ID   FUCK_ECO57              Reviewed;         472 AA.
AC   Q8X6R3;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2024, sequence version 4.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=L-fuculokinase {ECO:0000255|HAMAP-Rule:MF_00986};
DE            EC=2.7.1.51 {ECO:0000255|HAMAP-Rule:MF_00986};
DE   AltName: Full=L-fuculose kinase {ECO:0000255|HAMAP-Rule:MF_00986};
GN   Name=fucK {ECO:0000255|HAMAP-Rule:MF_00986};
GN   OrderedLocusNames=Z4120, ECs3663;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the phosphorylation of L-fuculose.
CC       {ECO:0000255|HAMAP-Rule:MF_00986}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate;
CC         Xref=Rhea:RHEA:12376, ChEBI:CHEBI:15378, ChEBI:CHEBI:17617,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57846, ChEBI:CHEBI:456216;
CC         EC=2.7.1.51; Evidence={ECO:0000255|HAMAP-Rule:MF_00986};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00986};
CC   -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC       and glycerone phosphate from L-fucose: step 2/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00986}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00986}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG57917.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG57917.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB37086.2; -; Genomic_DNA.
DR   PIR; A85932; A85932.
DR   PIR; G91086; G91086.
DR   RefSeq; NP_311690.2; NC_002695.1.
DR   AlphaFoldDB; Q8X6R3; -.
DR   SMR; Q8X6R3; -.
DR   STRING; 155864.Z4120; -.
DR   GeneID; 916532; -.
DR   KEGG; ece:Z4120; -.
DR   KEGG; ecs:ECs_3663; -.
DR   PATRIC; fig|386585.9.peg.3829; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_11_2_6; -.
DR   UniPathway; UPA00563; UER00625.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008737; F:L-fuculokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07773; FGGY_FK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00986; Fuculokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR013450; Fuculokinase.
DR   NCBIfam; TIGR02628; fuculo_kin_coli; 1.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF5; XYLULOSE KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Fucose metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..472
FT                   /note="L-fuculokinase"
FT                   /id="PRO_0000059424"
SQ   SEQUENCE   472 AA;  52257 MW;  4651B640494CACFE CRC64;
     MKQEVILVLD CGATNVRAIA VNRQGKIVAR ASTPNASDIA MENNTWHQWS LDAILQRFAD
     CCRQINSELT ECHIRGIAVT TFGVDGALVD KQGNLLYPII SWKCPRTAAV MDNIERLISA
     QRLQAISGVG AFSFNTLYKL VWLKENHPQL LERAHAWLFI SSLINHRLTG EFTTDITMAG
     TSQMLDIQQR DFSPQILQAT GIPRRLFPRL VEAGEQIGTL QNSAAAMLGL PVGIPVISAG
     HDTQFALFGA GAEQNEPVLS SGTWEILMVR SAQVDTSLLS QYAGSTCELD SQAGLYNPGM
     QWLASGVLEW VRKLFWTAET PWQMLIEEAR LIAPGADGVK MQCDLLSCQN AGWQGVTLNT
     TRGHFYRAAL EGLTAQLQRN LQMLEKIGHF KASELLLVGG GSRNTLWNQI KANMLDIPLK
     VLDDAETTVA GAALFGWYGV GEFNSPEEAR AQIHYQFRYF YPQTEPEFIE EV
//