FUCK_ECO57
ID FUCK_ECO57 Reviewed; 482 AA.
AC Q8X6R3;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 3.
DT 03-AUG-2022, entry version 107.
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; Proteobacteria; 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}.
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DR EMBL; AE005174; AAG57917.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37086.1; -; 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.EDL933_3984; -.
DR EnsemblBacteria; AAG57917; AAG57917; Z4120.
DR EnsemblBacteria; BAB37086; BAB37086; ECs_3663.
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 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; Reference proteome; Transferase.
FT CHAIN 1..482
FT /note="L-fuculokinase"
FT /id="PRO_0000059424"
SQ SEQUENCE 482 AA; 53234 MW; 42C7D3BC97D7D4C9 CRC64;
MLSGYIAGAI 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
