XYLB_KLEPN
ID XYLB_KLEPN Reviewed; 483 AA.
AC P29444;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Xylulose kinase {ECO:0000255|HAMAP-Rule:MF_02220};
DE Short=Xylulokinase {ECO:0000255|HAMAP-Rule:MF_02220};
DE EC=2.7.1.17 {ECO:0000255|HAMAP-Rule:MF_02220};
GN Name=xylB {ECO:0000255|HAMAP-Rule:MF_02220};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=1324398; DOI=10.1007/bf00283840;
RA Feldmann S.D., Sahm H., Sprenger G.A.;
RT "Cloning and expression of the genes for xylose isomerase and xylulokinase
RT from Klebsiella pneumoniae 1033 in Escherichia coli K12.";
RL Mol. Gen. Genet. 234:201-210(1992).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02220};
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_02220, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61059; CAA43390.1; -; Genomic_DNA.
DR PIR; S25070; S25070.
DR AlphaFoldDB; P29444; -.
DR SMR; P29444; -.
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 HAMAP; MF_02220; XylB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01312; XylB; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Transferase; Xylose metabolism.
FT CHAIN 1..483
FT /note="Xylulose kinase"
FT /id="PRO_0000059551"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT BINDING 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT SITE 6
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ SEQUENCE 483 AA; 51907 MW; 835FF494018FE872 CRC64;
MYIGIDLGTS GVKAILLNEQ GEVVASHTEK LTVSRPHPLW SEQDPEQWWL ATDTAMKALG
AHDSLRHVKG LGIAGQMHGA TLLDKSLQVL RPAILWNDGR CAEECQLLED KVSASRQITG
NLMMPGFTAP KLLWVQRHEA AVFSQVDKVL LPKDYLRLRM TGELASDMSD AAGTMWLDVA
RRDWSDEMLA ACDLSRDAMP ALFEGSDVTG QLRPEVAQAW NMPPALVVGG GGDNAAGAVG
IGMADAGQAM LSLGTSGVYF AVSEGFLSKP ESAVHSFCHA CRGRWHLMSV MLSAASCLDW
AAKLTGLASV PALIAAAQTA DESAGPVWFL PYLSGERTPH NNPQAKGVFF GLTHQHGPAE
LARAVLEGVG YALADGMDVV HACAIKPEAI TLIGGGRARY WRQMLADISG LQLDYRTGGD
VGPALGAARL AHVAVHDEAD RPGLLKPLPL EQAHRPDDRR VAHYAPQREI FARIFSKLKP
LMS