[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; Close T.J., Choi D.W.; Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION, AND MASS SPECTROMETRY. PubMed=9531482 [NCBI, ExPASy, EBI, Israel, Japan] Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A.; "The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase."; Biochem. J. 331:437-445(1998).
[5]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-262, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.; "Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli."; Mol. Cell. Proteomics 0:0-0(2008).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
ENZYME REGULATION: Activated by citrate.
SUBUNIT: Homooctamer or homodecamer.
SUBCELLULAR LOCATION: Cytoplasm (Probable).
MASS SPECTROMETRY: Mass=37979.3; Method=MALDI; Range=2-350; Source=PubMed:9531482;.
SIMILARITY: Belongs to the deoC/fbaB aldolase family. FbaB subfamily.
CAUTION: Was originally (Ref.1) thought to be a dehydrin.

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

U73760; AAB18249.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75158.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76584.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

AP_002695.1; -.
NP_416600.4; -.

3D structure databases

ModBase

P0A991.

Enzyme and pathway databases

BioCyc

EcoCyc:FRUCBISALD-CLASSI-MON; -.
MetaCyc:FRUCBISALD-CLASSI-MON; -.

Organism-specific databases

EchoBASE

EB3815; -.

EcoGene

EG14062; fbaB.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR002915; DeoC/AroFGH_arch.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01791; DeoC; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

946632; -.

GenomeReviews

AP009048_GR; JW5344.
U00096_GR; b2097.

KEGG

ecj:JW5344; -.
eco:b2097; -.

Phylogenomic databases

HOGENOM

P0A991; -.

Genome annotation databases

CMR

P0A991; b2097.

Other

ProtoNet

P0A991.

UniRef

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

Keywords

Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 350`	`349`	`Fructose-bisphosphate aldolase class 1.`	`PRO_0000138939`
`ACT_SITE`	`237 237`		`Schiff-base intermediate with dihydroxyacetone-P.`
`MOD_RES`	`208 208`		`N6-acetyllysine.`
`MOD_RES`	`262 262`		`N6-acetyllysine.`
`MUTAGEN`	`237 237`		`K->A: Loss of activity.`
`MUTAGEN`	`239 239`		`K->A: No change in activity.`
`CONFLICT`	`192 192`		`L -> V (in Ref. 1; AAB18249).`
`CONFLICT`	`309 309`		`N -> I (in Ref. 1; AAB18249).`

Sequence information

Length: 350 AA [This is the length of the unprocessed precursor]

Molecular weight: 38109 Da [This is the MW of the unprocessed precursor]

CRC64: 462341BE2459E587 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL RNMQTLYNTG 

        70         80         90        100        110        120 
RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL AIEAGCNCVA STYGVLASVS 

       130        140        150        160        170        180 
RRYAHRIPFL VKLNHNETLS YPNTYDQTLY ASVEQAFNMG AVAVGATIYF GSEESRRQIE 

       190        200        210        220        230        240 
EISAAFERAH ELGMVTVLWA YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM 

       250        260        270        280        290        300 
AENNGGYKAI NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS 

       310        320        330        340        350 
DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA

P0A991 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