Reviewed,
UniProtKB/Swiss-Prot P23917 (MAK_ECOLI)
Last modified
June 16, 2009.
Version 62.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Fructokinase EC=2.7.1.4 Alternative name(s): D-fructose kinase Manno(fructo)kinase | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 302 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 process | Carbohydrate metabolism |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructokinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
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. | |
| PIR | B64768. |
| RefSeq | AP_001045.1. NP_414928.2. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 949086. |
| GenomeReviews | Gene locus JW0385 in contig AP009048_GR. Gene locus b0394 in contig U00096_GR. |
| KEGG | ecj:JW0385. eco:b0394. |
Organism-specific databases | |
| EchoBASE | EB1265. |
| EcoGene | EG11288. mak. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P23917. |
| OMA | P23917. ECETPIR. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:EG11288-MON. MetaCyc:EG11288-MON. |
Family and domain databases | |
| InterPro | IPR000600. ROK. [Graphical view] |
| Pfam | PF00480. ROK. 1 hit. [Graphical view] |
| PROSITE | PS01125. ROK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MAK_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P23917 Secondary accession number(s): P71316, P75705, Q2MC31 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

Clusters with


