ID J9VJV0_CRYNH Unreviewed; 626 AA.
AC J9VJV0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=CNAG_05243 {ECO:0000313|EMBL:AFR94498.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94498.2, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR94498.2, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
CC -!- FUNCTION: Highly specific D-xylulose kinase which participates in the
CC catabolism of xylose. Xylose is a major component of hemicelluloses
CC such as xylan. Most fungi utilize D-xylose via three enzymatic
CC reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and
CC xylulokinase, to form xylulose 5-phosphate, which enters pentose
CC phosphate pathway. {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|ARBA:ARBA00001811,
CC 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; CP003823; AFR94498.2; -; Genomic_DNA.
DR RefSeq; XP_012048554.1; XM_012193164.1.
DR AlphaFoldDB; J9VJV0; -.
DR GeneID; 23888572; -.
DR KEGG; cng:CNAG_05243; -.
DR VEuPathDB; FungiDB:CNAG_05243; -.
DR HOGENOM; CLU_016149_5_0_1; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000010091; Chromosome 4.
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-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:AFR94498.2};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 6..290
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 301..513
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 626 AA; 69175 MW; D1D9C1B219F082FF CRC64;
MSSPLFLGLD ASTQSLKASL LSVNLDVVAE CAVHFDSDLP QFGTKGGVHF GSDGQVHSPV
MMLAEAMDLL FDKIKIAGWK VDDIRGVAAA GQQHASVYWS RTSSKLLASL NPSLPLSSQL
AEAFSRPIIP NWQDSSTTAE CQALDAAVGG PAALAQLTGS RAYERFTGAQ IMRFKRVDPV
AYDQTDRIGL VSNTVTTLLC LDGEVKGIDE SDACGMNLWT MNRKQRGWNQ ELLKAIAGDD
GAAELSRKLG TVETDGGRVV GHIGKWFVDR YGFNSECCVF PGTGDNPATF LSLTLRESEG
LVSLGTSDVV LISTSTYHPD PEYHAFFHPA QIAPPSEQDE QNRQGAEPLR YFNMIVYKNG
SLTRQHVRDL YFDGSWDKFN AAIEELRPKS VIDLPSRTAF WWLLPDIVPH GAHGIYKYIT
DPTAGTLFEV PAAKKVDRFP DIRQEALALL ESQLFNYRSR VSSILDDSST TYDPSSPNVD
AFLPRLTKVY ATGGASANRT ILSLMADVLS TKVCKNVEYL DGKWKDADWN ACSVGVAYKA
RWGWERVIAA DGDERKWVGF DTVIRECREA RKKIRGDEGK GLELEEEGIR IIASPGPGSR
AYERRVEWWR ELERKALEEQ RAEKTA
//
