ID A0A1H0TCN9_9MICO Unreviewed; 472 AA.
AC A0A1H0TCN9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN04489867_2738 {ECO:0000313|EMBL:SDP51764.1};
OS Pedococcus dokdonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Pedococcus.
OX NCBI_TaxID=443156 {ECO:0000313|EMBL:SDP51764.1, ECO:0000313|Proteomes:UP000199077};
RN [1] {ECO:0000313|Proteomes:UP000199077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; LT629711; SDP51764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0TCN9; -.
DR STRING; 443156.SAMN04489867_2738; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000199077; 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 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 PRINTS; PR00301; HEATSHOCK70.
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 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 9..222
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 247..428
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 13
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 472 AA; 48543 MW; 68FC7A23BFDFD3AB CRC64;
MPDAPRTLVA GVDSSTQSTK VVVCDATTGE MVRSGRAPHP DGTAVHPDRW WEAFTVATAD
GLLDDVAAIA VGGQQHGMCA LDDQGDVVRD ALLWNDTRSA QAARDLTDEL GGPQEWVRRT
GSALVPSFTV TKVRWLAEHE PDNAARVHDV VLPHDWLTAQ ILKQGNGFER YTTDRGDASG
TGYFSSSTDS YLPDLQELAL GRVFGVPAVL RPSEIAGRTE GGMVVGPGTG DNAGAALGLG
LRHGDVVVSL GTSGAVFADA DQPVADPNGL IASFASASGG HLPLMATLNA ARVLTAAAKL
LGTDLAGLDR LALAAEPGAG GLTLLPYLDG ERSPNLPDAT GTLGGLTRSN ATPENLARAA
VEGMLANLVA GVSDVRRLGL PVERVVLIGG AARSEAVRAV APGLFGVPVA IPEPGEYVGL
GAARQAAWVL GGSAAPPEWE VRYEATLDPP ADDVGASVLD RYAGLLATVH PS
//
