ID   A0A0C7P408_DEFTU        Unreviewed;       491 AA.
AC   A0A0C7P408;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
GN   Name=xylB3 {ECO:0000313|EMBL:CEP78609.1};
GN   Synonyms=xylB {ECO:0000256|HAMAP-Rule:MF_02220,
GN   ECO:0000256|RuleBase:RU364073};
GN   ORFNames=DTL3_1315 {ECO:0000313|EMBL:CEP78609.1};
OS   Defluviitoga tunisiensis.
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Defluviitoga.
OX   NCBI_TaxID=1006576 {ECO:0000313|EMBL:CEP78609.1, ECO:0000313|Proteomes:UP000032809};
RN   [1] {ECO:0000313|Proteomes:UP000032809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L3 {ECO:0000313|Proteomes:UP000032809};
RA   Wibberg D.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_02220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216;
CC         EC=2.7.1.17; Evidence={ECO:0000256|HAMAP-Rule:MF_02220,
CC         ECO:0000256|RuleBase:RU364073};
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_02220, ECO:0000256|RuleBase:RU003733}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN824141; CEP78609.1; -; Genomic_DNA.
DR   RefSeq; WP_045088022.1; NZ_LN824141.1.
DR   AlphaFoldDB; A0A0C7P408; -.
DR   STRING; 1006576.DTL3_1315; -.
DR   KEGG; dtn:DTL3_1315; -.
DR   PATRIC; fig|1006576.9.peg.1312; -.
DR   HOGENOM; CLU_009281_3_0_0; -.
DR   OrthoDB; 39631at2; -.
DR   Proteomes; UP000032809; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07808; FGGY_D-XK_EcXK-like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02220; XylB; 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; IPR006000; Xylulokinase.
DR   NCBIfam; TIGR01312; XylB; 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_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02220};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU003733};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032809};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU003733};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_02220}.
FT   DOMAIN          4..242
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          252..435
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            8
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   491 AA;  55704 MW;  80CF9F0144519E5F CRC64;
     MEKYLGIDVG TTSIKGLVVD ENGRLLDTYS WPLKMDIPKP GWAEQDPNLW WEGVLEILRN
     VSLKHTISAI GFSGQMHSLV CLDKNFQVIR PAILWCDQRT TQQCKKATEI MGGETKVIEK
     MGNPFLEGFT FPKILWIKEN ERANFNKIKK ILLPKDYIIY KLTGNLGIDY SDASGTACFN
     VNKNTWDSEV FEKFEIDISI MPDIYLSYDD RGELRNELKS QLGWNNCKIV SGGADNAAAA
     FGIGISKKGE SMVSIGTSGT VLTITENKKP DLEGKIHYFN HVLENKYYYM GVMLSAANTL
     NWVRDHFFPH SSWDEIEERI NNSKPGSNGI IFLPYLNGER TPHRDPNARG VIFGISSINN
     ENDILRATME GITFGLRDSF ELIKEKTEIK DMRIVGGGAK NKTWIKLVAA NFKMPIKIPQ
     IDEGGAYGAS MLAALGNGQN LEHVLNWVKI KEIIEPDDNL FEIYDELYEI YKKLYFSLKQ
     NYIQMAKFLN L
//