XYLB_LEVBR
ID XYLB_LEVBR Reviewed; 502 AA.
AC P35850;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Xylulose kinase {ECO:0000255|HAMAP-Rule:MF_02220, ECO:0000303|PubMed:1587475};
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, ECO:0000303|PubMed:1587475};
OS Levilactobacillus brevis (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=9835554; DOI=10.1128/aem.64.12.4720-4728.1998;
RA Chaillou S., Bor Y.-C., Batt C.A., Postma P.W., Pouwels P.H.;
RT "Molecular cloning and functional expression in Lactobacillus plantarum 80
RT of xylT, encoding the D-xylose-H+ symporter of Lactobacillus brevis.";
RL Appl. Environ. Microbiol. 64:4720-4728(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX PubMed=1587475; DOI=10.1016/0378-1119(92)90718-5;
RA Bor Y.-C., Moraes C., Lee S.-P., Crosby W.L., Sinskey A.J., Batt C.A.;
RT "Cloning and sequencing the Lactobacillus brevis gene encoding xylose
RT isomerase.";
RL Gene 114:127-131(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 -!- INDUCTION: By D-xylose. {ECO:0000269|PubMed:9835554}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_02220, ECO:0000305}.
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DR EMBL; AF045552; AAC95126.1; -; Genomic_DNA.
DR EMBL; M84564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC1138; JC1138.
DR AlphaFoldDB; P35850; -.
DR SMR; P35850; -.
DR PRIDE; P35850; -.
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 2: Evidence at transcript level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Transferase; Xylose metabolism.
FT CHAIN 1..502
FT /note="Xylulose kinase"
FT /id="PRO_0000059552"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT SITE 9
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ SEQUENCE 502 AA; 55168 MW; 33B6265CE62CC35E CRC64;
MGKYVLGVDL GTSAVKVSAL DHSGQIVAQE SFDYDLIQKQ PGYNEQNPED WVSGTTVAIV
RLILNDHLDA SNIEGLSYSG QMHGLVLLDE NKKVLRPAIL WNDTRSTPQR EEIEAKLGDE
FVHITRNQPL EGFTLTKLLW VKQNEPDIWA KAKYFVLPKD YVRYRMTGNL AMDYSDATGT
VLLDVAKGEW SQKICAALDI PMSMCPPLIK SIDLAGTVTP AYAEFSGLTT DTKVFGGAAD
NAAGAVGAGI LHPNMVLSSI GTSGVVLKYE DNADVNYHGV LQFEDHAIPD KFYSMGVTLA
AGYSFTWFKK TFAPAEDFTD VVASAAKSTV GANGLLYTPY IVGERAPYAD ADIRGSFTGV
DGTHQRYDFV RAVLEGIIFS FRDLFDIYEE NGGDFDTVVS IGGGAKSPLW LQIQADIFNR
KVVSLTNEQG PGMGAAMIAA TGLGWFDSLQ DCAETFVHFG KAYEPNPDNV KKYEKMHAIY
KQVYQQTKTI SEQLLDYRRA EL