ID F4V5E3_ECOLX Unreviewed; 482 AA.
AC F4V5E3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=L-fuculokinase {ECO:0000256|HAMAP-Rule:MF_00986};
DE EC=2.7.1.51 {ECO:0000256|HAMAP-Rule:MF_00986};
DE AltName: Full=L-fuculose kinase {ECO:0000256|HAMAP-Rule:MF_00986};
GN Name=fucK {ECO:0000256|HAMAP-Rule:MF_00986};
GN ORFNames=ECNG_00825 {ECO:0000313|EMBL:EGI39784.1};
OS Escherichia coli TA280.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI39784.1, ECO:0000313|Proteomes:UP000004877};
RN [1] {ECO:0000313|EMBL:EGI39784.1, ECO:0000313|Proteomes:UP000004877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA280 {ECO:0000313|EMBL:EGI39784.1,
RC ECO:0000313|Proteomes:UP000004877};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli TA280.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of L-fuculose.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00986};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00986};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC and glycerone phosphate from L-fucose: step 2/3. {ECO:0000256|HAMAP-
CC Rule:MF_00986}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00986, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; GL884370; EGI39784.1; -; Genomic_DNA.
DR AlphaFoldDB; F4V5E3; -.
DR HOGENOM; CLU_009281_11_2_6; -.
DR UniPathway; UPA00563; UER00625.
DR Proteomes; UP000004877; Unassembled WGS sequence.
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 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 {ECO:0000256|HAMAP-Rule:MF_00986};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00986};
KW Fucose metabolism {ECO:0000256|ARBA:ARBA00023253, ECO:0000256|HAMAP-
KW Rule:MF_00986};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00986, ECO:0000256|RuleBase:RU003733};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00986};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00986}.
FT DOMAIN 15..259
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 269..448
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 482 AA; 53216 MW; E3AD593BF6D50E17 CRC64;
MLSGYIAGAI MKQEVILVLD CGATNVRAIA VNRQGKIVAR ASTPNASDIA MENNTWHQWS
LDAILQRFAD CCRQINSKLT ECHIRGIAVT TFGVDGALVD KQGNLLYPII SWKCPRTAAV
MDNIERLISA QQLQAISGVG AFSFNTLYKL VWLKENHPQL LERAHAWLFI SSLINHRLTG
EFTTDITMAG TSQMLDIQQR DFSPQILHAT GIPRRLFPRL VEAGEQIGTL QNSAAAMLGL
PVGIPVISAG HDTQFALFGA GAEQNEPVLS SGTWEILMVR SAQVDTSLLS QYAGSTCELD
SQAGLYNPGM QWLASGVLEW VRKLFWTAET PWQMLIEEAR LIAPGADGVK MQCDLLSCQN
AGWQGVTLNT TRGHFYRAAL EGLTAQLQRN LQMLEKIGHF KASELLLVGG GSRNTLWNQI
KANMLDIPVK VLDDAETTVA GAALFGWYGV GEFNSPEEAR AQIHYQYRYF YPQTEPEFIE
EV
//
