ID K0JVA2_SACES Unreviewed; 458 AA.
AC K0JVA2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ECO:0000313|EMBL:CCH29916.1};
GN OrderedLocusNames=BN6_26030 {ECO:0000313|EMBL:CCH29916.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH29916.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH29916.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; HE804045; CCH29916.1; -; Genomic_DNA.
DR RefSeq; WP_015100028.1; NC_019673.1.
DR AlphaFoldDB; K0JVA2; -.
DR STRING; 1179773.BN6_26030; -.
DR KEGG; sesp:BN6_26030; -.
DR PATRIC; fig|1179773.3.peg.2602; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_12_0_11; -.
DR OrthoDB; 9805576at2; -.
DR BioCyc; SESP1179773:BN6_RS12630-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
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; IPR018483; Carb_kinase_FGGY_CS.
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.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000006281};
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..229
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 236..418
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 71..72
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 458 AA; 46474 MW; D7A66F79D5DFA52F CRC64;
MTLVAGIDSS TQSCKVVVRD AESGVLVREG RAPHPPGTEV DPGAWWDALG VASRAAGGLD
DVAAVSVAAQ QHGLVCLDGS GVVVRPALLW NDTRSAGAAR DLVAELGAAA WVAAVGNVPV
ASLTVAKLRW LAEHEPGNAD RTAAVCLPHD WLTWRLSGGR GVESLTTDRS DASGTGYWSA
AGGEYRLELL ERAFGRVPTV VPSVLGPGAL SGRFGAGCGD NAAAALGVQA RPGDVVVSVG
TSGTAFARAS RPVADPTGTV NGFADAEGGH LPLVCTLNAS RVLDAAAALL GVDLAELSRL
ASSAPAGADG LVLVPYLEGE RTPDKPDSTG AVHGLRLDNA TPGNFARAAV EGLLCGLADA
IDALAAVGTP VERVLLIGGG ARSAAVREIA PAVFGRPVVL PATGEYVADG AARQAAWALA
GADAPPHWAE LRSTVVEADP TPWVRERYAT ARDLTVNR
//
