ID A0A1R4INR1_9MICO Unreviewed; 465 AA.
AC A0A1R4INR1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220};
DE Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220};
DE EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220};
GN Name=xylB {ECO:0000256|HAMAP-Rule:MF_02220};
GN ORFNames=FM119_02825 {ECO:0000313|EMBL:SJN21511.1};
OS Mycetocola reblochoni REB411.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=1255698 {ECO:0000313|EMBL:SJN21511.1, ECO:0000313|Proteomes:UP000196778};
RN [1] {ECO:0000313|Proteomes:UP000196778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB411 {ECO:0000313|Proteomes:UP000196778};
RA Dridi B.;
RL Submitted (FEB-2017) 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 -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_02220}.
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DR EMBL; FUKR01000017; SJN21511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4INR1; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000196778; Unassembled WGS sequence.
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 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; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02220};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02220};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000313|EMBL:SJN21511.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220};
KW Reference proteome {ECO:0000313|Proteomes:UP000196778};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000313|EMBL:SJN21511.1};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 3..231
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 249..431
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 7
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 465 AA; 48194 MW; F6844A554829B873 CRC64;
MLVAGIDSST QSCKVVVRDA ATGRLLREGR APHPDGTEVD PARWWDALQH AVRAAGGLDD
VAAVSVAAQQ HGMVVLDEGG RVIRDALLWN DTRSADAARD LVREFGAEVL AERTGLVPVA
SFTITKLRWL RDAEPDNAAR VAAVALPHDW LSWRLRGYGP EGESARGPVL EELTTDRSDA
SGTGYWSPRT GRYDHELLIA ALGHDAVLPT VLGPDETAGR TPSGARVGAG AGDNAGAALG
LDADTGDVVV SIGTSGTVFS VADAPVIDPS GIAAGLADAA GGFLPLSATL NAARVLDQTA
LVLGVDVADL GDLALEAEPG ASGLVLQPYF DGERTPNLPE ATATLFGMTR ASFTRPGLAR
AAIEGMLCGL ADALDAHRAL GVDARRLLLI GGAALNPAVR EIASRVFDIP VVVPAPGEYV
ADGAARQAAW ALTGSRPGWP IDTVATIEPR PFPVIREQYA ARAPS
//
