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   16-JUN-2009, entry version 54.
DE   RecName: Full=Fructokinase;
DE            EC=2.7.1.4;
GN   Name=scrK; OrderedLocusNames=SMU_1840;
OS   Streptococcus mutans.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   MEDLINE=93329360; PubMed=8336109;
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 / Serotype c;
RX   MEDLINE=22295063; PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   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: ATP + D-fructose = ADP + D-fructose 6-
CC       phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Inhibition by zinc ions (Potential).
CC   -!- SIMILARITY: Belongs to the ROK (nagC/xylR) family.
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DR   EMBL; D13175; BAA02467.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59463.1; -; Genomic_DNA.
DR   RefSeq; NP_722157.1; -.
DR   GeneID; 1029053; -.
DR   GenomeReviews; AE014133_GR; SMU_1840.
DR   KEGG; smu:SMU.1840; -.
DR   NMPDR; fig|210007.1.peg.1670; -.
DR   HOGENOM; Q07211; -.
DR   OMA; Q07211; GMAAGPS.
DR   BioCyc; SMUT210007:SMU_1840-MON; -.
DR   BRENDA; 2.7.1.4; 20716.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000600; ROK.
DR   Pfam; PF00480; ROK; 1.
DR   PROSITE; PS01125; ROK; FALSE_NEG.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    293       Fructokinase.
FT                                /FTId=PRO_0000095686.
FT   NP_BIND     236    240       ATP (By similarity).
FT   METAL       156    156       Zinc (By similarity).
FT   METAL       174    174       Zinc (By similarity).
FT   METAL       177    177       Zinc (By similarity).
FT   METAL       180    180       Zinc (By similarity).
FT   BINDING     133    133       ATP (By similarity).
FT   BINDING     188    188       ATP; via imide nitrogen (By similarity).
FT   CONFLICT    139    139       T -> A (in Ref. 1; BAA02467).
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
//