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Fructose-bisphosphate aldolase A (EC 4.1.2.13) (Muscle-type aldolase)

 ALDOA_RABIT             Reviewed;         364 AA.
P00883; Q28671;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
16-JAN-2019, entry version 164.
RecName: Full=Fructose-bisphosphate aldolase A;
EC=4.1.2.13;
AltName: Full=Muscle-type aldolase;
Name=ALDOA;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6546378;
Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.;
"The complete nucleotide sequence for rabbit muscle aldolase A
messenger RNA.";
J. Biol. Chem. 259:1127-1131(1984).
[2]
PRELIMINARY PROTEIN SEQUENCE OF 2-364.
TISSUE=Muscle;
PubMed=4417717;
Sajgo M., Hajos G.;
"The amino acid sequence of rabbit muscle aldolase.";
Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974).
[3]
PROTEIN SEQUENCE OF 2-364.
TISSUE=Muscle;
PubMed=4812352; DOI=10.1126/science.183.4130.1204;
Lai C.-Y., Nakai N., Chang D.;
"Amino acid sequence of rabbit muscle aldolase and the structure of
the active center.";
Science 183:1204-1206(1974).
[4]
PROTEIN SEQUENCE OF 2-165.
PubMed=1122141; DOI=10.1016/0003-9861(75)90397-5;
Nakai N., Chang D., Lai C.-Y.;
"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.";
Arch. Biochem. Biophys. 166:347-357(1975).
[5]
PROTEIN SEQUENCE OF 174-201, AND SEQUENCE REVISION.
PubMed=534504; DOI=10.1042/bj1830429;
Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.;
"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.";
Biochem. J. 183:429-444(1979).
[6]
PROTEIN SEQUENCE OF 252-364, AND SEQUENCE REVISION.
PubMed=1122142; DOI=10.1016/0003-9861(75)90398-7;
Lai C.-Y.;
"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.";
Arch. Biochem. Biophys. 166:358-368(1975).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
PubMed=6687628; DOI=10.1038/302718a0;
Putney S.D., Herlihy W.C., Schimmel P.R.;
"A new troponin T and cDNA clones for 13 different muscle proteins,
found by shotgun sequencing.";
Nature 302:718-721(1983).
[8]
ACTIVE SITE, AND DEAMIDATION AT ASN-361.
PubMed=4857186; DOI=10.1016/S0006-291X(74)80360-8;
Hartman F.C., Welch M.H.;
"Identification of the histidyl residue of rabbit muscle aldolase
alkylated by N-bromoacetylethanolamine phosphate.";
Biochem. Biophys. Res. Commun. 57:85-92(1974).
[9]
ACTIVE SITE.
PubMed=5453;
Hartman F.C., Brown J.P.;
"Affinity labeling of a previously undetected essential lysyl residue
in class I fructose bisphosphate aldolase.";
J. Biol. Chem. 251:3057-3062(1976).
[10]
SUBSTRATE-BINDING SITE.
PubMed=499203; DOI=10.1111/j.1432-1033.1979.tb13258.x;
Patthy L., Varadi A., Thesz J., Kovacs K.;
"Identification of the C-1-phosphate-binding arginine residue of
rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled
peptide by chemisorption chromatography.";
Eur. J. Biochem. 99:309-313(1979).
[11]
INTERACTION WITH FBP2, AND SUBCELLULAR LOCATION.
PubMed=15757649; DOI=10.1016/j.febslet.2005.01.071;
Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.;
"The effect of calcium ions on subcellular localization of aldolase-
FBPase complex in skeletal muscle.";
FEBS Lett. 579:1607-1612(2005).
[12]
INTERACTION WITH FBP2.
PubMed=18214967; DOI=10.1002/prot.21909;
Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.;
"Evolutionary conserved N-terminal region of human muscle fructose
1,6-bisphosphatase regulates its activity and the interaction with
aldolase.";
Proteins 72:209-216(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=8989320; DOI=10.1038/nsb0197-36;
Blom N., Sygusch J.;
"Product binding and role of the C-terminal region in class I D-
fructose 1,6-bisphosphate aldolase.";
Nat. Struct. Biol. 4:36-39(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH
SUBSTRATE, SUBUNIT, AND MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND
ARG-304.
PubMed=10504235; DOI=10.1021/bi9828371;
Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R.,
Allen K.N.;
"Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its
natural substrate in a cleavage-defective mutant at 2.3 A.";
Biochemistry 38:12655-12664(1999).
