ID B1LJE2_ECOSM Unreviewed; 498 AA.
AC B1LJE2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Cryptic L-xylulose kinase {ECO:0000313|EMBL:ACB15798.1};
DE EC=2.7.1.53 {ECO:0000313|EMBL:ACB15798.1};
GN Name=lyx {ECO:0000313|EMBL:ACB15798.1};
GN OrderedLocusNames=EcSMS35_3903 {ECO:0000313|EMBL:ACB15798.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB15798.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB15798.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|RuleBase:RU003733}.
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DR EMBL; CP000970; ACB15798.1; -; Genomic_DNA.
DR RefSeq; WP_000196098.1; NC_010498.1.
DR AlphaFoldDB; B1LJE2; -.
DR KEGG; ecm:EcSMS35_3903; -.
DR HOGENOM; CLU_009281_3_1_6; -.
DR Proteomes; UP000007011; Chromosome.
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 Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:ACB15798.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003733}.
FT DOMAIN 4..250
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 259..440
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 498 AA; 55249 MW; 703618D4FEC8AA79 CRC64;
MTQYWLGLDC GGSWLKAGLY DREGREAGVQ RLPLCALSPQ PGWAERDMAE LWQCCMAVIR
TLLTHSGVSG EQIVGIGISA QGKGLFLLDK NDKPLGNAIL SSDRRAMEIV RRWQEDGIPE
KLYPLTRQTL WTGHPVSLLR WLKEHEPERY AQIGCVMMTH DYLRWCLTGV KGCEESNISE
SNLYNMSLEE YDPCLTDWLG IAEINHALPP VVGSAEICGE ITAQTAALTG LKAGTPVVGG
LFDVVSTALC AGIEDEFTLN AVMGTWAVTS GITRGLRDGE AHPYVYGRYV NDGQFIVHEA
SPTSSGNLEW FTAQWGEISF DEINQAVASL PKAGGDLFFL PFLYGSNAGL EMTSGFYGMQ
AIHTRAHLLQ AIYEGVVFSH MTHLNRMRER FTDVHTLRVT GGPAHSDVWM QMLADVSGLR
IELPQVEETG CFGAALAARV GTGVYRDFSE AQRDLQHPVR TLLPDMTAHQ LYQQKYQRYQ
HLIAALEGFH ARIKEHTL
//
