuei361 – 3611Deamidated asparagine; in form beta1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00883.

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

IntActiP00883. 1 interaction.
MINTiMINT-7995296.
STRINGi9986.ENSOCUP00000020204.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Beta strandi29 – 335Combined sources
Helixi37 – 459Combined sources
Turni46 – 483Combined sources
Helixi53 – 6412Combined sources
Helixi68 – 703Combined sources
Turni71 – 733Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 844Combined sources
Turni89 – 913Combined sources
Helixi94 – 996Combined sources
Turni100 – 1023Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1253Combined sources
Helixi131 – 14010Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi155 – 1573Combined sources
Helixi161 – 18020Combined sources
Beta strandi184 – 1918Combined sources
Helixi199 – 21921Combined sources
Helixi224 – 2263Combined sources
Helixi246 – 25813Combined sources
Beta strandi267 – 2704Combined sources
Helixi277 – 28913Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi296 – 3038Combined sources
Helixi304 – 31411Combined sources
Helixi318 – 3203Combined sources
Helixi321 – 33818Combined sources
Turni339 – 3413Combined sources
Beta strandi345 – 3473Combined sources
Helixi351 – 3544Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00883.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP00883.
KOiK01623.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → Q AA sequence (PubMed:1122141).Curated
Sequence conflicti274 – 2763GQS → SQE AA sequence (PubMed:1122142).Curated
Sequence conflicti276 – 2761S → E AA sequence (PubMed:1122142).Curated
Sequence conflicti294 – 2963KPW → WPK AA sequence (PubMed:1122142).Curated
Sequence conflicti354 – 3541S → R in CAA24246 (PubMed:6687628).Curated

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_008257929.1.
XP_008256152.1. XM_008257930.1.
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_008257929.1.
XP_008256152.1. XM_008257930.1.
UniGeneiOcu.864.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00883. 1 interaction.
MINTiMINT-7995296.
STRINGi9986.ENSOCUP00000020204.

Chemistry

BindingDBiP00883.
ChEMBLiCHEMBL4695.

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

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP00883.
KOiK01623.

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.
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

  1. "The complete nucleotide sequence for rabbit muscle aldolase A messenger RNA."
    Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.
    J. Biol. Chem. 259:1127-1131(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The amino acid sequence of rabbit muscle aldolase."
    Sajgo M., Hajos G.
    Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-364.
    Tissue: Muscle.
  3. "Amino acid sequence of rabbit muscle aldolase and the structure of the active center."
    Lai C.-Y., Nakai N., Chang D.
    Science 183:1204-1206(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-364.
    Tissue: Muscle.
  4. "Studies on the structure of rabbit muscle aldolase. Ordering of the tryptic peptides; sequence of 164 amino acid residues in the NH2-terminal BrCN peptide."
    Nakai N., Chang D., Lai C.-Y.
    Arch. Biochem. Biophys. 166:347-357(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165.
  5. "Extended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver."
    Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.
    Biochem. J. 183:429-444(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 174-201, SEQUENCE REVISION.
  6. "Studies on the structure of rabbit muscle aldolase. Determination of the primary structure of the COOH-terminal BrCN peptide; the complete sequence of the subunit polypeptide chain."
    Lai C.-Y.
    Arch. Biochem. Biophys. 166:358-368(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 252-364, SEQUENCE REVISION.
  7. "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
    Putney S.D., Herlihy W.C., Schimmel P.R.
    Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
  8. "Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate."
    Hartman F.C., Welch M.H.
    Biochem. Biophys. Res. Commun. 57:85-92(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, DEAMIDATION AT ASN-361.
  9. "Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase."
    Hartman F.C., Brown J.P.
    J. Biol. Chem. 251:3057-3062(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  10. "Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography."
    Patthy L., Varadi A., Thesz J., Kovacs K.
    Eur. J. Biochem. 99:309-313(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING SITE.
  11. "The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle."
    Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.
    FEBS Lett. 579:1607-1612(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2, SUBCELLULAR LOCATION.
  12. "Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase."
    Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.
    Proteins 72:209-216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2.
  13. "Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase."
    Blom N., Sygusch J.
    Nat. Struct. Biol. 4:36-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  14. "Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A."
    Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R., Allen K.N.
    Biochemistry 38:12655-12664(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND ARG-304.
  15. "A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases."
    Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.
    J. Biol. Chem. 277:9474-9483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), MUTAGENESIS OF GLU-188; GLU-190 AND LYS-230.
  16. "A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein."
    St-Jean M., Izard T., Sygusch J.
    J. Biol. Chem. 282:14309-14315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, FUNCTION.
  17. "Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant."
    Sherawat M., Tolan D.R., Allen K.N.
    Acta Crystallogr. D 64:543-550(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, SUBUNIT.
  18. "Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
    Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
    J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION WITH SNX9, SUBUNIT, CATALYTIC ACTIVITY.

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: June 24, 2015
This is version 141 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

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.