ID S8DLP9_9LAMI Unreviewed; 536 AA.
AC S8DLP9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
DE Flags: Fragment;
GN ORFNames=M569_14280 {ECO:0000313|EMBL:EPS60522.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS60522.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS60522.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- FUNCTION: Mediates 1-deoxy-D-xylulose (DX) phosphorylation in the
CC cytoplasm prior to the translocation of 1-deoxy-D-xylulose 5-phosphate
CC into plastids. Can also phosphorylate D-xylulose (Xyl). Uses
CC preferentially ATP as cosubstrate. {ECO:0000256|RuleBase:RU367058}.
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|RuleBase:RU367058};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU367058}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS60522.1}.
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DR EMBL; AUSU01007503; EPS60522.1; -; Genomic_DNA.
DR AlphaFoldDB; S8DLP9; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07776; FGGY_D-XK_euk; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR042024; D-XK_euk.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR PANTHER; PTHR10196; SUGAR KINASE; 1.
DR PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 2.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367058};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367058};
KW Kinase {ECO:0000256|RuleBase:RU367058};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 11..288
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 299..481
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT NON_TER 536
FT /evidence="ECO:0000313|EMBL:EPS60522.1"
SQ SEQUENCE 536 AA; 59204 MW; E245B3C0DF1C2E5A CRC64;
MEDSSLPQGS YFLGFDSSTQ SLKATVLDSN LNIVAKEIIT FDSDLPHYNT RGGVLRDPAV
DGRIVSPTVM WVEALDLLLQ KLKKSNFDFR KVAAVSGSGQ QHGSVYWKTG SSSILSSLDS
EKPLLDQLGE AFSLKESPIW MDSSTTEQCK AIEEAIGGPL KLSKLTGSRA HERYTGPQIR
KLFETQPESY KNTERISLVS SFMASLLIGK YAAIDHTDGA GMNLMDIKKR AWSKKALEVT
APDLEAKLGN LAPAYAVAGF ISPYFVERYN FDEKCLIIQW SGDNPNSLAG LTLNTSGDLA
ISLGTSDTVF GITDDHKPSL EGHVFPNPVD LKGYMVMLCY KNGSLTRQEI RDRCADESWE
RFNELLESTP RLNGGKLGFY YKEHEITPPV PVGFHRYVLE NFKGYTLDQV KATQVSDFDP
PSEVRAVIEG QFLSMRCHAE RFGMPSPPKR IIATGGASLN EAILTCIASI FGCNVYTART
TTHPPHTPAP FSFDGRFYFL FLSWGADSAS MGAALRAAHG WLCETRRKFV PIGEMY
//
