ID A0A3L6TH34_PANMI Unreviewed; 562 AA.
AC A0A3L6TH34;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=C2845_PM03G14220 {ECO:0000313|EMBL:RLN36036.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN36036.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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:RLN36036.1}.
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DR EMBL; PQIB02000002; RLN36036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6TH34; -.
DR STRING; 4540.A0A3L6TH34; -.
DR Proteomes; UP000275267; Chromosome 3.
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; 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 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, ECO:0000313|EMBL:RLN36036.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 13..288
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 299..496
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 562 AA; 61598 MW; E49AAA4732C544DE CRC64;
MTGPGSLPEG SLFLGFDSST QSLKATVLNN ELTIVASEIV NFDSELPHYK TEGGVYRDST
DDGHIFSPTI MWVEALELLL EKLKPKINFS KVVSVSGSGQ QHGSVYWKKG SKAVLSSLDS
SKSLLLQLKD AFSTMNSPIW MDSSTTKQCR EIENEVGGAL ELAKLTGSRA YERFTGPQIR
KIYQTEPNVY EDTERISLVS SFMASILVGS YASIDETDGA GMNLMDINQR TWSKTVLEAT
APGLEAKLGN LAPAYSAAGR IAPYFVERFQ FDKNCLVIQW SGDNPNSLAG LTLNTPGDLA
ISLGTSDTVF GITAEAKPSL EGHVFPNPVE PDGYMVMLCY KNGSLTREDV RNQCAEKSWD
VFNSYLEKTP PLNGGKLGFY YKDHEILPPL PVGFHRYIVE NLDDASSDNL VEREVAEFNP
PSEVRAIIEG QMLSMRGHAE RFGMPNPPKR IIATGGASSN ESILKSIAQI FGCPVFTVQR
PDSASLGAAL RAAHGWLCNA EGSFVPISCL YEGNLEKTSL GSKLAVPAGD KEEDRELLKK
YTLLMRKRME IERRLVEKIG RA
//
