ID   SCRK_PEDPE              Reviewed;         288 AA.
AC   P43468;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
GN   Name=scrK;
OS   Pediococcus pentosaceus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=1255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPE1.0;
RA   Leenhouts K.K.J., Bolhuis A.A., Kok J.J., Venema G.G.;
RT   "The sucrose and raffinose operons of Pediococcus pentosaceus PPE1.0.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibition by zinc ions. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; Z32771; CAA83667.1; -; Genomic_DNA.
DR   EMBL; L32093; AAA25565.1; -; Genomic_DNA.
DR   PIR; S44256; S44256.
DR   AlphaFoldDB; P43468; -.
DR   SMR; P43468; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..288
FT                   /note="Fructokinase"
FT                   /id="PRO_0000095685"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  30668 MW;  3EDDBD9781B7E3E4 CRC64;
     MLLGAIEAGG TKFVCATGAE NGQVSDRISI PTTTPVETMT AVDDYFTTHP VDAIGIGSFG
     PIGVNPHDPK YGYITTTPKP GWGDFDFLGH LKSQFNIPLY WTTDVNEAAY GESMIGIAKD
     VPNSIYMTIG TGVGAGVISQ NHIFNGRTHT ELGHMRLNRL PGDDFKSNCP YHDICLEGLA
     AGPAVGKRTG KAGKDIPVDD PVWPIITDYI AQACVNLTVA FAPDKIILNG GVMNQRQLFP
     MIREKFAAYL NGYEEVPPLD DYIVPAGLGN NSGIAGGLLL AQAALKNA