XYLB_LACLA
ID XYLB_LACLA Reviewed; 501 AA.
AC Q9CFG8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
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}; OrderedLocusNames=LL1508;
GN ORFNames=L0231;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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}.
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DR EMBL; AE005176; AAK05606.1; -; Genomic_DNA.
DR PIR; D86813; D86813.
DR RefSeq; NP_267664.1; NC_002662.1.
DR RefSeq; WP_010906011.1; NC_002662.1.
DR AlphaFoldDB; Q9CFG8; -.
DR SMR; Q9CFG8; -.
DR STRING; 272623.L0231; -.
DR PaxDb; Q9CFG8; -.
DR EnsemblBacteria; AAK05606; AAK05606; L0231.
DR KEGG; lla:L0231; -.
DR PATRIC; fig|272623.7.peg.1618; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_0_9; -.
DR OMA; WHVMGVT; -.
DR Proteomes; UP000002196; 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 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 Reference proteome; Transferase; Xylose metabolism.
FT CHAIN 1..501
FT /note="Xylulose kinase"
FT /id="PRO_0000059553"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
FT SITE 8
FT /note="Important for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02220"
SQ SEQUENCE 501 AA; 55814 MW; 0FBAB1370D3F64D8 CRC64;
MTYVLGIDLG TSSLKGILMD EVGNLITTKS AEYQIDTPKQ GYSEQRPEYW IVALESVLTG
LSVEISDFGQ QLAGISFSGQ MHSLVVLDDN NKPVYPAILW NDVRTSKQCQ EITDRLGQRL
LEITKNIALE GFTLPKILWL QENEPEVWSR VKKIMLPKDY LSLWLTGNIY TEFSDAAGTL
LLDIEKKQWS EEITDAFNID RRILPELIES TDRTGFVKAE IAERYKLTNE VKVFAGGADN
AAAALGVGLI NEEVGLISMG TSGVVSAYEP KIADYKGKLH FFNHTVPGAC YSMGVTLAAG
NSLNWYKETF GKGLSFNELL SEVYTVSPGS EGLLFTPYIV GERTPHFDSK IRGSFIGISA
HHEQKHFSRA VLEGITFSLR DSKDIMEKTK NKKFKRLISV GGGAQNPDIM QMQADIFNSE
MIRLTVEQGP GLGACMIAAF GCGLFDSLEA VTKAFVHYKE ASFIPNPKNV ARYEQIYQIW
KQVYKNTSEI SHQLVEFNDE G