ID   LYXK_HAEIN              Reviewed;         485 AA.
AC   P44991;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Probable L-xylulose kinase;
DE            Short=L-xylulokinase;
DE            EC=2.7.1.53;
GN   Name=lyx; Synonyms=lyxK, sgbK; OrderedLocusNames=HI_1027;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-xylulose = ADP + H(+) + L-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:18869, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57829, ChEBI:CHEBI:456216;
CC         EC=2.7.1.53;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22687.1; -; Genomic_DNA.
DR   PIR; H64164; H64164.
DR   RefSeq; NP_439187.1; NC_000907.1.
DR   AlphaFoldDB; P44991; -.
DR   SMR; P44991; -.
DR   STRING; 71421.HI_1027; -.
DR   EnsemblBacteria; AAC22687; AAC22687; HI_1027.
DR   KEGG; hin:HI_1027; -.
DR   PATRIC; fig|71421.8.peg.1071; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_1_6; -.
DR   OrthoDB; 9805576at2; -.
DR   PhylomeDB; P44991; -.
DR   BioCyc; HINF71421:G1GJ1-1067-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008744; F:L-xylulokinase activity; IEA:UniProtKB-EC.
DR   CDD; cd07802; FGGY_L-XK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   PANTHER; PTHR43095:SF3; L-XYLULOSE_3-KETO-L-GULONATE KINASE; 1.
DR   PANTHER; PTHR43095; SUGAR 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; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..485
FT                   /note="Probable L-xylulose kinase"
FT                   /id="PRO_0000059561"
SQ   SEQUENCE   485 AA;  54965 MW;  8E63C56CB775A66D CRC64;
     MHYYLGIDCG GTFIKAAIFD QNGTLQSIAR RNIPIISEKP GYAERDMDEL WNLCAQVIQK
     TIRQSSILPQ QIKAIGISAQ GKGAFFLDKD NKPLGRAILS SDQRAYEIVQ CWQKENILQK
     FYPITLQTLW MGHPVSILRW IKENEPSRYE QIHTILMSHD YLRFCLTEKL YCEETNISES
     NFYNMREGKY DIQLAKLFGI TECIDKLPPI IKSNKIAGYV TSRAAEQSGL VEGIPVVGGL
     FDVVSTALCA DLKDDQHLNV VLGTWSVVSG VTHYIDDNQT IPFVYGKYPE KNKFIIHEAS
     PTSAGNLEWF VNQFNLPNYD DINHEIAKLK PASSSVLFAP FLYGSNAKLG MQAGFYGIQS
     HHTQIHLLQA IYEGVIFSLM SHLERMQVRF PNASTVRVTG GPAKSEVWMQ MLADISGMRL
     EIPNIEETGC LGAALMAMQA ESAVEISQIL NIDRKIFLPD KNQYSKYQHK YHRYLKFIEA
     LKNLD
//