ID A0A075JGQ6_9MICO Unreviewed; 470 AA.
AC A0A075JGQ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=HX89_08660 {ECO:0000313|EMBL:AIF41000.1};
OS Dermacoccus nishinomiyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF41000.1, ECO:0000313|Proteomes:UP000027986};
RN [1] {ECO:0000313|EMBL:AIF41000.1, ECO:0000313|Proteomes:UP000027986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M25 {ECO:0000313|EMBL:AIF41000.1,
RC ECO:0000313|Proteomes:UP000027986};
RA Hong K.W., Chan K.G.;
RT "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_02220}.
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DR EMBL; CP008889; AIF41000.1; -; Genomic_DNA.
DR RefSeq; WP_038568568.1; NZ_CP008889.1.
DR AlphaFoldDB; A0A075JGQ6; -.
DR GeneID; 41841212; -.
DR KEGG; dni:HX89_08660; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_12_0_11; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000027986; 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; 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:AIF41000.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220};
KW Reference proteome {ECO:0000313|Proteomes:UP000027986};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02220};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 6..225
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 244..426
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 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 10
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 470 AA; 48636 MW; 0C144827078C367C CRC64;
MSPRLVAGVD SSTQSTKIVV CDAETGAVVR TSRAPHPDGT SVDPEVWWRA YEDATADGML
DDVEAIAVGG QQHGMVALDS DGAVIREALL WNDVRSAGAA RDLVDELGGA GAWVDRLDVV
PVAAFTVAKV RWLRDAEPDN AARLDTVVLP HDWLTGRILQ AGGGLRGWTT DRGDASGTGY
WSPVTGEYDA DIQRLALGRE FGVPRVLGPA EPAGVTDAGL VVGAGTGDNM GAALGLGLQP
GDVVVSLGTS GTVFAVQDTP TRDASGQIAG FASADGRHLP LMCTLNAARV LTAGAQLLGV
DLDEFSRLAL AAPIGAQGLT LLPYLDGERT PDLPDATGTL GGLTRANATP ENVARACVEG
MLANLVAGVE GLKQHGLSAR RIVLIGGAAA SAAVREIAPI LFGLPVHIPA PGEYVGIGAA
RQAAWALAGG DEPPAWQVAY DHELEATDDD VTAGRAVYER YLRLQRQLHG
//
