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Database: UniProt
Entry: Q7MJI3_VIBVY
LinkDB: Q7MJI3_VIBVY
Original site: Q7MJI3_VIBVY 
ID   Q7MJI3_VIBVY            Unreviewed;       488 AA.
AC   Q7MJI3;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
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   OrderedLocusNames=VV2178 {ECO:0000313|EMBL:BAC94942.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC94942.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC94942.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC94942.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA   Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA   Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94942.1; -; Genomic_DNA.
DR   RefSeq; WP_011150691.1; NC_005139.1.
DR   AlphaFoldDB; Q7MJI3; -.
DR   STRING; 672.VV93_v1c19190; -.
DR   KEGG; vvy:VV2178; -.
DR   PATRIC; fig|196600.6.peg.2195; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_11_2_6; -.
DR   UniPathway; UPA00563; UER00625.
DR   Proteomes; UP000002675; Chromosome I.
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 {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|HAMAP-Rule:MF_00986,
KW   ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          4..247
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          256..443
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   488 AA;  53537 MW;  FAAAEF6AB05319D6 CRC64;
     MSVVIVLDCG ATNLRAIAID SQGKIVASYF VKNETKQDIN NPDYHIWDFE QIWTKLVECG
     QKVIAEVGAK NVLALTVTTF GVDGAPFDNQ GNQLYPIISW KCPRTVPVMK QVEQELDRLQ
     LYRDNGIGDY SFNTLYKLRW FQQHQPQLFE QMDKFVFISS MITHQLTGVW STDYTMAGTS
     MMTDLTLCNW NPAVLEYLGL SEEQFPPLVM AGDVIGSVTS DIAKLLGLGA DVPVISAGHD
     TQFALVGSGA AENQAFLSSG TWEILMARSQ RPQLDVHALQ HGVTVELDSV KGFYNPAIQW
     LSSAVVEWVA NQFFTAEQAS GELYKVMIEE AREVGNGASG VVFKPNFTTN ADGIGQGAIE
     GLGLHTNRGQ IARAVFEGLS KQLKQRFDYL SQLCQLSDGP VVVVGGGTKN DLWNQLRADA
     LQRSLHIVEQ AEATVIGAAM FAFTGSGFYP DIDSAQAQMK PSLRVVNPSL LNTPPLESKT
     VQQESTHA
//
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