NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

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 .
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

BA000033; BAB96390.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_647342.1; -.

3D structure databases

HSSP

P00883; 1EWD. [HSSP ENTRY / PDB]

ModBase

Q8NUM5.

Enzyme and pathway databases

BioCyc

SAUR196620:MW2525-MON; -.

Ontologies

GO:0004332;	Molecular function: fructose-bisphosphate aldolase activity (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00729; -; 1.
PBIL [Tree]

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; FALSE_NEG.

ProtoNet

Q8NUM5.

Genome annotation databases

GeneID

1004661; -.

GenomeReviews

BA000033_GR; MW2525.

KEGG

sam:MW2525; -.

Phylogenomic databases

HOGENOM

Q8NUM5; -.

Genome annotation databases

CMR

Q8NUM5; MW2525.

Other

UniRef

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

Keywords

Complete proteome; Glycolysis; Lyase; Schiff base.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 296`	`295`	`Fructose-bisphosphate aldolase class 1.`	`PRO_0000216908`
`ACT_SITE`	`175 175`		`Proton acceptor (By similarity).`
`ACT_SITE`	`212 212`		`Schiff-base intermediate with dihydroxyacetone-P (By similarity).`

Sequence information

Length: 296 AA [This is the length of the unprocessed precursor]

Molecular weight: 32967 Da [This is the MW of the unprocessed precursor]

CRC64: C6D620FBD9F76E96 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS 

        70         80         90        100        110        120 
PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID 

       130        140        150        160        170        180 
NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI 

       190        200        210        220        230        240 
NAKDKAEIEK VLKAELKKGL DNLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG 

       250        260        270        280        290 
YSREKANELL KDNAELIASF SRALASDLRA GQSKEEFDKA LGDAVESIYD ASVNKN

Q8NUM5 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