ID   SCRK_ZYMMO              Reviewed;         301 AA.
AC   Q03417; Q5NLR7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
GN   Name=frk; OrderedLocusNames=ZMO1719;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC   11199 / NRRL B-4490 / ZM6;
RX   PubMed=1317376; DOI=10.1128/jb.174.11.3455-3460.1992;
RA   Zembrzuski B., Chilco P., Liu X.L., Liu J., Conway T., Scopes R.K.;
RT   "Cloning, sequencing, and expression of the Zymomonas mobilis fructokinase
RT   gene and structural comparison of the enzyme with other hexose kinases.";
RL   J. Bacteriol. 174:3455-3460(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
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:0000305};
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; M97296; AAA27687.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV90343.1; -; Genomic_DNA.
DR   PIR; A41894; A41894.
DR   RefSeq; WP_011241465.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q03417; -.
DR   SMR; Q03417; -.
DR   STRING; 264203.ZMO1719; -.
DR   EnsemblBacteria; AAV90343; AAV90343; ZMO1719.
DR   GeneID; 58027431; -.
DR   KEGG; zmo:ZMO1719; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_3_0_5; -.
DR   OMA; DIQAYYI; -.
DR   OrthoDB; 1130699at2; -.
DR   Proteomes; UP000001173; Chromosome.
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; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..301
FT                   /note="Fructokinase"
FT                   /id="PRO_0000095687"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32609 MW;  F94EF75DE5E91228 CRC64;
     MKNDKKIYGC IEGGGTKFML ALIDSDRKML AVERVPTTTP EETLGKSVEF FKKALPQYAD
     SFASFGIASF GPLCLDRKSP KWGYITNTPK PFWPNTDVVT PFKEAFGCPV EIDTDVNGAA
     LAENFWGASK GTHTSVYVTV GTGFGGGVLI DGKPIHGLAH PEMGHGIPIR HPDDRDFEGC
     CPYHGGCYEG LASGTAIRKR WGKALNEMEP AEFEKAREII AFYLAHFNVT LQAFISPERI
     VFGGGVMHVD GMLASVRRQT AEIANSYFEG ADFEKIIVLP GLGDQAGMMG AFALALAAEN
     K