[15]
X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), AND MUTAGENESIS OF GLU-188;
GLU-190 AND LYS-230.
PubMed=11779856; DOI=10.1074/jbc.M107600200;
Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.;
"A conserved glutamate residue exhibits multifunctional catalytic
roles in D-fructose-1,6-bisphosphate aldolases.";
J. Biol. Chem. 277:9474-9483(2002).
[16]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, AND
FUNCTION.
PubMed=17329259; DOI=10.1074/jbc.M611505200;
St-Jean M., Izard T., Sygusch J.;
"A hydrophobic pocket in the active site of glycolytic aldolase
mediates interactions with Wiskott-Aldrich syndrome protein.";
J. Biol. Chem. 282:14309-14315(2007).
[17]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, AND
SUBUNIT.
PubMed=18453690; DOI=10.1107/S0907444908004976;
Sherawat M., Tolan D.R., Allen K.N.;
"Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A
dimer variant.";
Acta Crystallogr. D 64:543-550(2008).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9,
INTERACTION WITH SNX9, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=20129922; DOI=10.1074/jbc.M109.092049;
Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.;
"Mechanism of aldolase control of sorting nexin 9 function in
endocytosis.";
J. Biol. Chem. 285:11983-11990(2010).
-!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In
addition, may also function as scaffolding protein.
{ECO:0000269|PubMed:17329259}.
-!- CATALYTIC ACTIVITY:
Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
EC=4.1.2.13; Evidence={ECO:0000269|PubMed:20129922};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 4/4.
-!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with
FBP2; the interaction blocks FBP2 inhibition by physiological
concentrations of AMP and reduces inhibition by Ca(2+).
{ECO:0000269|PubMed:10504235, ECO:0000269|PubMed:15757649,
ECO:0000269|PubMed:17329259, ECO:0000269|PubMed:18214967,
ECO:0000269|PubMed:18453690, ECO:0000269|PubMed:20129922}.
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
{ECO:0000269|PubMed:15757649}. Cytoplasm, myofibril, sarcomere, M
line {ECO:0000269|PubMed:15757649}. Note=In skeletal muscle,
accumulates around the M line and within the I band, colocalizing
with FBP2 on both sides of the Z line in the absence of Ca(2+).
-!- PTM: Asn-361 in form alpha is deaminated to Asp in form beta.
-!- 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.
-!- MISCELLANEOUS: Alkylation of Arg-43 inactivates the enzyme.
-!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/ALD/";
-----------------------------------------------------------------------
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EMBL; K02300; AAA31156.1; -; mRNA.
EMBL; V00876; CAA24245.1; -; mRNA.
EMBL; V00877; CAA24246.1; -; mRNA.
PIR; A92444; ADRBA.
RefSeq; NP_001075707.1; NM_001082238.1.
RefSeq; XP_008256151.1; XM_008257929.2.
RefSeq; XP_008256152.1; XM_008257930.2.
RefSeq; XP_017197924.1; XM_017342435.1.
UniGene; Ocu.864; -.
PDB; 1ADO; X-ray; 1.90 A; A/B/C/D=2-364.
PDB; 1EWD; X-ray; 2.46 A; A/B/C/D=2-364.
PDB; 1EWE; X-ray; 2.60 A; A/B/C/D=2-364.
PDB; 1EX5; X-ray; 2.20 A; A/B/C/D=2-364.
PDB; 1J4E; X-ray; 2.65 A; A/B/C/D=2-364.
PDB; 1ZAH; X-ray; 1.80 A; A/B/C/D=2-364.
PDB; 1ZAI; X-ray; 1.76 A; A/B/C/D=2-364.
PDB; 1ZAJ; X-ray; 1.89 A; A/B/C/D=2-364.
PDB; 1ZAL; X-ray; 1.89 A; A/B/C/D=2-364.
PDB; 2OT0; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 2OT1; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 2QUT; X-ray; 1.88 A; A/B/C/D=2-364.
PDB; 2QUU; X-ray; 1.98 A; A/B/C/D=2-364.
PDB; 2QUV; X-ray; 2.22 A; A/B/C/D=2-364.
PDB; 3B8D; X-ray; 2.00 A; A/B/C/D=2-364.
PDB; 3BV4; X-ray; 1.70 A; A=5-344.
PDB; 3DFN; X-ray; 1.86 A; A/B/C/D=2-364.
PDB; 3DFO; X-ray; 1.94 A; A/B/C/D=2-364.
PDB; 3DFP; X-ray; 2.05 A; A/B/C/D=2-364.
PDB; 3DFQ; X-ray; 1.82 A; A/B/C/D=2-364.
PDB; 3DFS; X-ray; 2.03 A; A/B/C/D=2-364.
PDB; 3DFT; X-ray; 1.94 A; A/B/C/D=2-364.
PDB; 3LGE; X-ray; 2.20 A; A/B/C/D=2-364.
PDB; 3TU9; X-ray; 2.09 A; A/B/C/D=2-364.
PDB; 5F4X; X-ray; 1.84 A; A/B/C/D=2-364.
PDB; 5TLE; X-ray; 1.58 A; A/B/C/D=2-364.
PDB; 5TLH; X-ray; 2.20 A; A/B/C/D=2-364.
PDB; 5TLW; X-ray; 2.29 A; A/B/C/D=2-364.
PDB; 5TLZ; X-ray; 1.97 A; A/B/C/D=2-364.
PDB; 5VY5; EM; 2.60 A; A/B/C/D=2-364.
PDB; 6ALD; X-ray; 2.30 A; A/B/C/D=2-364.
PDB; 6MWQ; EM; 3.00 A; A/B/C/D=12-348.
PDBsum; 1ADO; -.
PDBsum; 1EWD; -.
PDBsum; 1EWE; -.
PDBsum; 1EX5; -.
PDBsum; 1J4E; -.
PDBsum; 1ZAH; -.
PDBsum; 1ZAI; -.
PDBsum; 1ZAJ; -.
PDBsum; 1ZAL; -.
PDBsum; 2OT0; -.
PDBsum; 2OT1; -.
PDBsum; 2QUT; -.
PDBsum; 2QUU; -.
PDBsum; 2QUV; -.
PDBsum; 3B8D; -.
PDBsum; 3BV4; -.
PDBsum; 3DFN; -.
PDBsum; 3DFO; -.
PDBsum; 3DFP; -.
PDBsum; 3DFQ; -.
PDBsum; 3DFS; -.
PDBsum; 3DFT; -.
PDBsum; 3LGE; -.
PDBsum; 3TU9; -.
PDBsum; 5F4X; -.
PDBsum; 5TLE; -.
PDBsum; 5TLH; -.
PDBsum; 5TLW; -.
PDBsum; 5TLZ; -.
PDBsum; 5VY5; -.
PDBsum; 6ALD; -.
PDBsum; 6MWQ; -.
ProteinModelPortal; P00883; -.
SMR; P00883; -.
BioGrid; 1172078; 2.
IntAct; P00883; 1.
MINT; P00883; -.
STRING; 9986.ENSOCUP00000020204; -.
BindingDB; P00883; -.
ChEMBL; CHEMBL4695; -.
MoonProt; P00883; -.
iPTMnet; P00883; -.
PRIDE; P00883; -.
Ensembl; ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneID; 100009055; -.
KEGG; ocu:100009055; -.
CTD; 226; -.
eggNOG; KOG1557; Eukaryota.
eggNOG; COG3588; LUCA.
GeneTree; ENSGT00390000010235; -.
HOGENOM; HOG000220876; -.
HOVERGEN; HBG002386; -.
InParanoid; P00883; -.
KO; K01623; -.
OMA; DYREMLF; -.
OrthoDB; 799973at2759; -.
BRENDA; 4.1.2.13; 1749.
SABIO-RK; P00883; -.
UniPathway; UPA00109; UER00183.
EvolutionaryTrace; P00883; -.
PRO; PR:P00883; -.
Proteomes; UP000001811; Chromosome 6.
Bgee; ENSOCUG00000006329; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell.
GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
GO; GO:0006096; P:glycolytic process; IDA:UniProtKB.
GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IMP:CAFA.
GO; GO:0030335; P:positive regulation of cell migration; IDA:CAFA.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR029768; Aldolase_I_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000741; FBA_I.
Pfam; PF00274; Glycolytic; 1.
PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycolysis; Isopeptide bond; Lyase;
Phosphoprotein; Reference proteome; Schiff base; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1122141,
ECO:0000269|PubMed:4812352}.
CHAIN 2 364 Fructose-bisphosphate aldolase A.
/FTId=PRO_0000216938.
