ID Q8ZL91_SALTY Unreviewed; 484 AA.
AC Q8ZL91;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
GN Name=xylB {ECO:0000256|HAMAP-Rule:MF_02220,
GN ECO:0000256|RuleBase:RU364073, ECO:0000313|EMBL:AAL22519.1};
GN OrderedLocusNames=STM3660 {ECO:0000313|EMBL:AAL22519.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL22519.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL22519.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC phosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02220,
CC ECO:0000256|RuleBase:RU364073};
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_02220, ECO:0000256|RuleBase:RU003733}.
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DR EMBL; AE006468; AAL22519.1; -; Genomic_DNA.
DR RefSeq; NP_462560.1; NC_003197.2.
DR RefSeq; WP_000275326.1; NC_003197.2.
DR AlphaFoldDB; Q8ZL91; -.
DR STRING; 99287.STM3660; -.
DR PaxDb; 99287-STM3660; -.
DR GeneID; 1255184; -.
DR KEGG; stm:STM3660; -.
DR PATRIC; fig|99287.12.peg.3871; -.
DR HOGENOM; CLU_009281_3_0_6; -.
DR OMA; RVHTFCH; -.
DR PhylomeDB; Q8ZL91; -.
DR BioCyc; SENT99287:STM3660-MONOMER; -.
DR Proteomes; UP000001014; 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 CDD; cd07808; FGGY_D-XK_EcXK-like; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02220; XylB; 1.
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 InterPro; IPR006000; Xylulokinase.
DR NCBIfam; TIGR01312; XylB; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF6; XYLULOSE 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; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02220};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU003733};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02220};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 1..240
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 249..435
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 233
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 6
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 484 AA; 52597 MW; 5DCD7F4703033459 CRC64;
MYIGIDLGTS GVKAILLNEQ GDVLATHTEK LTVSRPHPLW SEQEPEQWWQ ATDRAVKGLG
RQQSLSGVRA LGIAGQMHGA TLLDSRQQVL RPAILWNDGR CSEECAWLEK QVPQSRAITG
NLMMPGFTAP KLVWVQRHEP DIFYQIDKVL LPKDFLRLRM TGVFASDMSD AAGTMWLDVK
KRDWSDVMLN ACHLTRQQMP ALFEGSDITG TLLPEVASAW GMPAVPVVAG GGDNAAGAVG
VGMIDAGQAM LSLGTSGVYF AVSDGFLSKP ESAVHSFCHA LPERWHLMSV MLSAASCLDW
AAKLTGQENV PALIAAAQQA DEHADSIWFL PYLSGERTPH NNPQAKGVFF GLTHQHGPAE
LARAVLEGVG YALADGMDVV HACGVKPASV TLIGGGARSE YWRQMLSDIS GLQLDYRTGG
DVGPALGAAR LAQIAVNKQT PLADVLPQLP LEQAHYPDAQ RHAVYQQRRE TFRRLYQQLL
PLMS
//
