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Database: UniProt
Entry: A0A0D0KDN4_9MICO
LinkDB: A0A0D0KDN4_9MICO
Original site: A0A0D0KDN4_9MICO 
ID   A0A0D0KDN4_9MICO        Unreviewed;       428 AA.
AC   A0A0D0KDN4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=xylB {ECO:0000256|HAMAP-Rule:MF_02220,
GN   ECO:0000256|RuleBase:RU364073};
GN   ORFNames=RU09_02415 {ECO:0000313|EMBL:KIP94990.1};
OS   Microbacterium sp. MEJ108Y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1587523 {ECO:0000313|EMBL:KIP94990.1, ECO:0000313|Proteomes:UP000032119};
RN   [1] {ECO:0000313|EMBL:KIP94990.1, ECO:0000313|Proteomes:UP000032119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEJ108Y {ECO:0000313|EMBL:KIP94990.1,
RC   ECO:0000313|Proteomes:UP000032119};
RA   Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT   "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT   draft genome assemblies.";
RL   Submitted (DEC-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   -!- 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:KIP94990.1}.
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DR   EMBL; JXQX01000004; KIP94990.1; -; Genomic_DNA.
DR   RefSeq; WP_042537078.1; NZ_JXQX01000004.1.
DR   AlphaFoldDB; A0A0D0KDN4; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000032119; 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; 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   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..212
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          243..424
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        228
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   428 AA;  44160 MW;  BEB0F9A87DC2FF29 CRC64;
     MPLVLGVDSS TQSCKAVVVD TATGAVVRAG RATHPDGTSV DPEAWWRALN AAITEAGSLD
     EIEAWSIGGQ QHGLVALDES GRVIRDALLW NDTRSAGAAT ELIAEYGATE LAARTGLVPV
     ASFTITKLRW LRDHEPENAA RVAAVALPHD WLTWRLRGFG PENPVLDELV TDRSDASGTG
     YWNPSTGEYD RELLVAALGH DAILPRVLAH DEWTTDADGR RVGAGAGDNA AAALGLGAVP
     GDAVVSIGTS GTVCAISTTP LSDATGTVAG FADASGNFLP LVATLNAARV VDVTAALLGV
     THDEFSDLAL QATPGADGLT LLPYFEGERT PNLPDATASL SGMTLASTTR ENLARAAVEG
     MLRGLGAGLD ALRDLGIPLE RALLIGGGAQ SEAVRRVAPE ILGLPVEVPE PGEYVALGAA
     RQAALIVD
//
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