Reviewed, UniProtKB/Swiss-Prot P00883 (ALDOA_RABIT)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase A
    EC=4.1.2.13
Alternative name(s):
    Muscle-type aldolase

Gene names

Name:

ALDOA

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Tetramer.
Post-translational modification	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. Alkylation of Arg-43 inactivates the enzyme.
Sequence similarities	Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.3 Ref.4

Chain

2 – 364

363

Fructose-bisphosphate aldolase A

PRO_0000216938

Sites

Active site

188

1

Proton acceptor Ref.8 Ref.9

Active site

230

1

Schiff-base intermediate with dihydroxyacetone-P Ref.8 Ref.9

Binding site

43

1

Substrate

Binding site

304

1

Substrate

Site

73

1

Essential for substrate cleavage

Site

108

1

Essential for substrate cleavage

Site

147

1

Alkylation inactivates the enzyme

Site

362

1

Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base

Site

364

1

Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue

13

1

N6-acetyllysine By similarity

Modified residue

36

1

Phosphoserine By similarity

Modified residue

39

1

Phosphoserine By similarity

Modified residue

42

1

N6-acetyllysine By similarity

Modified residue

46

1

Phosphoserine By similarity

Modified residue

65

1

Phosphothreonine By similarity

Modified residue

204

1

Phosphotyrosine By similarity

Modified residue

223

1

Phosphotyrosine By similarity

Modified residue

235

1

Phosphothreonine By similarity

Modified residue

241

1

Phosphothreonine By similarity

Modified residue

354

1

Phosphoserine By similarity

Modified residue

356

1

Phosphoserine By similarity

Modified residue

361

1

Deamidated asparagine; in form beta

Experimental info

Mutagenesis

35

1

E → A: Reduces activity 14-fold. Ref.12

Mutagenesis

43

1

R → A: Reduces activity 14-fold. Ref.12

Mutagenesis

147

1

K → A: Loss of activity. Ref.12

Mutagenesis

188

1

E → A: Reduces activity over 100-fold. Ref.13

Mutagenesis

188

1

E → Q: Reduces activity over 1000-fold. Ref.13

Mutagenesis

190

1

E → Q: Reduces activity 20-fold. Ref.13

Mutagenesis

230

1

K → M: Loss of activity. Ref.13

Mutagenesis

304

1

R → A: Reduces activity 400-fold. Ref.12

Sequence conflict

35

1

E → Q AA sequence Ref.4

Sequence conflict

274 – 276

3

GQS → SQE AA sequence Ref.6

Sequence conflict

276

1

S → E AA sequence Ref.6

Sequence conflict

294 – 296

3

KPW → WPK AA sequence Ref.6

Sequence conflict

354

1

S → R in CAA24246. Ref.7

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

10 – 23

14

Beta strand

29 – 33

5

Helix

37 – 46

10

Helix

53 – 64

12

Helix

68 – 73

6

Beta strand

74 – 79

6

Helix

81 – 84

4

Helix

94 – 100

7

Beta strand

104 – 108

5

Beta strand

113 – 115

3

Beta strand

119 – 121

3

Beta strand

123 – 125

3

Helix

131 – 140

10

Beta strand

145 – 152

8

Beta strand

155 – 157

3

Helix

161 – 180

20

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

246 – 260

15

Beta strand

267 – 270

4

Helix

277 – 289

13

Beta strand

296 – 303

8

Helix

304 – 314

11

Helix

318 – 320

3

Helix

321 – 338

18

Turn

339 – 341

3

Beta strand

358 – 360

3

Sequences

	Sequence		Length	Mass (Da)
	P00883-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E61BCBC60F668324	FASTA	364	39,343
	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

References

[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: 6546378] [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: 4417717] [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: 4812352] [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: 1122141] [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: 534504] [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: 1122142] [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: 6687628] [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: 4857186] [Abstract] Cited for: ACTIVE SITE.
[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: 5453] [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: 499203] [Abstract] Cited for: SUBSTRATE-BINDING SITE.
[11]	"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: 8989320] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[12]	"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: 10504235] [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.
[13]	"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: 11779856] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), MUTAGENESIS OF GLU-188; GLU-190 AND LYS-230.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

K02300 mRNA. Translation: AAA31156.1.
V00876 mRNA. Translation: CAA24245.1.
V00877 mRNA. Translation: CAA24246.1.

PIR

ADRBA. A92444.

RefSeq

NP_001075707.1.

UniGene

Ocu.864

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ADO	X-ray	1.90	A/B/C/D	2-364	[»]
1EWD	X-ray	2.46	A/B/C/D	2-364	[»]
1EWE	X-ray	2.60	A/B/C/D	2-364	[»]
1EX5	X-ray	2.20	A/B/C/D	2-364	[»]
1J4E	X-ray	2.65	A/B/C/D	2-363	[»]
1ZAH	X-ray	1.80	A/B/C/D	2-363	[»]
1ZAI	X-ray	1.76	A/B/C/D	2-363	[»]
1ZAJ	X-ray	1.89	A/B/C/D	2-363	[»]
1ZAL	X-ray	1.89	A/B/C/D	2-363	[»]
2OT0	X-ray	2.05	A/B/C/D	2-364	[»]
2OT1	X-ray	2.05	A/B/C/D	2-364	[»]
2QUT	X-ray	1.88	A/B/C/D	2-364	[»]
2QUU	X-ray	1.98	A/B/C/D	2-364	[»]
2QUV	X-ray	2.22	A/B/C/D	2-364	[»]
3B8D	X-ray	2.00	A/B/C/D	2-364	[»]
3BV4	X-ray	1.70	A	5-344	[»]
3DFN	X-ray	1.86	A/B/C/D	2-364	[»]
3DFO	X-ray	1.94	A/B/C/D	2-364	[»]
3DFP	X-ray	2.05	A/B/C/D	2-364	[»]
3DFQ	X-ray	1.82	A/B/C/D	2-364	[»]
3DFS	X-ray	2.03	A/B/C/D	2-364	[»]
3DFT	X-ray	1.94	A/B/C/D	2-364	[»]
6ALD	X-ray	2.30	A/B/C/D	2-364	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSOCUG00000006329. Oryctolagus cuniculus. [Contig view]

GeneID

100009055.

Phylogenomic databases

HOVERGEN

P00883.

Enzyme and pathway databases

BRENDA

4.1.2.13. 255.

Family and domain databases

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR11627. Aldolase_I. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

ProDom

PD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALDOA_RABIT

Accession

Primary (citable) accession number: P00883
Secondary accession number(s): Q28671

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)