ID   XKS1_ASPFN              Reviewed;         572 AA.
AC   B8NTI4;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA; ORFNames=AFLA_098240;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963484; EED46161.1; -; Genomic_DNA.
DR   RefSeq; XP_002383697.1; XM_002383656.1.
DR   AlphaFoldDB; B8NTI4; -.
DR   SMR; B8NTI4; -.
DR   STRING; 5059.CADAFLAP00011562; -.
DR   EnsemblFungi; EED46161; EED46161; AFLA_098240.
DR   VEuPathDB; FungiDB:AFLA_098240; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OMA; QHGTVFW; -.
DR   Proteomes; UP000001875; 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   GO; GO:0005998; P:xylulose catabolic process; IEA:EnsemblFungi.
DR   CDD; cd07776; FGGY_D-XK_euk; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR042024; D-XK_euk.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase; Xylose metabolism.
FT   CHAIN           1..572
FT                   /note="Probable D-xylulose kinase A"
FT                   /id="PRO_0000393518"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         470..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   572 AA;  62910 MW;  E8A5D99221835427 CRC64;
     MQGPLYIGFD LSTQQLKALV VNSDLKVVYV SKFDFDADSR GFPIKKGVIT NEAEHEVYAP
     VALWLQALDG VLEGLKKQGL DFARVKGISG AGQQHGSVYW GQDAERLLKE LDSGKSLEDQ
     LSGAFSHPYS PNWQDSSTQK ECDEFDAFLG GADKLANATG SKAHHRFTGP QILRFQRKYP
     EVYKKTSRIS LVSSFLASLF LGHIAPLDIS DACGMNLWNI KQGAYDEKLL QLCAGPSGVE
     DLKRKLGAVP EDGGINLGQI DRYYIERYGF SSDCTIIPAT GDNPATILAL PLRPSDAMVS
     LGTSTTFLMS TPNYMPDPAT HFFNHPTTAG LYMFMLCYKN GGLAREHIRD AINDKLGMAG
     DKDPWANFDK ITLETAPMGQ KKDSDPMKMG LFFPRPEIVP NLRAGQWRFD YNPADGSLHE
     TNGGWNKPAD EARAIVESQF LSLRLRSRGL TASPGQGMPA QPRRVYLVGG GSKNKAIAKV
     AGEILGGSDG VYKLEIGDNA CALGAAYKAV WALERKDGQT FEDLIGQRWR EEDFIEKIAD
     GYQKGVFEKY GAALEGFEKM ELQVLKQEGE TR