ID D4BGV9_9ENTR Unreviewed; 472 AA.
AC D4BGV9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 ECO:0000313|EMBL:EFE06710.1};
GN ORFNames=CIT292_09766 {ECO:0000313|EMBL:EFE06710.1};
OS Citrobacter youngae ATCC 29220.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE06710.1, ECO:0000313|Proteomes:UP000003880};
RN [1] {ECO:0000313|EMBL:EFE06710.1, ECO:0000313|Proteomes:UP000003880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE06710.1,
RC ECO:0000313|Proteomes:UP000003880};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE06710.1}.
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DR EMBL; ABWL02000021; EFE06710.1; -; Genomic_DNA.
DR RefSeq; WP_006686990.1; NZ_GG730301.1.
DR AlphaFoldDB; D4BGV9; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_11_2_6; -.
DR UniPathway; UPA00563; UER00625.
DR Proteomes; UP000003880; 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 5..249
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 259..436
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 472 AA; 51864 MW; A77009059A0E1922 CRC64;
MKQDVILVLD CGATNVRAIA VDRQGKIIAR ASTPNASDIA AENSAWHQWS LEAILQRFAD
CCQRLSPQLA NCHVRGIAVT TFGVDGALVD KNGKQLYPVI SWKCPRTAAV MENIHRYMTP
QQLQEISGVG AFSFNTLYKL VWLKENHPQL LEQAHAWLFI SSLINHRLTG EFTTDITMAG
TSQMLDIQQR DFSHDILQAT GIPRRLFPRL VEAGEQIGTL QPEAASQLGL TAGIPVISAG
HDTQFALFGA GAQQDEPVLS SGTWEILMVR SAQVNTSLLS HYAGSTCELD SQAGLYNPGM
QWLASGVLEW VRKLLWTAET PWQTLIDEAQ AIPAGAEGVK MQCDLLACQN AGWQGVTLNT
TRGHFYRAAL EGLTEQLQRN LQTLEKIGHF QASELLLVGG GSRNALWNQI KANVLGIPVK
VLDDAETTVA GAAMFAWSGI GEFTSAEQAR VQVRYQYRYF YPQTEPELTG VE
//
