ID   SCRK_STRMU              Reviewed;         293 AA.
AC   Q07211;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
GN   Name=scrK; OrderedLocusNames=SMU_1840;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=8336109; DOI=10.1099/00221287-139-5-921;
RA   Sato Y., Yamamoto Y., Kizaki H., Kuramitsu H.K.;
RT   "Isolation, characterization and sequence analysis of the scrK gene
RT   encoding fructokinase of Streptococcus mutans.";
RL   J. Gen. Microbiol. 139:921-927(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; D13175; BAA02467.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59463.1; -; Genomic_DNA.
DR   RefSeq; NP_722157.1; NC_004350.2.
DR   RefSeq; WP_002262656.1; NC_004350.2.
DR   AlphaFoldDB; Q07211; -.
DR   SMR; Q07211; -.
DR   STRING; 210007.SMU_1840; -.
DR   PRIDE; Q07211; -.
DR   EnsemblBacteria; AAN59463; AAN59463; SMU_1840.
DR   KEGG; smu:SMU_1840; -.
DR   PATRIC; fig|210007.7.peg.1643; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_3_0_9; -.
DR   OMA; DIQAYYI; -.
DR   PhylomeDB; Q07211; -.
DR   Proteomes; UP000002512; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..293
FT                   /note="Fructokinase"
FT                   /id="PRO_0000095686"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        139
FT                   /note="T -> A (in Ref. 1; BAA02467)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  31712 MW;  1089AF37B2C5B807 CRC64;
     MSKLYGSIEA GGTKFVCAVG DENFQILEKV QFPTTTPYET IEKTVAFFKK FEADLASVAI
     GSFGPIDIDQ NSDTYGYITS TPKPNWANVD FVGLISKDFK IPFYFTTDVN SSAYGETIAR
     SNVKSLVYYT IGTGIGAGTI QNGEFIGGMG HTEAGHVYMA PHPNDVHHGF VGTCPFHKGC
     LEGLAAGPSL EARTGIRGEL IEQNSEVWDI QAYYIAQAAI QATVLYRPQV IVFGGGVMAQ
     EHMLNRVREK FTSLLNDYLP VPDVKDYIVT PAVAENGSAT LGNLALAKKI AAR