ID XKS1_ASPCL Reviewed; 573 AA.
AC A1CAU3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-APR-2013, entry version 32.
DE RecName: Full=Probable D-xylulose kinase A;
DE Short=Xylulokinase A;
DE EC=2.7.1.17;
GN Name=xkiA; ORFNames=ACLA_012890;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC
OS 3887 / NRRL 1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC mitosporic Trichocomaceae; Aspergillus.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Highly specific D-xylulose kinase which participates in
CC the catabolism of xylose. Xylose is a major component of
CC hemicelluloses such as xylan. Most fungi utilize D-xylose via
CC three enzymatic reactions, xylose reductase (XR), xylitol
CC dehydrogenase (XDH), and xylulokinase, to form xylulose 5-
CC phosphate, which enters pentose phosphate pathway (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + D-xylulose = ADP + D-xylulose 5-
CC phosphate.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- INDUCTION: By D-xylose, L-arabinose or L-arabitol.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DS027049; EAW12861.1; -; Genomic_DNA.
DR RefSeq; XP_001274287.1; XM_001274286.1.
DR ProteinModelPortal; A1CAU3; -.
DR STRING; 5057.CADACLAP00001387; -.
DR EnsemblFungi; CADACLAT00001406; CADACLAP00001387; CADACLAG00001406.
DR GeneID; 4706424; -.
DR KEGG; act:ACLA_012890; -.
DR eggNOG; COG1070; -.
DR HOGENOM; HOG000174850; -.
DR KO; K00854; -.
DR OrthoDB; EOG4578GH; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:EC.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; FALSE_NEG.
DR PROSITE; PS00445; FGGY_KINASES_2; FALSE_NEG.
PE 2: Evidence at transcript level;
KW ATP-binding; Carbohydrate metabolism; Complete proteome; Cytoplasm;
KW Kinase; Nucleotide-binding; Transferase; Xylose metabolism.
FT CHAIN 1 573 Probable D-xylulose kinase A.
FT /FTId=PRO_0000393516.
SQ SEQUENCE 573 AA; 63148 MW; 2248064E535829B4 CRC64;
MASQGPLYIG FDLSTQQLKG LVVNSELKVV HISKFDFDAD SRGFSIKKGV LTNEAEHEVF
APVALWLQAL DGVLDGLRKQ GLDFSRVRGI SGAGQQHGSV YWGENAEKLL GGLDAGKTLE
EQLSGAFSHP FSPNWQDAST QKECDEFDAV LGGPEQLAEA TGSKAHHRFT GPQILRFQRK
YPEVYKKTSR ISLVSSFLAS LLLGHIAPMD ISDVCGMNLW NIRKGAYDED LLKLCAGPFG
MEDLKRKLGD VPEDGGLHLG KINKYYIDRY GFSSDCEILP STGDNPATIL ALPLRPSDAM
VSLGTSTTFL MSTPSYKPDP ATHFFNHPTT PGLYMFMLCY KNGGLAREHV RDAINEKLGS
PASQSWENFD RITLETPPLG QKSESDPMKL GLFFPRPEIV PNLRSGQWRF NYNPANETLT
ESNDGWNNPS DEARAIVESQ MLSLRLRSRG LTQSPGAKIP PQPRRVYLVG GGSKNKAIAK
VAGEILGGSD GVYKLDVGDN ACALGAAYKA VWAMERTPGQ TFEDLIGQRW REEEFIEKIA
DGYQKGVFEK YGNAVEGFEK MEHQVLEQEA ARK
//
