[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2985560 [NCBI, ExPASy, EBI, Israel, Japan] Burgess D.G., Penhoet E.E.; "Characterization of the chicken aldolase B gene."; J. Biol. Chem. 260:4604-4614(1985).

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: 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.
SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.

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

M10946; AAA48587.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A22568; ADCHB.

NP_001007978.1; -.

3D structure databases

HSSP

P79226; 1FDJ. [HSSP ENTRY / PDB]

SMR

P07341; 3-364.

ModBase

P07341.

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

ENSGALG00000015544; Gallus gallus. [Contig view]

GeneID

427308; -.

KEGG

gga:427308; -.

Phylogenomic databases

HOGENOM

P07341; -.

HOVERGEN

P07341; -.

Other

UniRef

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

Keywords

Glycolysis; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase B.`	`PRO_0000216945`
`ACT_SITE`	`188 188`		`Proton acceptor (By similarity).`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P (By similarity).`
`BINDING`	`56 56`		`Substrate (By similarity).`
`BINDING`	`147 147`		`Substrate (By similarity).`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate (By similarity).`

Sequence information

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

Molecular weight: 39296 Da [This is the MW of the unprocessed precursor]

CRC64: 40E0C300FB574CEB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTHQFPALSP EQKKALSDIA QRIVASGKGI LAADESVGTM GNRLQRINVE NTEENRRAFR 

        70         80         90        100        110        120 
EILFSSDASI SKSIGGVILF HETLYQKDSS GKPFPAIIKE KGMVVGIKLD AGTAPLAGTN 

       130        140        150        160        170        180 
GETTIQGLDK LAERCAQYKK DGADFGKWRA VLKISSTTPS QLAIQENANT LARYASICQQ 

       190        200        210        220        230        240 
NGLVPIVEPE VLPDGDHDLQ RCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHSC 

       250        260        270        280        290        300 
PKKYTPQDVA VATVTTLLRT VPAAVPGICF LSGGQSEEEA SLNLNAMNQS PLPKPWKLTF 

       310        320        330        340        350        360 
SYGRALQASA LAAWLGKSEN KKAAQEAFCK RAQINSLACR GQYVTSGKTD TAATQSLFTA 


SYTY

P07341 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