REGION 272 274 Substrate binding. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
ACT_SITE 188 188 Proton acceptor.
{ECO:0000269|PubMed:11779856}.
ACT_SITE 230 230 Schiff-base intermediate with
dihydroxyacetone-P.
{ECO:0000269|PubMed:11779856}.
BINDING 43 43 Substrate. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
BINDING 304 304 Substrate. {ECO:0000244|PDB:6ALD,
ECO:0000269|PubMed:10504235}.
SITE 73 73 Essential for substrate cleavage.
SITE 108 108 Essential for substrate cleavage.
SITE 147 147 Alkylation inactivates the enzyme.
SITE 362 362 Alkylation inactivates the enzyme;
essential for the subsequent hydrolysis
of the dihydroxyacetone Schiff base.
SITE 364 364 Necessary for preference for fructose
1,6-bisphosphate over fructose 1-
phosphate.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 42 42 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 111 111 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P09972}.
MOD_RES 111 111 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P05065}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 312 312 N6-malonyllysine. {ECO:0000250}.
MOD_RES 330 330 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04075}.
MOD_RES 361 361 Deamidated asparagine; in form beta.
{ECO:0000269|PubMed:4857186}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P04075}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04075}.
MUTAGEN 35 35 E->A: Reduces activity 14-fold.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 43 43 R->A: Reduces activity 14-fold.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 129 129 D->V: Alters protein-protein
interactions, leading to a dimeric
protein.
MUTAGEN 147 147 K->A: Loss of activity.
{ECO:0000269|PubMed:10504235}.
MUTAGEN 188 188 E->A: Reduces activity over 100-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 188 188 E->Q: Reduces activity over 1000-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 190 190 E->Q: Reduces activity 20-fold.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 230 230 K->M: Loss of activity.
{ECO:0000269|PubMed:11779856}.
MUTAGEN 304 304 R->A: Reduces activity 400-fold.
{ECO:0000269|PubMed:10504235}.
CONFLICT 35 35 E -> Q (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 274 276 GQS -> SQE (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 276 276 S -> E (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 294 296 KPW -> WPK (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 354 354 S -> R (in Ref. 7; CAA24246).
{ECO:0000305}.
HELIX 10 23 {ECO:0000244|PDB:5TLE}.
STRAND 29 33 {ECO:0000244|PDB:5TLE}.
HELIX 37 45 {ECO:0000244|PDB:5TLE}.
TURN 46 48 {ECO:0000244|PDB:5TLE}.
HELIX 53 64 {ECO:0000244|PDB:5TLE}.
HELIX 68 70 {ECO:0000244|PDB:5TLE}.
TURN 71 73 {ECO:0000244|PDB:5TLE}.
STRAND 74 79 {ECO:0000244|PDB:5TLE}.
HELIX 81 84 {ECO:0000244|PDB:5TLE}.
TURN 89 91 {ECO:0000244|PDB:1EWE}.
HELIX 94 100 {ECO:0000244|PDB:5TLE}.
STRAND 104 108 {ECO:0000244|PDB:5TLE}.
STRAND 113 115 {ECO:0000244|PDB:5TLE}.
STRAND 119 121 {ECO:0000244|PDB:5TLE}.
STRAND 123 125 {ECO:0000244|PDB:5TLE}.
HELIX 131 140 {ECO:0000244|PDB:5TLE}.
STRAND 145 152 {ECO:0000244|PDB:5TLE}.
STRAND 155 157 {ECO:0000244|PDB:5TLE}.
HELIX 161 180 {ECO:0000244|PDB:5TLE}.
STRAND 184 191 {ECO:0000244|PDB:5TLE}.
HELIX 199 219 {ECO:0000244|PDB:5TLE}.
HELIX 224 226 {ECO:0000244|PDB:5TLE}.
HELIX 246 258 {ECO:0000244|PDB:5TLE}.
STRAND 267 270 {ECO:0000244|PDB:5TLE}.
HELIX 277 289 {ECO:0000244|PDB:5TLE}.
STRAND 290 292 {ECO:0000244|PDB:2QUV}.
STRAND 296 303 {ECO:0000244|PDB:5TLE}.
HELIX 304 314 {ECO:0000244|PDB:5TLE}.
HELIX 318 320 {ECO:0000244|PDB:5TLE}.
HELIX 321 338 {ECO:0000244|PDB:5TLE}.
TURN 339 341 {ECO:0000244|PDB:5TLE}.
