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UniProtKB/Swiss-Prot entry P23917


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAK_ECOLI
Primary accession number P23917
Secondary accession numbers P71316 P75705 Q2MC31
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on June 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 60)
Name and origin of the protein
Protein name Fructokinase
Synonyms EC 2.7.1.4
D-fructose kinase
Manno(fructo)kinase
Gene name
Name: mak
Synonyms: yajF
OrderedLocusNames: b0394, JW0385
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8807285 [NCBI, ExPASy, EBI, Israel, Japan]
Ryder L., Sharples G.J., Lloyd R.G.;
"Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12.";
Genetics 143:1101-1114(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-302.
PubMed=1744033 [NCBI, ExPASy, EBI, Israel, Japan]
Reeder T.C., Schleif R.F.;
"Mapping, sequence, and apparent lack of function of araJ, a gene of the Escherichia coli arabinose regulon.";
J. Bacteriol. 173:7765-7771(1991).
[6]
ROLE IN FRUCTOSE METABOLISM.
DOI=10.1073/pnas.211569798; PubMed=11742072 [NCBI, ExPASy, EBI, Israel, Japan]
Sproul A.A., Lambourne L.T., Jims J.-J.D., Kornberg H.L.;
"Genetic control of manno(fructo)kinase activity in Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 98:15257-15259(2001).
[7]
FUNCTION, SUBSTRATE SPECIFICITY, AND KINETIC PARAMETERS.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1021/bi049424m; PubMed=15157072 [NCBI, ExPASy, EBI, Israel, Japan]
Miller B.G., Raines R.T.;
"Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases.";
Biochemistry 43:6387-6392(2004).
Comments
  • FUNCTION: Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine.
  • CATALYTIC ACTIVITY: ATP + D-fructose = ADP + D-fructose 6-phosphate.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=1.3 mM for D-fructose (at 25 degrees Celsius and pH 7.6);
    KM=1.8 mM for ATP (at 25 degrees Celsius and pH 7.6);
    KM=59 mM for glucose (at 25 degrees Celsius and pH 7.6);
    Note=Catalytic efficiency with D-fructose as substrate is 55- fold higher than that with D-glucose;
  • SIMILARITY: Belongs to the ROK (nagC/xylR) 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
X76979; CAA54284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18118.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73497.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64787; AAA23475.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64768; B64768.
RefSeq AP_001045.1; -.
NP_414928.2; -.
3D structure databases
ModBase P23917.
Enzyme and pathway databases
BioCyc EcoCyc:EG11288-MON; -.
MetaCyc:EG11288-MON; -.
Organism-specific databases
EchoBASE EB1265; -.
EcoGene EG11288; mak.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008865; Molecular function: fructokinase activity (inferred from electronic annotation from EC).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000600; ROK.
Graphical view of domain structure.
Pfam PF00480; ROK; 1.
Pfam graphical view of domain structure.
PROSITE PS01125; ROK; 1.
ProtoNet P23917.
Genome annotation databases
GeneID 949086; -.
GenomeReviews U00096_GR; b0394.
AP009048_GR; JW0385.
KEGG ecj:JW0385; -.
eco:b0394; -.
Phylogenomic databases
HOGENOM P23917; -.
Genome annotation databases
CMR P23917; b0394.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   302  302     Fructokinase. PRO_0000095689
NP_BIND   4    11  8     ATP (Potential). 
NP_BIND   133   140  8     ATP (Potential). 
Sequence information
Length: 302 AA [This is the length of the unprocessed precursor] Molecular weight: 32500 Da [This is the MW of the unprocessed precursor] CRC64: 9791F9C29C91049C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRIGIDLGGT KTEVIALGDA GEQLYRHRLP TPRDDYRQTI ETIATLVDMA EQATGQRGTV 

        70         80         90        100        110        120 
GMGIPGSISP YTGVVKNANS TWLNGQPFDK DLSARLQREV RLANDANCLA VSEAVDGAAA 

       130        140        150        160        170        180 
GAQTVFAVII GTGCGAGVAF NGRAHIGGNG TAGEWGHNPL PWMDEDELRY REEVPCYCGK 

       190        200        210        220        230        240 
QGCIETFISG TGFAMDYRRL SGHALKGSEI IRLVEESDPV AELALRRYEL RLAKSLAHVV 

       250        260        270        280        290        300 
NILDPDVIVL GGGMSNVDRL YQTVGQLIKQ FVFGGECETP VRKAKHGDSS GVRGAAWLWP 


QE 

P23917 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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