ID V7AXD8_PHAVU Unreviewed; 558 AA.
AC V7AXD8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=PHAVU_009G114000g {ECO:0000313|EMBL:ESW09273.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW09273.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|EMBL:ESW09273.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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}.
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DR EMBL; CM002296; ESW09273.1; -; Genomic_DNA.
DR EMBL; CM002296; ESW09274.1; -; Genomic_DNA.
DR RefSeq; XP_007137279.1; XM_007137217.1.
DR RefSeq; XP_007137280.1; XM_007137218.1.
DR AlphaFoldDB; V7AXD8; -.
DR STRING; 3885.V7AXD8; -.
DR EnsemblPlants; ESW09273; ESW09273; PHAVU_009G114000g.
DR EnsemblPlants; ESW09274; ESW09274; PHAVU_009G114000g.
DR GeneID; 18619834; -.
DR Gramene; ESW09273; ESW09273; PHAVU_009G114000g.
DR Gramene; ESW09274; ESW09274; PHAVU_009G114000g.
DR KEGG; pvu:PHAVU_009G114000g; -.
DR eggNOG; KOG2531; Eukaryota.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000000226; Chromosome 9.
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; 3.
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:UP000000226};
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..495
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 558 AA; 61313 MW; DFF0C4244A5B159D CRC64;
MAELTLPQDS YFLGFDSSTQ SLKATVLDSN LHIVASELVH FDSDLPHYKT KDGVYRDPSG
SGRIVSPTLM WVEALDLMLQ KLSKSGFDLA KVAAVSGSGQ QHGSVYWKNG SSQILSSLDP
KRTLLDQLEH AFSINESPVW MDCSTTAECR AIEKACGGAL EFARITGSRA YERFTGPQIK
KMFDTQPEVY DSTERISIVS SFMASLFVGV YAAIDHSDGA GMNLMDLKER TWSKVALEAT
APGLESKLGA LAPAYAVAGN IASYFVQRYH FNKDCLVVQW SGDNPNSLAG LTLNTPGDLA
ISLGTSDTVF MITENPNPGL EGHVFPNPVD AKGYMVMLVY KNGSLTREDV RNRCADKSWD
VFNKFLEQTQ PLNGGKLGFY YKEHEIIPPL PVGFHRYVIE NFSDSLHELK EREVEEEFDP
PSEVRAIVEG QFLSMRAHAE RFGMPSPPKR IIATGGASAN KCILSSIASI FGCDVYTVER
PDSASLGAAL RAAHGLLCKK KGSFIPISEM YMDKAEKTSL SCKLAVNAGD EELVSKYASI
MKKRIEIENR LVQKLGRC
//