STRAND 345 347 {ECO:0000244|PDB:1ZAI}.
HELIX 351 354 {ECO:0000244|PDB:3DFQ}.
STRAND 358 360 {ECO:0000244|PDB:1ADO}.
HELIX 361 363 {ECO:0000244|PDB:5TLE}.
SEQUENCE 364 AA; 39343 MW; E61BCBC60F668324 CRC64;
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKYSHEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFIS
NHAY


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E0622b ELISA ALDOB,Bos taurus,Bovine,Fructose-bisphosphate aldolase B,Liver-type aldolase 96T
E0622b ELISA kit ALDOB,Bos taurus,Bovine,Fructose-bisphosphate aldolase B,Liver-type aldolase 96T
U0622b CLIA ALDOB,Bos taurus,Bovine,Fructose-bisphosphate aldolase B,Liver-type aldolase 96T
E0622r ELISA kit Aldob,Fructose-bisphosphate aldolase B,Liver-type aldolase,Rat,Rattus norvegicus 96T
E0622h ELISA kit ALDB,ALDOB,Fructose-bisphosphate aldolase B,Homo sapiens,Human,Liver-type aldolase 96T
E0622h ELISA ALDB,ALDOB,Fructose-bisphosphate aldolase B,Homo sapiens,Human,Liver-type aldolase 96T
E0622Rb ELISA kit ALDB,ALDOB,Fructose-bisphosphate aldolase B,Liver-type aldolase,Oryctolagus cuniculus,Rabbit 96T
E0622Rb ELISA ALDB,ALDOB,Fructose-bisphosphate aldolase B,Liver-type aldolase,Oryctolagus cuniculus,Rabbit 96T
U0622Rb CLIA ALDB,ALDOB,Fructose-bisphosphate aldolase B,Liver-type aldolase,Oryctolagus cuniculus,Rabbit 96T
U0622h CLIA ALDB,ALDOB,Fructose-bisphosphate aldolase B,Homo sapiens,Human,Liver-type aldolase 96T
E0622c ELISA ALDOB,Chicken,Fructose-bisphosphate aldolase B,Gallus gallus,Liver-type aldolase 96T
U0622c CLIA ALDOB,Chicken,Fructose-bisphosphate aldolase B,Gallus gallus,Liver-type aldolase 96T
E0622c ELISA kit ALDOB,Chicken,Fructose-bisphosphate aldolase B,Gallus gallus,Liver-type aldolase 96T
25-695 Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) is a tetrameric glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacet 0.05 mg
CSB-EL001586RA Rat aldolase B, fructose-bisphosphate (ALDOB) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001583RA Rat aldolase A, fructose-bisphosphate (ALDOA) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001587RA Rat aldolase C, fructose-bisphosphate (ALDOC) ELISA kit, Species Rat, Sample Type serum, plasma 96T
20312313-1 ALD | fructose-1,6 bisphosphate aldolase 100 uL
E02F0213 Rat Fructose-1,6-bisphosphate aldolase 96 Tests/kit

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1493: Carbon assimilation C4 pathway
WP253: Glycolysis
WP1946: Cori Cycle
WP1024: Steroid Biosynthesis
WP1143: Steroid Biosynthesis
WP1613: 1,4-Dichlorobenzene degradation
WP1627: Benzoate degradation via hydroxylation
WP1632: Biphenyl degradation
WP1637: Carbazole degradation
WP1646: Ethylbenzene degradation
WP1649: Fluorene degradation
WP1686: Phenylalanine metabolism
WP1704: Styrene degradation
WP1710: Toluene and xylene degradation
WP2199: Seed Development
WP2263: Prostate Cancer
WP496: Steroid Biosynthesis
WP55: Steroid Biosynthesis
WP66: Steroid Biosynthesis
WP792: Steroid Biosynthesis
WP907: Steroid Biosynthesis
WP1017: Type II interferon signaling (IFNG)
WP1088: Striated Muscle Contraction
WP1136: Type II interferon signaling (IFNG)
WP1253: Type II interferon signaling (IFNG)

Related Genes :
[fbaA fba fda b2925 JW2892] Fructose-bisphosphate aldolase class 2 (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (Fructose-bisphosphate aldolase class II)
[fbp TK2164] Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase)
