XKS1_ASPNC
ID XKS1_ASPNC Reviewed; 570 AA.
AC A2QMS4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, 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=An07g03140;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270126; CAL00248.1; -; Genomic_DNA.
DR RefSeq; XP_001391397.1; XM_001391360.2.
DR AlphaFoldDB; A2QMS4; -.
DR SMR; A2QMS4; -.
DR PaxDb; A2QMS4; -.
DR EnsemblFungi; CAL00248; CAL00248; An07g03140.
DR GeneID; 4981581; -.
DR KEGG; ang:ANI_1_1644064; -.
DR VEuPathDB; FungiDB:An07g03140; -.
DR HOGENOM; CLU_016149_5_0_1; -.
DR Proteomes; UP000006706; Chromosome 4L.
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; Reference proteome; Transferase; Xylose metabolism.
FT CHAIN 1..570
FT /note="Probable D-xylulose kinase A"
FT /id="PRO_0000393520"
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; 62762 MW; DB30560DD5868E86 CRC64;
MQGPLYIGFD LSTQQLKGLV VNSDLKVVYV SKFDFDADSH 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 QAAEGFEKME LEVLRQEGKH