Fructose-bisphosphate aldolase B - Mus musculus (Mouse)

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Q91Y97 (ALDOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Fructose-bisphosphate aldolase B
EC=4.1.2.13

Alternative name(s):
Aldolase 2
Liver-type aldolase

Gene names

Name:	Aldob
Synonyms:	Aldo2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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 By similarity.
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADH oxidation Inferred from electronic annotation. Source: Compara fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: Compara fructose metabolic process Inferred from electronic annotation. Source: Compara glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway positive regulation of ATPase activity Inferred from electronic annotation. Source: Compara vacuolar proton-transporting V-type ATPase complex assembly Inferred from electronic annotation. Source: Compara
Cellular_component	centriolar satellite Inferred from electronic annotation. Source: Compara
Molecular_function	fructose binding Inferred from electronic annotation. Source: Compara 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

Removed Ref.3

Chain

2 – 364

363

Fructose-bisphosphate aldolase B

PRO_0000216941

Sites

Active site

188

Proton acceptor By similarity

Active site

230

Schiff-base intermediate with dihydroxyacetone-P

Binding site

Substrate

Binding site

147

Substrate

Site

364

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

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

Phosphoserine Ref.4

Experimental info

Sequence conflict

H → Y in AAH34173. Ref.2

Sequence conflict

155 – 156

AD → DH in AAL06323. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q91Y97 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E6CD995D0073ED47
Show »

FASTA

364

39,507

        10         20         30         40         50         60 
MAHRFPALTP EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 

        70         80         90        100        110        120 
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GNLFRNVLKE KGIVVGIKLD QGGAPLAGTN 

       130        140        150        160        170        180 
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ 

       190        200        210        220        230        240 
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 

       250        260        270        280        290        300 
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINRC PLPRPWKLSF 

       310        320        330        340        350        360 
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAMANCQAAQ GQYVHTGSSG AAATQSLFTA 


SYTY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse aldolase B (aldo2) genomic sequence of the open reading frame including first poly A site and signals." Funari V.A., Tolan D.R. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon, Kidney and Liver.
[3]	Kanor S., Quadroni M., Bienvenut W.V. Submitted (MAR-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12 AND 108-120, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Strain: C57BL/6J. Tissue: Skeletal muscle.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF403567, AF403565, AF403566 Genomic DNA. Translation: AAL06323.1. BC016435 mRNA. Translation: AAH16435.1. BC022113 mRNA. Translation: AAH22113.1. BC024056 mRNA. Translation: AAH24056.1. BC024112 mRNA. Translation: AAH24112.1. BC026577 mRNA. Translation: AAH26577.1. BC030724 mRNA. Translation: AAH30724.1. BC030725 mRNA. Translation: AAH30725.1. BC034169 mRNA. Translation: AAH34169.1. BC034171 mRNA. Translation: AAH34171.1. BC034172 mRNA. Translation: AAH34172.1. BC034173 mRNA. Translation: AAH34173.1. BC036130 mRNA. Translation: AAH36130.1. BC036131 mRNA. Translation: AAH36131.1. BC036132 mRNA. Translation: AAH36132.1. BC036133 mRNA. Translation: AAH36133.1.
IPI	IPI00127206.
RefSeq	NP_659152.1. NM_144903.2.
UniGene	Mm.482116.
3D structure databases
ProteinModelPortal	Q91Y97.
SMR	Q91Y97. Positions 2-349.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000029987.
PTM databases
PhosphoSite	Q91Y97.
Proteomic databases
PaxDb	Q91Y97.
PRIDE	Q91Y97.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029987; ENSMUSP00000029987; ENSMUSG00000028307.
GeneID	230163.
KEGG	mmu:230163.
Organism-specific databases
CTD	229.
MGI	MGI:87995. Aldob.
Phylogenomic databases
eggNOG	COG3588.
GeneTree	ENSGT00390000010235.
HOGENOM	HOG000220876.
HOVERGEN	HBG002386.
InParanoid	Q91Y97.
KO	K01623.
OMA	IDNQCPS.
OrthoDB	EOG444KKK.
Enzyme and pathway databases
UniPathway	UPA00109; UER00183.
Gene expression databases
ArrayExpress	Q91Y97.
Bgee	Q91Y97.
CleanEx	MM_ALDOB.
Genevestigator	Q91Y97.
GermOnline	ENSMUSG00000028307. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view]
PANTHER	PTHR11627. PTHR11627. 1 hit.
Pfam	PF00274. Glycolytic. 1 hit. [Graphical view]
PROSITE	PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ALDOB. mouse.
NextBio	379836.
SOURCE	Search...

Entry information

Entry name

ALDOB_MOUSE

Accession

Primary (citable) accession number: Q91Y97
Secondary accession number(s): Q8K034, Q91W73

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents