ID B0X8P6_CULQU Unreviewed; 544 AA.
AC B0X8P6;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN Name=6049218 {ECO:0000313|EnsemblMetazoa:CPIJ015417-PA};
GN ORFNames=CpipJ_CPIJ015417 {ECO:0000313|EMBL:EDS42638.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS42638.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS42638.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ015417-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ015417-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate,
CC a molecule that may play an important role in the regulation of glucose
CC metabolism and lipogenesis. {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; DS232495; EDS42638.1; -; Genomic_DNA.
DR RefSeq; XP_001866018.1; XM_001865983.1.
DR AlphaFoldDB; B0X8P6; -.
DR STRING; 7176.B0X8P6; -.
DR EnsemblMetazoa; CPIJ015417-RA; CPIJ015417-PA; CPIJ015417.
DR GeneID; 6049218; -.
DR KEGG; cqu:CpipJ_CPIJ015417; -.
DR VEuPathDB; VectorBase:CPIJ015417; -.
DR VEuPathDB; VectorBase:CQUJHB017535; -.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_8_0_1; -.
DR InParanoid; B0X8P6; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000002320; 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 GO; GO:0005997; P:xylulose 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, ECO:0000313|EMBL:EDS42638.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 132..286
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 294..485
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 544 AA; 60307 MW; 5E9DB70C34CCAD40 CRC64;
MQSENETYLG FDLSTQKLKA VLLNTRLENV AHAEVKFDSD LPEFRTSGGV NAGAAKNEFY
VQPVMWVKAL DMVLDRLVVQ GGDLSTVMAV SGSAQQHGSL YWSRSGLQTL RNLDADKFLH
TQIDDSAFTV HRTPIWMDGT TGEQCEQMEE AVGGRDKMVE ITGSKCYERF TGPQIRKVFQ
QRPDVYRNTE RISLVSSFLA SIFLGDVAPI DFSDGSGMNL LDIRQRAWSD VCLTACAPNL
DAKLGTPVRA DSVIGSIGQF FVQRYNFNTG CKVVAFTGDN LSALAGMTIG QDWLALSLGT
SDTLMMKLNE PPNLQEGHVL VHPTEDGFMG LLCFRNGSLV RDIFKRAEAN DNWENFSELL
DSTPRGNFGN MALHFISKEI IPPVKGSLRW NKTSSLESSE SARGVLKYSA PQTEIRALVE
GQMLTRKAFA TEMGFSFGEN TRILATGGAS ANRSILQVCS DVFNAPVYIQ QTTEAALVGA
AYRAKYVLEK SRGLQRSYYD YVTQLLPEHS VTRVCDPAQD SSDIYDGMLE RQRQMVGYLK
EHQD
//