[FBA1 YKL060C YKL320] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[fba HVO_1494 C498_11261] Fructose-bisphosphate aldolase class 2 (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (Fructose-bisphosphate aldolase class II)
[FBA1 CAALFM_C401750CA CaO19.12088 CaO19.4618] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (37 kDa major allergen) (Fructose-1,6-bisphosphate aldolase) (IgE-binding allergen)
[fbp STK_03180] Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase)
[Ald CG6058] Fructose-bisphosphate aldolase (EC 4.1.2.13)
[fbaB dhnA b2097 JW5344] Fructose-bisphosphate aldolase class 1 (EC 4.1.2.13) (Fructose-bisphosphate aldolase class I) (FBP aldolase)
[FBA8 At3g52930 F8J2_100] Fructose-bisphosphate aldolase 8, cytosolic (AtFBA8) (EC 4.1.2.13) (Cytosolic aldolase 1) (cAld1)
[FBA6 At2g36460] Fructose-bisphosphate aldolase 6, cytosolic (AtFBA6) (EC 4.1.2.13) (Cytosolic aldolase 2) (cAld2)
[FBA2 At4g38970 F19H22.70] Fructose-bisphosphate aldolase 2, chloroplastic (AtFBA2) (EC 4.1.2.13)
[kbaY agaY kba yraC b3137 JW3106] D-tagatose-1,6-bisphosphate aldolase subunit KbaY (TBPA) (TagBP aldolase) (EC 4.1.2.40) (D-tagatose-bisphosphate aldolase class II) (Ketose 1,6-bisphosphate aldolase class II) (Tagatose-bisphosphate aldolase)
[agaY agaY_1 agaY_2 kbaY kbaY_1 kbaY_2 A6581_06135 A6592_14490 A8C65_02445 A8G17_24215 A9819_18030 A9R57_12875 AC789_1c35070 ACN002_3231 ACN81_18735 ACU57_14720 ACU90_11840 AKG99_18810 AM270_10360 AM446_04575 AM464_08310 AMK83_06615 AML07_27945 AML35_14160 APT94_22945 APU18_16660 APZ14_04020 ARC77_12125 AU473_06025 AUQ13_02800 AUS26_18535 AW059_15450 AZZ83_001415 B1K96_05960 B7C53_19450 BB545_10055 BEN53_19445 BHF46_07040 BHS81_18925 BIZ41_14335 BJJ90_03045 BK248_21775 BK292_10495 BK334_09815 BK383_15710 BK400_20325 BMT49_25850 BMT53_18450 BN17_30821 BTQ04_16760 BTQ06_20745 BVL39_10420 BW690_01005 BWP17_07060 BXT93_18380 BZL31_25275 BZL69_07435 C2U48_17840 C3K24_11445 C4J69_18785 C4K41_03525 C5715_12280 C5N07_16465 C5P01_19110 C5P43_02160 C6669_12295 C6986_20200 C6B13_15150 C7235_03500 C7B02_08945 C7B06_16525 C7B07_10875 C7B08_03310 C9E25_21030 CA593_10600 CG691_12975 CG692_22965 CG705_12120 CG706_23220 COD30_05970 COD46_22025 CR538_03350 CR539_20970 CRD98_04990 CRE06_06550 CRM83_23775 CSB64_06340 CT143_11135 CT146_02800 CVH05_07665 CWS33_08100 CXB56_06685 D0X26_08835 D1900_24065 D2183_08305 D2F89_23160 D3I61_18805 DIV22_09280 DIV25_06765 DL545_03915 DL800_22990 DNQ41_21475 DNR41_10930 DQE83_16800 DTL43_04020 DTL84_11155 DTL90_07295 DTM27_04405 DTM45_14255 EC1094V2_507 EC3234A_53c00160 EC95NR1_02516 ECONIH1_18600 ECs4017 EL75_0549 EL79_0572 EL80_0564 ERS085365_00596 ERS085366_00607 ERS085374_01873 ERS085379_00428 ERS085383_00753 ERS085386_00541 ERS085404_02243 ERS085406_03651 ERS085416_00299 ERS139211_00539 ERS150873_01748 ERS150876_00972 FORC28_0668 HMPREF3040_01995 HW43_20655 JD73_01650 MS6198_36220 MS8345_03490 NCTC10082_03001 NCTC10764_04039 NCTC10767_01694 NCTC10865_00851 NCTC11022_03300 NCTC11341_01695 NCTC12950_00651 NCTC13125_03918 NCTC13148_03216 NCTC13462_04280 NCTC13846_00667 NCTC7152_00616 NCTC8009_01738 NCTC8622_00268 NCTC8960_03245 NCTC8985_05190 NCTC9036_00713 NCTC9037_00830 NCTC9045_00750 NCTC9050_03774 NCTC9055_02547 NCTC9062_02519 NCTC9111_01031 NCTC9117_00956 NCTC9119_00687 NCTC9434_00595 NCTC9701_00743 NCTC9703_05134 NCTC9706_02907 NCTC9969_00822 PU06_20125 RG28_20800 RK56_014885 RX35_04224 SAMEA3472033_00859 SAMEA3472044_03367 SAMEA3472047_01838 SAMEA3472055_00433 SAMEA3472056_03039 SAMEA3472067_02761 SAMEA3472070_01205 SAMEA3472080_00912 SAMEA3472108_00133 SAMEA3472110_01572 SAMEA3472112_01556 