ID   FUCK_SALTI              Reviewed;         472 AA.
AC   Q8Z428;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=STY3117, t2885;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
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DR   EMBL; AL513382; CAD02803.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70441.1; -; Genomic_DNA.
DR   RefSeq; NP_457372.1; NC_003198.1.
DR   RefSeq; WP_001763972.1; NZ_WSUR01000005.1.
DR   AlphaFoldDB; Q8Z428; -.
DR   SMR; Q8Z428; -.
DR   STRING; 220341.16504057; -.
DR   EnsemblBacteria; AAO70441; AAO70441; t2885.
DR   KEGG; stt:t2885; -.
DR   KEGG; sty:STY3117; -.
DR   PATRIC; fig|220341.7.peg.3172; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_11_2_6; -.
DR   OMA; SDLWMQI; -.
DR   UniPathway; UPA00563; UER00625.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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   HAMAP; MF_00986; Fuculokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR013450; Fuculokinase.
DR   PANTHER; PTHR10196:SF60; PTHR10196:SF60; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR02628; fuculo_kin_coli; 1.
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; Transferase.
FT   CHAIN           1..472
FT                   /note="L-fuculokinase"
FT                   /id="PRO_0000059426"
SQ   SEQUENCE   472 AA;  51746 MW;  5CD73548EED519E8 CRC64;
     MKQDVILVLD CGATNVRAIA VDRQGKIVAR ASTANASDIA AENSAWHQWS LDAILQRFAD
     CCRSLSSALS ECVVRGITVT TFGVDGALVD AQGKLLYPVI SWKCPRTAAV METIERFISP
     RQLQTLSGVG AFSFNTLYKL VWLKENHPRL LEQAHCWLFI SSLINHRLTG EFTTDITMAG
     TSQLLDIHQR DFSPEILQAT GLARRLFPRI VEAGAPIGTL QTDAARLLGL PAGVPVISAE
     HDTQFALFGA GAQQGEPVLS SGTWEILMVR SGQVDTSLLS QYPGSTCELD SQSGLYNPGM
     QWLASGVLEW VRKLLWTPET PWQTLIDEAR AIPAGAEGVR MQCDLLACQN AGWQGVTLNT
     TRGHFYRAAL EGLTAQLQRN LRTLEKIGHF NATELLLVGG GSRNALWNQI KANQLDIPIK
     VLDDAETTVA GAAMFGWYGV GEFSSPEQAR AQVNYQYRYF WPQTEPEIIE GV