GenomeNet

Database: UniProt
Entry: A0A010Q0X2_9PEZI
LinkDB: A0A010Q0X2_9PEZI
Original site: A0A010Q0X2_9PEZI 
ID   A0A010Q0X2_9PEZI        Unreviewed;       570 AA.
AC   A0A010Q0X2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE            EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN   ORFNames=CFIO01_11441 {ECO:0000313|EMBL:EXF73397.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF73397.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF73397.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF73397.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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. {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXF73397.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JARH01001065; EXF73397.1; -; Genomic_DNA.
DR   RefSeq; XP_007602955.1; XM_007602893.1.
DR   AlphaFoldDB; A0A010Q0X2; -.
DR   STRING; 1445577.A0A010Q0X2; -.
DR   KEGG; cfj:CFIO01_11441; -.
DR   eggNOG; KOG2531; Eukaryota.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   OrthoDB; 1704034at2759; -.
DR   Proteomes; UP000020467; 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, ECO:0000313|EMBL:EXF73397.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Transferase {ECO:0000256|RuleBase:RU367058};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW   ECO:0000256|RuleBase:RU367058}.
FT   DOMAIN          134..245
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          301..512
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   570 AA;  61933 MW;  C78AFE55D9D4E846 CRC64;
     MSSGPLYLGF DLSTQQLKAI VVQSDLTVVS EAKVDFDADF GKQYGLRKGV LTNEAEGEVY
     APVAMFLEAI DLVLSRLSAK TPMDRIKGIS GSCQQHGSTY WGQEAETLLG GLPQSDKPLV
     EQLKEAFSFP YAPNWQDHST QAQCDEFDAN FETAQRLAEV TGSAAHHRFT GTQIMRLRQK
     RPEMYAATSR ISLVSSFLAS VLLGSVAPID ISDVCGMNLW DISAGNWSEP LLELTAGSKS
     GVSDLRAKLG EPRHDGGGSM GAISGYFVRR YGFSAECQVA PFTGDNPATI LALPLRPMDA
     IVSLGTSSTF LMVTPVYKPD AAYHFFNHPC TPGQYMFMLC YKNGGLARES VRDALPKPEG
     GDPWANFNKA VLDTPPLDVR SEKDDAKLGL YFDLPEIVPN IKAGTWRYTA KQDGSALTEA
     SEPWSKETDA RIIVESQALS MRLRSQNLVH SPESDSKVPA QPRRIYLVGG GSLNPAIARV
     MGDVLGGAEG VYKLDVGGNA CALGGAYKAV WALERGEGET FDELIGKRWK EEGAIQKVDG
     GYKEGVFEGY QPVVGAFEEM EKRILKVAHN
//
DBGET integrated database retrieval system