ID   LYXK_ECOLI              Reviewed;         498 AA.
AC   P37677; Q2M7P3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=L-xylulose/3-keto-L-gulonate kinase;
DE            Short=L-xylulokinase;
DE            EC=2.7.1.- {ECO:0000269|PubMed:11741871, ECO:0000269|PubMed:7961955};
DE            EC=2.7.1.53 {ECO:0000269|PubMed:11741871, ECO:0000269|PubMed:7961955};
DE   AltName: Full=3-dehydro-L-gulonate kinase;
GN   Name=lyx; Synonyms=lyxK, sgbK, xylK, yiaP; OrderedLocusNames=b3580, JW3552;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12;
RX   PubMed=7961955; DOI=10.1016/s0021-9258(18)43932-4;
RA   Sanchez J.C., Gimenez R., Schneider A., Fessner W.-D., Baldoma L.,
RA   Aquilar J., Badia J.;
RT   "Activation of a cryptic gene encoding a kinase for L-xylulose opens a new
RT   pathway for the utilization of L-lyxose by Escherichia coli.";
RL   J. Biol. Chem. 269:29665-29669(1994).
RN   [5]
RP   DISCUSSION OF SEQUENCE.
RA   Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT   "Novel phosphotransferases system genes revealed by bacterial genome
RT   analysis: operons encoding homologues of sugar-specific permease domains of
RT   the phosphotransferase system and pentose catabolic enzymes.";
RL   Genome Sci. Technol. 1:53-75(1996).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA   Yew W.S., Gerlt J.A.;
RT   "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT   functions to products of the yjf-sga and yia-sgb operons.";
RL   J. Bacteriol. 184:302-306(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of L-xylulose and 3-keto-L-
CC       gulonate. Is involved in L-lyxose utilization via xylulose, and may
CC       also be involved in the utilization of 2,3-diketo-L-gulonate.
CC       {ECO:0000269|PubMed:11741871, ECO:0000269|PubMed:7961955}.
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; Evidence={ECO:0000269|PubMed:11741871,
CC         ECO:0000269|PubMed:7961955};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18870;
CC         Evidence={ECO:0000269|PubMed:7961955};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate + ATP = 3-dehydro-L-gulonate 6-phosphate
CC         + ADP + H(+); Xref=Rhea:RHEA:28222, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57655, ChEBI:CHEBI:58774,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11741871};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28223;
CC         Evidence={ECO:0000269|PubMed:11741871};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 mM for L-xylulose {ECO:0000269|PubMed:7961955};
CC         KM=0.4 mM for ATP {ECO:0000269|PubMed:7961955};
CC         Vmax=33 umol/min/mg enzyme with L-xylulose as substrate
CC         {ECO:0000269|PubMed:7961955};
CC       pH dependence:
CC         Optimum pH is 8.4 with L-xylulose as substrate.
CC         {ECO:0000269|PubMed:7961955};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7961955}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; U00039; AAB18557.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76604.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77713.1; -; Genomic_DNA.
DR   PIR; S47801; S47801.
DR   RefSeq; NP_418037.1; NC_000913.3.
DR   RefSeq; WP_000196054.1; NZ_SSZK01000041.1.
DR   AlphaFoldDB; P37677; -.
DR   SMR; P37677; -.
DR   BioGRID; 4262550; 7.
DR   IntAct; P37677; 2.
DR   STRING; 511145.b3580; -.
DR   PaxDb; P37677; -.
DR   PRIDE; P37677; -.
DR   DNASU; 948101; -.
DR   EnsemblBacteria; AAC76604; AAC76604; b3580.
DR   EnsemblBacteria; BAE77713; BAE77713; BAE77713.
DR   GeneID; 948101; -.
DR   KEGG; ecj:JW3552; -.
DR   KEGG; eco:b3580; -.
DR   PATRIC; fig|1411691.4.peg.3132; -.
DR   EchoBASE; EB2192; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_1_6; -.
DR   InParanoid; P37677; -.
DR   OMA; AAYQKKW; -.
DR   PhylomeDB; P37677; -.
DR   BioCyc; EcoCyc:LYXK-MON; -.
DR   BioCyc; MetaCyc:LYXK-MON; -.
DR   BRENDA; 2.7.1.53; 2026.
DR   PRO; PR:P37677; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008744; F:L-xylulokinase activity; IDA:EcoCyc.
DR   GO; GO:0019324; P:L-lyxose metabolic process; IMP:EcoCyc.
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   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..498
FT                   /note="L-xylulose/3-keto-L-gulonate kinase"
FT                   /id="PRO_0000059560"
SQ   SEQUENCE   498 AA;  55155 MW;  207EC94507141E34 CRC64;
     MTQYWLGLDC GGSWLKAGLY DREGREAGVQ RLPLCALSPQ PGWAERDMAE LWQCCMAVIR
     ALLTHSGVSG EQIVGIGISA QGKGLFLLDK NDKPLGNAIL SSDRRAMEIV RRWQEDGIPE
     KLYPLTRQTL WTGHPVSLLR WLKEHEPERY AQIGCVMMTH DYLRWCLTGV KGCEESNISE
     SNLYNMSLGE YDPCLTDWLG IAEINHALPP VVGSAEICGE ITAQTAALTG LKAGTPVVGG
     LFDVVSTALC AGIEDEFTLN AVMGTWAVTS GITRGLRDGE AHPYVYGRYV NDGEFIVHEA
     SPTSSGNLEW FTAQWGEISF DEINQAVASL PKAGGDLFFL PFLYGSNAGL EMTSGFYGMQ
     AIHTRAHLLQ AIYEGVVFSH MTHLNRMRER FTDVHTLRVT GGPAHSDVWM QMLADVSGLR
     IELPQVEETG CFGAALAARV GTGVYHNFSE AQRDLRHPVR TLLPDMTAHQ LYQKKYQRYQ
     HLIAALQGFH ARIKEHTL