[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=6094564 [NCBI, ExPASy, EBI, Israel, Japan] Tsutsumi K., Mukai T., Tsutsumi R., Mori M., Daimon M., Tanaka T., Yatsuki H., Hori K., Ishikawa K.; "Nucleotide sequence of rat liver aldolase B messenger RNA."; J. Biol. Chem. 259:14572-14575(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Sprague-Dawley; DOI=10.1016/0022-2836(85)90081-6; PubMed=2580098 [NCBI, ExPASy, EBI, Israel, Japan] Tsutsumi K., Mukai T., Tsutsumi R., Hidaka S., Arai Y., Hori K., Ishikawa K.; "Structure and genomic organization of the rat aldolase B gene."; J. Mol. Biol. 181:153-160(1985).
[3]	NUCLEOTIDE SEQUENCE OF 185-364. PubMed=6304044 [NCBI, ExPASy, EBI, Israel, Japan] Tsutsumi K., Mukai T., Hidaka S., Miyahara H., Tsutsumi R., Tanaka T., Hori K., Ishikawa K.; "Rat aldolase isozyme gene."; J. Biol. Chem. 258:6537-6542(1983).
[4]	PROTEIN SEQUENCE OF 41-68. PubMed=1834654 [NCBI, ExPASy, EBI, Israel, Japan] Brand I.A., Heinickel A.; "Key enzymes of carbohydrate metabolism as targets of the 11.5-kDa Zn(2+)-binding protein (parathymosin)."; J. Biol. Chem. 266:20984-20989(1991).

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

M10149; AAA40716.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02284; CAA26156.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02285; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02286; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02287; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02288; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02289; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02290; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X02291; CAA26156.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V01223; CAA24533.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A22585; ADRTB.

UniGene

Rn.98207

3D structure databases

PDB

1N30; Model; -; A=1-364.

[ExPASy / RCSB / EBI]

1N30; -.

P00884; 2-364.

Organism-specific databases

RGD

2090; Aldob.

Gene expression databases

ArrayExpress

P00884; -.

GermOnline

ENSRNOG00000006807; Rattus norvegicus.

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

ENSRNOG00000006807; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P00884; -.

Other

UniRef

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

Keywords

3D-structure; Acetylation; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 364`	`363`	`Fructose-bisphosphate aldolase B.`	`PRO_0000216943`
`ACT_SITE`	`188 188`		`Proton acceptor (By similarity).`
`ACT_SITE`	`230 230`		`Schiff-base intermediate with dihydroxyacetone-P.`
`BINDING`	`56 56`		`Substrate.`
`BINDING`	`147 147`		`Substrate.`
`SITE`	`364 364`	`1`	`Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate.`
`MOD_RES`	`2 2`		`N-acetylalanine (By similarity).`
`MOD_RES`	`36 36`		`Phosphoserine (By similarity).`
`CONFLICT`	`234 234`		`L -> V (in Ref. 2; CAA26156).`
`HELIX`	`9 23`	`15`
`HELIX`	`24 26`	`3`
`STRAND`	`28 32`	`5`
`HELIX`	`36 46`	`11`
`HELIX`	`52 63`	`12`
`HELIX`	`67 71`	`5`
`STRAND`	`73 78`	`6`
`HELIX`	`80 84`	`5`
`STRAND`	`88 90`	`3`
`HELIX`	`93 100`	`8`
`STRAND`	`103 107`	`5`
`STRAND`	`111 114`	`4`
`STRAND`	`118 120`	`3`
`STRAND`	`122 125`	`4`
`HELIX`	`130 140`	`11`
`STRAND`	`144 151`	`8`
`HELIX`	`160 179`	`20`
`STRAND`	`183 190`	`8`
`HELIX`	`198 218`	`21`
`HELIX`	`223 225`	`3`
`HELIX`	`245 259`	`15`
`STRAND`	`266 269`	`4`
`HELIX`	`276 288`	`13`
`STRAND`	`295 302`	`8`
`HELIX`	`303 313`	`11`
`HELIX`	`317 319`	`3`
`HELIX`	`320 339`	`20`
`STRAND`	`344 346`	`3`
`STRAND`	`352 356`	`5`

Sequence information

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

Molecular weight: 39618 Da [This is the MW of the unprocessed precursor]

CRC64: E120FC119F0180F8 [This is a checksum on the sequence]

        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

P00884 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