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Database: UniProt
Entry: U7QZT1_PHOTE
LinkDB: U7QZT1_PHOTE
Original site: U7QZT1_PHOTE 
ID   U7QZT1_PHOTE            Unreviewed;       480 AA.
AC   U7QZT1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=O185_13325 {ECO:0000313|EMBL:ERT12607.1};
OS   Photorhabdus temperata J3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=1389415 {ECO:0000313|EMBL:ERT12607.1, ECO:0000313|Proteomes:UP000017133};
RN   [1] {ECO:0000313|EMBL:ERT12607.1, ECO:0000313|Proteomes:UP000017133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J3 {ECO:0000313|EMBL:ERT12607.1,
RC   ECO:0000313|Proteomes:UP000017133};
RA   Park G.-S., Hong S.-J., Shin J.-H.;
RT   "Whole Genome Shotgun Sequence of Photorhabdus temperata J3.";
RL   Submitted (OCT-2013) 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:ERT12607.1}.
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DR   EMBL; AXDT01000120; ERT12607.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7QZT1; -.
DR   PATRIC; fig|1389415.4.peg.2652; -.
DR   UniPathway; UPA00563; UER00625.
DR   Proteomes; UP000017133; 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..248
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          258..437
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   480 AA;  53269 MW;  BD112A5200F991A9 CRC64;
     MQNVVLVLDC GATNLRAIAV DSQGNVIAKE STPNTSDPDK ANPHWHIWSL DAILERLAGC
     CRGIIPKLSG YKICAITVTT FGVDGTLVDA KGDLLYPIIS WKCSRTIPIV ENIERYFSAE
     KLQTISGVGK FNFNTLYKLI WLKENHPALF DKAHVWLFIS SLINYRLTGV MSTDRTMAGT
     SQLLNIHNEQ FSEAILDAIS ISESLFPELV SAGEQIGILT PEVAKKLNLP SGIPVISSGH
     DTQFALFGSG AGLNQPVLSS GTWEILMVRT PHVNTHILPH YAGSTCELDA RKGIFNPGLQ
     WLASGVLEWI RRLFWRDIPP SEAYIQMIHE ALSVPPGANN LRMNCRLLTS EAGWCGITLN
     TERRHFYRAA LEALGYQLKQ NLSLLGKISG FHAKELVLVG GGSRNYLWNQ IKADILNLPI
     KVLNEAETTV LGASFFAWFG VGCYESSEKA REQFSYHYEL YTPGEHQEAY NSLAQDFIQE
//
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