ID A0A0D1CWJ4_USTMA Unreviewed; 628 AA.
AC A0A0D1CWJ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, 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=UMAG_12177 {ECO:0000313|EMBL:KIS70768.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS70768.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS70768.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003142; KIS70768.1; -; Genomic_DNA.
DR RefSeq; XP_011388138.1; XM_011389836.1.
DR AlphaFoldDB; A0A0D1CWJ4; -.
DR STRING; 237631.A0A0D1CWJ4; -.
DR EnsemblFungi; KIS70768; KIS70768; UMAG_12177.
DR GeneID; 23567931; -.
DR KEGG; uma:UMAG_12177; -.
DR VEuPathDB; FungiDB:UMAG_12177; -.
DR eggNOG; KOG2531; Eukaryota.
DR InParanoid; A0A0D1CWJ4; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004856; F:xylulokinase activity; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0005998; P:xylulose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0005997; P:xylulose metabolic process; IBA:GO_Central.
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 PANTHER; PTHR10196; SUGAR KINASE; 1.
DR PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 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};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 331..523
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 628 AA; 68414 MW; 7A752346FAE419C8 CRC64;
MEGTSPFFLG LDASTQALKA SLLDVDLNVL SELEIRFDRD LPQYKTTGGI SAPAADDDQG
TVVAPVMLYV ESIDMLAERM RSASWPLSRI RAISAAGQQH ASVYFSRAAP RIFTTLSAEK
TLTEQVEQAF SRKVVPNWQD SSTVDACKAF EKAVGGAEKL AQMTGSKAHT RFTGPQIYKF
RTQQPQAYKD TERIGLVSSF ITTLLCVGQG EDESSVIKGI DEADACGMNL LDMRPASSIT
ATKGRIEPGW NQTLLALASG ESEGSDASLG GAVELERKLG SIYRDAGTPV AKIGSWWTKK
YGFSPDCHVF PGTGDNPATF LAFSLAEREA IISLGTSDTV MVATHQFVPD PDFHAFFHPA
RLPSSGDAFF NMLVYKSGSL AREWIRDQYC NSDWAAFNAD VEKFKLQQDG EQRAGFYWLR
PEIIPPGASG IYRYIKPSTC GEWQKVDDFS DKGMNASGIL ETQMLNYRYR SSSIVAGPTT
SSGSAVDTSV LPLQAIYAVG GASSNPTITQ TMADVFGCDI VKPVQPAQDG KEWTPANYNF
CSVGAAYKAA WGWSRLQLKA GEKVPEFDEF VHTTKSSQAK RAGSVREGTG EVKGSVQVIC
RPTEGRTQVY TNVIGAWKQL EERAQKEQ
//
