SCRK_FUSMR
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 25-MAY-2022, entry version 58.
DE RecName: Full=Fructokinase;
DE EC=2.7.1.4;
DE Flags: Fragment;
GN Name=scrK {ECO:0000250|UniProtKB:O05510};
OS Fusobacterium mortiferum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=850;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 25557 / DSM 19809 / CCUG 14475 / VPI 4123A;
RX PubMed=1533618; DOI=10.1128/jb.174.10.3227-3235.1992;
RA Thompson J., Nguyen N.Y., Robrish S.A.;
RT "Sucrose fermentation by Fusobacterium mortiferum ATCC 25557: transport,
RT catabolism, and products.";
RL J. Bacteriol. 174:3227-3235(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.4;
CC Evidence={ECO:0000269|PubMed:1533618};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1533618};
CC Note=Divalent metal cations. Maximum activity was observed with Mg(2+).
CC {ECO:0000269|PubMed:1533618};
CC -!- ACTIVITY REGULATION: Inhibition by zinc ions.
CC {ECO:0000250|UniProtKB:O05510, ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for ATP {ECO:0000269|PubMed:1533618};
CC KM=1.8 mM for magnesium {ECO:0000269|PubMed:1533618};
CC KM=0.4 mM for fructose {ECO:0000269|PubMed:1533618};
CC Vmax=74 umol/min/mg enzyme for fructose 6-phosphate
CC {ECO:0000269|PubMed:1533618};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:1533618};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1533618}.
CC -!- INDUCTION: Induced by sucrose. {ECO:0000269|PubMed:1533618}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; Q09123; -.
DR SMR; Q09123; -.
DR SABIO-RK; Q09123; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..>27
FT /note="Fructokinase"
FT /id="PRO_0000095682"
FT NON_TER 27
FT /evidence="ECO:0000303|PubMed:1533618"
SQ SEQUENCE 27 AA; 2824 MW; 4721ABEF2E7BDCE9 CRC64;
MIIGAVEAGG TKFVDGVGNE KGEIFER