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Reviewed, UniProtKB/Swiss-Prot P23917 (MAK_ECOLI)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fructokinase
    EC=2.7.1.4
Alternative name(s):
    D-fructose kinase
    Manno(fructo)kinase
Gene names
Name: mak
Synonyms: yajF
Ordered Locus Names: b0394, JW0385
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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. Ref.6 Ref.7

Catalytic activity

ATP + D-fructose = ADP + D-fructose 6-phosphate.

Sequence similarities

Belongs to the ROK (nagC/xylR) family.

Biophysicochemical properties

Kinetic parameters:

Catalytic efficiency with D-fructose as substrate is 55-fold higher than that with D-glucose.

KM=1.3 mM for D-fructose (at 25 degrees Celsius and pH 7.6) Ref.7

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)

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fructokinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Fructokinase
PRO_0000095689

Regions

Nucleotide binding4 – 118ATP Potential
Nucleotide binding133 – 1408ATP Potential

Sequences

Sequence LengthMass (Da)Tools
P23917-1 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9791F9C29C91049C

FASTA30232,500
        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 

« Hide

References

« Hide 'large scale' references
[1]"Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains of Escherichia coli K-12."
Ryder L., Sharples G.J., Lloyd R.G.
Genetics 143:1101-1114(1996) [PubMed: 8807285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Sequence of minutes 4-25 of Escherichia coli."
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.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Mapping, sequence, and apparent lack of function of araJ, a gene of the Escherichia coli arabinose regulon."
Reeder T.C., Schleif R.F.
J. Bacteriol. 173:7765-7771(1991) [PubMed: 1744033] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-302.
[6]"Genetic control of manno(fructo)kinase activity in Escherichia coli."
Sproul A.A., Lambourne L.T., Jims J.-J.D., Kornberg H.L.
Proc. Natl. Acad. Sci. U.S.A. 98:15257-15259(2001) [PubMed: 11742072] [Abstract]
Cited for: ROLE IN FRUCTOSE METABOLISM.
[7]"Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases."
Miller B.G., Raines R.T.
Biochemistry 43:6387-6392(2004) [PubMed: 15157072] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Cross-references

Sequence databases

X76979 Genomic DNA. Translation: CAA54284.1.
U73857 Genomic DNA. Translation: AAB18118.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73497.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE76175.1.
M64787 Genomic DNA. Translation: AAA23475.1.
PIRB64768.
RefSeqAP_001045.1.
NP_414928.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID949086.
GenomeReviewsGene locus JW0385 in contig AP009048_GR.
Gene locus b0394 in contig U00096_GR.
KEGGecj:JW0385.
eco:b0394.

Organism-specific databases

EchoBASEEB1265.
EcoGeneEG11288. mak.
CMRSearch...

Phylogenomic databases

HOGENOMP23917.
OMAP23917. ECETPIR.

Enzyme and pathway databases

BioCycEcoCyc:EG11288-MON.
MetaCyc:EG11288-MON.

Family and domain databases

InterProIPR000600. ROK.
[Graphical view]
PfamPF00480. ROK. 1 hit.
[Graphical view]
PROSITEPS01125. ROK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMAK_ECOLI
AccessionPrimary (citable) accession number: P23917
Secondary accession number(s): P71316, P75705, Q2MC31
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents