Reviewed, UniProtKB/Swiss-Prot P79226 (ALDOB_RABIT)

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
Synonyms:	ALDB

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	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
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 By similarity

Chain

2 – 364

363

Fructose-bisphosphate aldolase B

PRO_0000216942

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

Secondary structure

1

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364

Helix Strand Turn

Details...

Helix

10 – 24

15

Helix

25 – 27

3

Beta strand

29 – 33

5

Helix

37 – 46

10

Helix

53 – 64

12

Helix

68 – 72

5

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

Helix

161 – 180

20

Beta strand

184 – 191

8

Helix

199 – 219

21

Helix

224 – 226

3

Helix

246 – 258

13

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

353 – 357

5

Sequences

	Sequence		Length	Mass (Da)
	P79226-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 65A58A50906EA954	FASTA	364	39,605
	10 20 30 40 50 60 MAHRFPALTP EQKKELSDIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 70 80 90 100 110 120 EILFTVDNSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE KGIVVGIKLD QGGAPLAGTN 130 140 150 160 170 180 KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANT LARYASICQQ 190 200 210 220 230 240 NGLVPIVEPE VIPDGDHDLE HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 250 260 270 280 290 300 TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF 310 320 330 340 350 360 SYGRALQASA LAAWGGKAEN KKATQEAFMK RAVVNCQAAK GQYVHTGSSG AASTQSLFTA SYTY

References

[1]	"Identification of conserved promoter elements for aldB and isozyme specific residues in aldolase B." Berardini T.Z., Amsden A.B., Penhoet E.E., Tolan D.R. Comp. Biochem. Physiol. 122B:53-61(1999) [PubMed: 10327593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Enhanced electron-density envelopes by extended solvent definition." Blom N., Sygush J. Acta Crystallogr. D 54:461-466(1998) [PubMed: 9761929] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U85645 Genomic DNA. Translation: AAB42087.1.

PIR

A28856.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FDJ	X-ray	2.10	A/B/C/D	2-363	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSOCUG00000014944. Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGEN

P79226.

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

ALDOB_RABIT

Accession

Primary (citable) accession number: P79226

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)