ID   SCRK_FUSMR              Reviewed;          27 AA.
AC   Q09123;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
DE   Flags: Fragment;
GN   Name=scrK;
OS   Fusobacterium mortiferum.
OC   Bacteria; Fusobacteria; Fusobacterales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=850;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND INDUCTION.
RC   STRAIN=ATCC 25557 / CCUG 14475;
RX   MEDLINE=92250417; PubMed=1533618;
RA   Thompson J., Nguyen N.Y., Robrish S.A.;
RT   "Sucrose fermentation by Fusobacterium mortiferum ATCC 25557:
RT   transport, catabolism, and products.";
RL   J. Bacteriol. 174:3227-3235(1992).
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose = ADP + D-fructose 6-
CC       phosphate.
CC   -!- COFACTOR: Divalent metal cations. Maximum activity was observed
CC       with magnesium.
CC   -!- ENZYME REGULATION: Inhibition by zinc ions (Potential).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for ATP;
CC         KM=1.8 mM for magnesium;
CC         KM=0.4 mM for fructose;
CC         Vmax=74 umol/min/mg enzyme for fructose 6-phosphate;
CC       pH dependence:
CC         Optimum pH is 6.5-7.5;
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: Induced by sucrose.
CC   -!- SIMILARITY: Belongs to the ROK (nagC/xylR) family.
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DR   BRENDA; 2.7.1.4; 97866.
DR   GO; GO:0005623; C:cell; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044275; P:cellular carbohydrate catabolic process; IDA:UniProtKB.
DR   InterPro; IPR000600; ROK.
DR   PROSITE; PS01125; ROK; PARTIAL.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Direct protein sequencing;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase;
KW   Zinc.
FT   CHAIN         1    >27       Fructokinase.
FT                                /FTId=PRO_0000095682.
FT   NON_TER      27     27
SQ   SEQUENCE   27 AA;  2824 MW;  4721ABEF2E7BDCE9 CRC64;
     MIIGAVEAGG TKFVDGVGNE KGEIFER
//