MAK_ECOLI
ID MAK_ECOLI Reviewed; 302 AA.
AC P23917; P71316; P75705; Q2MC31;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Fructokinase;
DE EC=2.7.1.4;
DE AltName: Full=D-fructose kinase;
DE AltName: Full=Manno(fructo)kinase;
GN Name=mak; Synonyms=yajF; OrderedLocusNames=b0394, JW0385;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8807285; DOI=10.1093/genetics/143.3.1101;
RA Ryder L., Sharples G.J., Lloyd R.G.;
RT "Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains
RT of Escherichia coli K-12.";
RL Genetics 143:1101-1114(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-302.
RX PubMed=1744033; DOI=10.1128/jb.173.24.7765-7771.1991;
RA Reeder T.C., Schleif R.F.;
RT "Mapping, sequence, and apparent lack of function of araJ, a gene of the
RT Escherichia coli arabinose regulon.";
RL J. Bacteriol. 173:7765-7771(1991).
RN [6]
RP ROLE IN FRUCTOSE METABOLISM.
RX PubMed=11742072; DOI=10.1073/pnas.211569798;
RA Sproul A.A., Lambourne L.T., Jims J.-J.D., Kornberg H.L.;
RT "Genetic control of manno(fructo)kinase activity in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15257-15259(2001).
RN [7]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND KINETIC PARAMETERS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15157072; DOI=10.1021/bi049424m;
RA Miller B.G., Raines R.T.;
RT "Identifying latent enzyme activities: substrate ambiguity within modern
RT bacterial sugar kinases.";
RL Biochemistry 43:6387-6392(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose to fructose-6-P.
CC Has also low level glucokinase activity in vitro. Is not able to
CC phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-
CC threonine. {ECO:0000269|PubMed:11742072, ECO:0000269|PubMed:15157072}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for D-fructose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072};
CC KM=1.8 mM for ATP (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072};
CC KM=59 mM for glucose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072};
CC Note=Catalytic efficiency with D-fructose as substrate is 55-fold
CC higher than that with D-glucose.;
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18118.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X76979; CAA54284.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18118.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73497.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76175.1; -; Genomic_DNA.
DR EMBL; M64787; AAA23475.1; -; Genomic_DNA.
DR PIR; B64768; B64768.
DR RefSeq; NP_414928.2; NC_000913.3.
DR RefSeq; WP_001219309.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P23917; -.
DR SMR; P23917; -.
DR BioGRID; 4259818; 15.
DR DIP; DIP-11288N; -.
DR IntAct; P23917; 30.
DR STRING; 511145.b0394; -.
DR jPOST; P23917; -.
DR PaxDb; P23917; -.
DR PRIDE; P23917; -.
DR EnsemblBacteria; AAC73497; AAC73497; b0394.
DR EnsemblBacteria; BAE76175; BAE76175; BAE76175.
DR GeneID; 949086; -.
DR KEGG; ecj:JW0385; -.
DR KEGG; eco:b0394; -.
DR PATRIC; fig|1411691.4.peg.1884; -.
DR EchoBASE; EB1265; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_3_6; -.
DR InParanoid; P23917; -.
DR OMA; DHLVMIT; -.
DR PhylomeDB; P23917; -.
DR BioCyc; EcoCyc:EG11288-MON; -.
DR BioCyc; MetaCyc:EG11288-MON; -.
DR SABIO-RK; P23917; -.
DR PRO; PR:P23917; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IDA:EcoCyc.
DR GO; GO:0004396; F:hexokinase activity; IBA:GO_Central.
DR GO; GO:0019158; F:mannokinase activity; IDA:EcoCyc.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="Fructokinase"
FT /id="PRO_0000095689"
FT BINDING 4..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 302 AA; 32500 MW; 9791F9C29C91049C CRC64;
MRIGIDLGGT KTEVIALGDA GEQLYRHRLP TPRDDYRQTI ETIATLVDMA EQATGQRGTV
GMGIPGSISP YTGVVKNANS TWLNGQPFDK DLSARLQREV RLANDANCLA VSEAVDGAAA
GAQTVFAVII GTGCGAGVAF NGRAHIGGNG TAGEWGHNPL PWMDEDELRY REEVPCYCGK
QGCIETFISG TGFAMDYRRL SGHALKGSEI IRLVEESDPV AELALRRYEL RLAKSLAHVV
NILDPDVIVL GGGMSNVDRL YQTVGQLIKQ FVFGGECETP VRKAKHGDSS GVRGAAWLWP
QE
