ID   XKS1_ASPTN              Reviewed;         573 AA.
AC   Q0CIL2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=ATEG_06472;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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 (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By D-xylose, L-arabinose or L-arabitol.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; CH476602; EAU33016.1; -; Genomic_DNA.
DR   RefSeq; XP_001215650.1; XM_001215650.1.
DR   AlphaFoldDB; Q0CIL2; -.
DR   SMR; Q0CIL2; -.
DR   STRING; 341663.Q0CIL2; -.
DR   EnsemblFungi; EAU33016; EAU33016; ATEG_06472.
DR   GeneID; 4322249; -.
DR   VEuPathDB; FungiDB:ATEG_06472; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OMA; STHFFNH; -.
DR   OrthoDB; 1704034at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase; Xylose metabolism.
FT   CHAIN           1..573
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393523"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         473..474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   573 AA;  63415 MW;  DE092A70270D0BAA CRC64;
     MAISAAQNPL YIGFDLSTQQ LKGLVVNSDL KVVYLSKFDF DADSRGFPIK KGVITNEAEH
     EVYAPVAMWL QALDTVLDGL RQQGLDFSRV KGISGAGQQH GSVYWGDRAE DLLQNLDPSK
     SLEAQLSDAF SHPYSPNWQD ASTQKECDEF DAYLGSQEAL AQATGSKAHH RFTGPQILRF
     QRKYPDVYRH TQRISLVSSF LASLFLGRFA PFDISDVCGM NLWNIKQGAY DEKLLKLCAG
     SFGVDDLKRK LGPVYEDGGL NLGSIHRYYV DRYGFNPDCT IIPATGDNPA TILALPLRPS
     DAMVSLGTST TFLMSTPSYQ PHPATHFFNH PTTAGLYMFM LCYKNGGLAR EQIRDAVNDK
     LGSSDDVWAN FDRTALQTPP LGQKADSDPM KMGLFFPRPE IVPNLRSGQW RFDYNPADGS
     LHETTAGWDQ PLDEARAIIE SQMLSLRLRS RGLTSSPGDG KPPQPRRVYL VGGGSKNKAI
     AKIAGEILGG SEGVYKLEIG DNACALGAAY KAVWALERSN GQTFEDLIGQ RWKEEDFIEK
     IADGYQPGVF EKYGQAVEGF EKMELQVLQQ EKK
//