[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=KOD1; Imanaka H., Fukui T., Atomi H., Imanaka T.; "Fructose-1,6-bisphosphate aldolase from Thermococcus kodakaraensis KOD1."; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=KOD1; DOI=10.1101/gr.3003105; PubMed=15710748 [NCBI, ExPASy, EBI, Israel, Japan] Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."; Genome Res. 15:352-363(2005).

Comments

CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
ENZYME REGULATION: Activated by citrate (By similarity).
SUBUNIT: Homooctamer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the deoC/fbaB 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

AB083709; BAC21177.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP006878; BAD85178.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_183402.1; -.

3D structure databases

HSSP

P58315; 1OJX. [HSSP ENTRY / PDB]

ModBase

Q8J308.

Enzyme and pathway databases

BioCyc

TKOD69014:TK0989-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

Q8J308.

Genome annotation databases

3233691; -.

AP006878_GR; TK0989.

tko:TK0989; -.

fig|69014.3.peg.631; -.

Phylogenomic databases

HOGENOM

Q8J308; -.

Genome annotation databases

CMR

Q8J308; TK0989.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Glycolysis; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 281`	`281`	`Fructose-bisphosphate aldolase class 1.`	`PRO_0000138951`
`ACT_SITE`	`191 191`		`Schiff-base intermediate with dihydroxyacetone-P (By similarity).`

Sequence information

Length: 281 AA [This is the length of the unprocessed precursor]

Molecular weight: 31240 Da [This is the MW of the unprocessed precursor]

CRC64: 9A95B90F50324B79 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDAYQSVGIR RRLKRFFRRD GRALIFAMDH GFEHGPTDFE PVWEHVNPRI IIRKVVRAGV 

        70         80         90        100        110        120 
DGVMMLPGIV RMAGDELKPD TGLMIKLTSK TELRPKEEQL LQSQLGYVED AIKLGADAIA 

       130        140        150        160        170        180 
ATVYWGSPQE DVMMRQFAEI ASYAHDLGFP VVQFAYPRGP YINEKYGKKE DYRVVMYGAR 

       190        200        210        220        230        240 
AAAETGADMI KTYWTGSKET FAKVVDAAAG VPVLLSGGAK TDNPVDFLKV VWDVIEAGGA 

       250        260        270        280 
GAVVGRNIFQ RENPEPMIKA LIRVIHRNED PEEAAKAEGL I

Q8J308 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