ID   SCRK_LACLC              Reviewed;         290 AA.
AC   P82371;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
GN   Name=scrK; Synonyms=sacK;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NZ9800;
RX   PubMed=10074089; DOI=10.1128/jb.181.6.1924-1926.1999;
RA   Luesink E.J., Marugg J.D., Kuipers O.P., de Vos W.M.;
RT   "Characterization of the divergent sacBK and sacAR operons, involved in
RT   sucrose utilization by Lactococcus lactis.";
RL   J. Bacteriol. 181:1924-1926(1999).
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: Inactivated by EDTA (By similarity). Inhibition by
CC       zinc ions (Potential). {ECO:0000250, ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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   EMBL; Z97015; CAB09691.1; -; Genomic_DNA.
DR   AlphaFoldDB; P82371; -.
DR   SMR; P82371; -.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..290
FT                   /note="Fructokinase"
FT                   /id="PRO_0000095683"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
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   290 AA;  31610 MW;  FC3AB0101C352570 CRC64;
     MSVYYGSIEA GGTKFVLAIA DEHFNIIKKF KFATTTPQET ISKTIKYFKE NRVSAIGLGS
     FGPIDLNLSS KTYGYITSTP KVGWKNINLV GQLKEALDIP IYFTTDVNAS AYGEMKNTGI
     KNLVYLTIGT GIGGGAIQNG YFIGGIGHSE MGHQRINRHR DVLTFEGICP FHGDCLEGVA
     AGPSLEARTG ILGEKISSDD PIWDILSYYI AQAAINATLT LAPECIILGG GVMEKPNMIS
     LIQKQFISML NNYIDLPCSV EKYIRLPTVK ENGSATLGNF YLAYSLFTKE