SAMEA3472114_00516 SAMEA3472147_03318 SAMEA3484427_00641 SAMEA3484429_00701 SAMEA3484433_01239 SAMEA3484434_03283 SAMEA3485101_01677 SAMEA3752372_01750 SAMEA3752557_01908 SAMEA3752559_03865 SAMEA3753064_02903 SAMEA3753097_03267 SAMEA3753106_03728 SAMEA3753290_00181 SAMEA3753300_02165 SAMEA3753391_02230 SAMEA3753397_00141 SK85_03447 UC41_11540 UN86_15655 WM48_17485 WQ89_06915 WR15_24715 YDC107_1814] D-tagatose-1,6-bisphosphate aldolase subunit KbaY (TBPA) (TagBP aldolase) (EC 4.1.2.40) (D-tagatose-bisphosphate aldolase class II) (Ketose 1,6-bisphosphate aldolase class II) (Tagatose-bisphosphate aldolase)
[FBP2] Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase)
[fsaA fsa mipB ybiZ b0825 JW5109] Fructose-6-phosphate aldolase 1 (EC 4.1.2.-) (Fructose-6-phosphate aldolase A) (FSAA)
[FBP2] Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase)
[fba Rv0363c MTCY13E10.25c] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[fba1 SPBC19C2.07] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[Fbp2] Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase) (RAE-30)
[Fbp2] Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase)
[PFKM PFKX] ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)
[fbaA fba fba1 tsr BSU37120] Probable fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[proA] 4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase (HMG/CHA aldolase) (EC 4.1.3.16) (EC 4.1.3.17) (4-hydroxy-2-oxoglutarate aldolase) (Oxaloacetate decarboxylase) (OAA decarboxylase) (EC 4.1.1.112)
[fba NCU07807] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[MJ1585] Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase (EC 2.2.1.11) (EC 4.1.2.13) (DKFP synthase) (Fructose-bisphosphate aldolase class 1) (Fructose-bisphosphate aldolase class I) (FBP aldolase)
[Pfkm Pfk-m Pfka] ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)
[cbbA] Fructose-bisphosphate aldolase (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase)
[PFKM M-PFK] ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)
[PFKM] ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)
[Pfkm Pfk-m] ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)

Bibliography :
[22700512] Comparative proteomic characterization of the sarcoplasmic proteins in the pectoralis major and supracoracoideus breast muscles in 2 chicken genotypes.
[22160517] Identification of a fructose-1,6-bisphosphate aldolase gene and association of the single nucleotide polymorphisms with growth traits in the clam Meretrix meretrix.
[21698747] Muscle-type 6-phosphofructo-1-kinase and aldolase associate conferring catalytic advantages for both enzymes.
[20800309] Malignant but not naïve hepatocytes of human and rodent origin are killed by TNF after metabolic depletion of ATP by fructose.
[15202499] Aldolase and actin protect rabbit muscle lactate dehydrogenase from ascorbate inhibition.
[11227796] Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ.
[10978512] Isolation and characterization of Xenopus laevis aldolase B cDNA and expression patterns of aldolase A, B and C genes in adult tissues, oocytes and embryos of Xenopus laevis.
[9427528] Structure of aldolase A (muscle-type) cDNA and its regulated expression in oocytes, embryos and adult tissues of Xenopus laevis.
[9244396] Mode of interactions of human aldolase isozymes with cytoskeletons.
[9143366] Lamprey fructose-1,6-bisphosphate aldolase: characterization of the muscle-type and non-muscle-type isozymes.
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