[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=6546378 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0003-9861(75)90397-5; PubMed=1122141 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0003-9861(75)90398-7; PubMed=1122142 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1038/302718a0; PubMed=6687628 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0006-291X(74)80360-8; PubMed=4857186 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1111/j.1432-1033.1979.tb13258.x; PubMed=499203 [NCBI, ExPASy, EBI, Israel, Japan] 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]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1038/nsb0197-36; PubMed=8989320 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH SUBSTRATE, AND MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND ARG-304. DOI=10.1021/bi9828371; PubMed=10504235 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), AND MUTAGENESIS OF GLU-188; GLU-190 AND LYS-230. DOI=10.1074/jbc.M107600200; PubMed=11779856 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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: Tetramer.
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.
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/ALD/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K02300; AAA31156.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00876; CAA24245.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00877; CAA24246.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A92444; ADRBA.

NP_001075707.1; -.

3D structure databases

PDB

1ADO; X-ray; 1.90 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1EWD; X-ray; 2.46 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1EWE; X-ray; 2.60 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1EWG; X-ray; 2.00 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1EX5; X-ray; 2.20 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1J4E; X-ray; 2.65 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1ZAH; X-ray; 1.80 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1ZAI; X-ray; 1.76 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1ZAJ; X-ray; 1.89 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
1ZAL; X-ray; 1.89 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]
2OT0; X-ray; 2.05 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
2OT1; X-ray; 2.05 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
2QUT; X-ray; 1.88 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
2QUU; X-ray; 1.98 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
2QUV; X-ray; 2.22 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
3B8D; X-ray; 2.00 A; A/B/C/D=2-364.	[ExPASy / RCSB / EBI]
3BV4; X-ray; 1.70 A; A=5-344.	[ExPASy / RCSB / EBI]
6ALD; X-ray; 2.30 A; A/B/C/D=1-364.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ADO; -.
1EWD; -.
1EWE; -.
1EWG; -.
1EX5; -.
1J4E; -.
1ZAH; -.
1ZAI; -.
1ZAJ; -.
1ZAL; -.
2OT0; -.
2OT1; -.
2QUT; -.
2QUU; -.
2QUV; -.
3B8D; -.
3BV4; -.
6ALD; -.

ModBase

P00883.

Family and domain databases

InterPro

IPR000741; Aldolase_I.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11627; Aldolase_I; 1.

Pfam

PF00274; Glycolytic; 1.
Pfam graphical view of domain structure.

ProDom

PD001128; Aldolase_I; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00158; ALDOLASE_CLASS_I; 1.

Genome annotation databases

Ensembl

ENSOCUG00000006329; Oryctolagus cuniculus. [Contig view]

GeneID

100009055; -.

Phylogenomic databases

HOVERGEN

P00883; -.

Other

LinkHub

P00883; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase A.`	`PRO_0000216938`
`ACT_SITE`	`188 188`		`Proton acceptor.`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`43 43`		`Substrate.`
`BINDING`	`304 304`		`Substrate.`
`SITE`	`73 73`	`1`	`Essential for substrate cleavage.`
`SITE`	`108 108`	`1`	`Essential for substrate cleavage.`
`SITE`	`147 147`	`1`	`Alkylation inactivates the enzyme.`
`SITE`	`362 362`	`1`	`Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base.`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`MOD_RES`	`13 13`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`36 36`		`Phosphoserine (By similarity).`
`MOD_RES`	`39 39`		`Phosphoserine (By similarity).`
`MOD_RES`	`42 42`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`46 46`		`Phosphoserine (By similarity).`
`MOD_RES`	`65 65`		`Phosphothreonine (By similarity).`
`MOD_RES`	`204 204`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`235 235`		`Phosphothreonine (By similarity).`
`MOD_RES`	`241 241`		`Phosphothreonine (By similarity).`
`MOD_RES`	`354 354`		`Phosphoserine (By similarity).`
`MOD_RES`	`356 356`		`Phosphoserine (By similarity).`
`MOD_RES`	`361 361`		`Deamidated asparagine; in form beta.`
`MUTAGEN`	`35 35`		`E->A: Reduces activity 14-fold.`
`MUTAGEN`	`43 43`		`R->A: Reduces activity 14-fold.`
`MUTAGEN`	`147 147`		`K->A: Loss of activity.`
`MUTAGEN`	`188 188`		`E->A: Reduces activity over 100-fold.`
`MUTAGEN`	`188 188`		`E->Q: Reduces activity over 1000-fold.`
`MUTAGEN`	`190 190`		`E->Q: Reduces activity 20-fold.`
`MUTAGEN`	`230 230`		`K->M: Loss of activity.`
`MUTAGEN`	`304 304`		`R->A: Reduces activity 400-fold.`
`CONFLICT`	`35 35`		`E -> Q (in Ref. 4; AA sequence).`
`CONFLICT`	`274 276`		`GQS -> SQE (in Ref. 6; AA sequence).`
`CONFLICT`	`276 276`		`S -> E (in Ref. 6; AA sequence).`
`CONFLICT`	`294 296`		`KPW -> WPK (in Ref. 6; AA sequence).`
`CONFLICT`	`354 354`		`S -> R (in Ref. 7; CAA24246).`
`HELIX`	`10 23`	`14`
`STRAND`	`29 33`	`5`
`HELIX`	`37 46`	`10`
`HELIX`	`53 64`	`12`
`HELIX`	`68 73`	`6`
`STRAND`	`74 79`	`6`
`HELIX`	`81 84`	`4`
`HELIX`	`94 100`	`7`
`STRAND`	`104 108`	`5`
`STRAND`	`113 115`	`3`
`STRAND`	`119 121`	`3`
`STRAND`	`123 125`	`3`
`HELIX`	`131 140`	`10`
`STRAND`	`145 152`	`8`
`STRAND`	`155 157`	`3`
`HELIX`	`161 180`	`20`
`STRAND`	`184 191`	`8`
`HELIX`	`199 219`	`21`
`HELIX`	`224 226`	`3`
`HELIX`	`246 260`	`15`
`STRAND`	`267 270`	`4`
`HELIX`	`277 289`	`13`
`STRAND`	`296 303`	`8`
`HELIX`	`304 314`	`11`
`HELIX`	`318 320`	`3`
`HELIX`	`321 338`	`18`
`TURN`	`339 341`	`3`
`STRAND`	`358 360`	`3`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39343 Da [This is the MW of the unprocessed precursor]

CRC64: E61BCBC60F668324 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPHSHPALTP EQKKELSDIA 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 ALAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
TQKYSHEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFIS 


NHAY

P00883 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools