Reviewed, UniProtKB/Swiss-Prot P00884 (ALDOB_RAT)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase B
    EC=4.1.2.13
Alternative name(s):
    Liver-type aldolase

Gene names

Name:

Aldob

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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	Homotetramer.
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.
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	gluconeogenesis Inferred from physical interaction. Source: RGD glycolysis Inferred from direct assay. Source: RGD response to carbohydrate stimulus Inferred from expression pattern. Source: RGD response to copper ion Inferred from expression pattern. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to peptide hormone stimulus Inferred from direct assay. Source: RGD response to starvation Inferred from expression pattern. Source: RGD response to zinc ion Inferred from direct assay. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD lysosome Inferred from direct assay. Source: RGD nucleus Inferred from direct assay. Source: RGD perinuclear region of cytoplasm Inferred from direct assay. Source: RGD
Molecular function	fructose-bisphosphate aldolase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 364

363

Fructose-bisphosphate aldolase B

PRO_0000216943

Sites

Active site

188

1

Proton acceptor By similarity

Active site

230

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

56

1

Substrate

Binding site

147

1

Substrate

Site

364

1

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

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

36

1

Phosphoserine By similarity

Experimental info

Sequence conflict

234

1

L → V in CAA26156. Ref.2

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

9 – 23

15

Helix

24 – 26

3

Beta strand

28 – 32

5

Helix

36 – 46

11

Helix

52 – 63

12

Helix

67 – 71

5

Beta strand

73 – 78

6

Helix

80 – 84

5

Beta strand

88 – 90

3

Helix

93 – 100

8

Beta strand

103 – 107

5

Beta strand

111 – 114

4

Beta strand

118 – 120

3

Beta strand

122 – 125

4

Helix

130 – 140

11

Beta strand

144 – 151

8

Helix

160 – 179

20

Beta strand

183 – 190

8

Helix

198 – 218

21

Helix

223 – 225

3

Helix

245 – 259

15

Beta strand

266 – 269

4

Helix

276 – 288

13

Beta strand

295 – 302

8

Helix

303 – 313

11

Helix

317 – 319

3

Helix

320 – 339

20

Beta strand

344 – 346

3

Beta strand

352 – 356

5

Sequences

	Sequence		Length	Mass (Da)
	P00884-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E120FC119F0180F8	FASTA	364	39,618
	10 20 30 40 50 60 MAHRFPALTS EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 70 80 90 100 110 120 ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN 130 140 150 160 170 180 KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRISDQCPS SLAIQENANA LARYASICQQ 190 200 210 220 230 240 NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMLTAGHAC 250 260 270 280 290 300 TKKYTPEQVA MATVTALHRT VPAAVPSICF LSGGMSEEDA TLNLNAIYRC PLPRPWKLSF 310 320 330 340 350 360 SYGRALQASA LAAWGGKAAN KKATQEAFMK RAVANCQAAQ GQYVHTGSSG AASTQSLFTA SYTY

References

[1]	"Nucleotide sequence of rat liver aldolase B messenger RNA." Tsutsumi K., Mukai T., Tsutsumi R., Mori M., Daimon M., Tanaka T., Yatsuki H., Hori K., Ishikawa K. J. Biol. Chem. 259:14572-14575(1984) [PubMed: 6094564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and genomic organization of the rat aldolase B gene." Tsutsumi K., Mukai T., Tsutsumi R., Hidaka S., Arai Y., Hori K., Ishikawa K. J. Mol. Biol. 181:153-160(1985) [PubMed: 2580098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley.
[3]	"Rat aldolase isozyme gene." Tsutsumi K., Mukai T., Hidaka S., Miyahara H., Tsutsumi R., Tanaka T., Hori K., Ishikawa K. J. Biol. Chem. 258:6537-6542(1983) [PubMed: 6304044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 185-364.
[4]	"Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa Zn(2+)-binding protein (parathymosin)." Brand I.A., Heinickel A. J. Biol. Chem. 266:20984-20989(1991) [PubMed: 1834654] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-68.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M10149 mRNA. Translation: AAA40716.1.
X02284 , X02285, X02286, X02287, X02288, X02289, X02290, X02291 Genomic DNA. Translation: CAA26156.1.
V01223 mRNA. Translation: CAA24533.1.

IPI

IPI00471911.

PIR

ADRTB. A22585.

UniGene

Rn.98207

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N30	model	-	A	1-364	[»]

SMR

P00884. Positions 2-364.

ModBase

Search...

Protein-protein interaction databases

STRING

P00884.

Genome annotation databases

Ensembl

ENSRNOT00000009111; ENSRNOP00000009111; ENSRNOG00000006807; Rattus norvegicus. [Genome view]
ENSRNOT00000059880; ENSRNOP00000056625; ENSRNOG00000006807; Rattus norvegicus. [Genome view]

Organism-specific databases

RGD

2090. Aldob.

Phylogenomic databases

HOVERGEN

P00884.

Enzyme and pathway databases

BRENDA

4.1.2.13. 248.

Gene expression databases

ArrayExpress

P00884.

Genevestigator

P00884.

GermOnline

ENSRNOG00000006807. Rattus norvegicus.

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

ALDOB_RAT

Accession

Primary (citable) accession number: P00884
Secondary accession number(s): P70706

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)