ID G0S4E8_CHATD Unreviewed; 573 AA.
AC G0S4E8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=CTHT_0022560 {ECO:0000313|EMBL:EGS20426.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS20426.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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:0000256|ARBA:ARBA00025184,
CC ECO:0000256|RuleBase:RU367058}.
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; Evidence={ECO:0000256|ARBA:ARBA00001811,
CC ECO:0000256|RuleBase:RU367058};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU367058}.
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DR EMBL; GL988041; EGS20426.1; -; Genomic_DNA.
DR RefSeq; XP_006692722.1; XM_006692659.1.
DR AlphaFoldDB; G0S4E8; -.
DR STRING; 759272.G0S4E8; -.
DR GeneID; 18256294; -.
DR KEGG; cthr:CTHT_0022560; -.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_5_0_1; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU367058};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367058};
KW Kinase {ECO:0000256|RuleBase:RU367058};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 134..291
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 301..514
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 573 AA; 62866 MW; E4922814EF5A2D8D CRC64;
MSNGPLYLGF DLSTQQLKAV VVQSDLQVVA DAKVDFDQDF GAKYGIKKGV LHNHAEGEVF
APVALWLESL DLVLQRLKEK NTPLNRIRGI SGSCQQHGSV YWSHQAQSLL AALKPEKALV
EQLADAFSHP YAPNWQDHST QQECDQFDVK LGSPERLAEV TGSAAHHRFT GTQIMRLKRK
LPDMYANTSR ISLVSSFLAS LFLGAIAPMD ISDVCGMNLW DIPSNDWSNP LLELAAGGPE
GAAELRHKLG EVEKDGGASL GRISSYFTAK YGFSPNCEIA PFTGDNPATI LALPLRPLDA
IVSLGTSTTF LMITPVYKPD PSYHFFNHPT TPGQYMFMLC YKNGSLAREK VRDALPKPTD
SPDPWANFNK AALAVPPLDV RSNSDRAKLG LYFYLPEIVP NIRAGTWRYT CNPTDGSDLQ
EETEEWPVET DARVIVESQA LSMRLRSQNL VSKPDPSGKL PAQPRRVYLV GGGSLNPAIQ
SILADVLGGA EGVYKLDVGG NACALGGAYK AVWAFERVQG ETFDELIGKR WKEEGAIQKV
AEGYREGVFE QYGSVLGAFE EMEQRILKVA KNT
//
