ID   XKS1_ASPNG              Reviewed;         570 AA.
AC   Q8X167;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=D-xylulose kinase A;
DE            Short=Xylulokinase A;
DE            EC=2.7.1.17;
GN   Name=xkiA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=11606204; DOI=10.1046/j.0014-2956.2001.02482.x;
RA   vanKuyk P.A., de Groot M.J., Ruijter G.J., de Vries R.P., Visser J.;
RT   "The Aspergillus niger D-xylulose kinase gene is co-expressed with genes
RT   encoding arabinan degrading enzymes, and is essential for growth on D-
RT   xylose and L-arabinose.";
RL   Eur. J. Biochem. 268:5414-5423(2001).
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:0000269|PubMed:11606204}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.76 mM for D-xylulose {ECO:0000269|PubMed:11606204};
CC         KM=0.061 mM for ATP {ECO:0000269|PubMed:11606204};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By D-xylose, L-arabinose or L-arabitol.
CC       {ECO:0000269|PubMed:11606204}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; AJ305311; CAC83746.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X167; -.
DR   SMR; Q8X167; -.
DR   PaxDb; 5061-CADANGAP00005475; -.
DR   VEuPathDB; FungiDB:An07g03140; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1120560; -.
DR   VEuPathDB; FungiDB:ATCC64974_45440; -.
DR   VEuPathDB; FungiDB:M747DRAFT_334296; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   OrthoDB; 1704034at2759; -.
DR   BioCyc; MetaCyc:MONOMER-13191; -.
DR   SABIO-RK; Q8X167; -.
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   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase; Xylose metabolism.
FT   CHAIN           1..570
FT                   /note="D-xylulose kinase A"
FT                   /id="PRO_0000393521"
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         364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         469..470
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   570 AA;  62809 MW;  DB28E6CC2728EE86 CRC64;
     MQGPLYIGFD LSTQQLKGLV VNSDLKVVYV SKFDFDADSR GFPIKKGVLT NEAEHEVFAP
     VALWLQALDG VLEGLRKQGM DFSQIKGISG AGQQHGSVYW GENAEKLLKE LDASKTLEEQ
     LDGAFSHPFS PNWQDSSTQK ECDEFDAALG GQSELAFATG SKAHHRFTGP QIMRFQRKYP
     DVYKKTSRIS LVSSFIASLF LGHIAPMDIS DVCGMNLWNI KKGAYDEKLL QLCAGSSGVD
     DLKRKLGDVP EDGGIHLGPI DRYYVERYGF SPDCTIIPAT GDNPATILAL PLRASDAMVS
     LGTSTTFLMS TPSYKPDPAT HFFNHPTTAG LYMFMLCYKN GGLARELVRD AVNEKLGEKP
     STSWANFDKV TLETPPMGQK ADSDPMKLGL FFPRPEIVPN LRSGQWRFDY NPKDGSLQPS
     NGGWDEPFDE ARAIVESQML SLRLRSRGLT QSPGEGIPAQ PRRVYLVGGG SKNKAIAKVA
     GEILGGSEGV YKLEIGDNAC ALGAAYKAVW AMERAEGQTF EDLIGKRWHE EEFIEKIADG
     YQPGVFERYG QAVEGFEKME LEVLRQEGKH
//