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Database: UniProt
Entry: A0A094HUJ2_9PEZI
LinkDB: A0A094HUJ2_9PEZI
Original site: A0A094HUJ2_9PEZI 
ID   A0A094HUJ2_9PEZI        Unreviewed;       570 AA.
AC   A0A094HUJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE            EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN   ORFNames=V501_01163 {ECO:0000313|EMBL:KFZ18537.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ18537.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ18537.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-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:KFZ18537.1}.
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DR   EMBL; JPKD01000389; KFZ18537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HUJ2; -.
DR   STRING; 1420914.A0A094HUJ2; -.
DR   HOGENOM; CLU_016149_5_0_1; -.
DR   Proteomes; UP000029315; 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:UP000029315};
KW   Transferase {ECO:0000256|RuleBase:RU367058};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW   ECO:0000256|RuleBase:RU367058}.
FT   DOMAIN          136..292
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          301..510
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   570 AA;  61321 MW;  5614A9A23F964AB9 CRC64;
     MSSSGSGPLY LGFDLSTQQL KAVVITSALN VAHEAKVDFD ADLAHHGITK GVFHPSPKEV
     TAPVAMWLEA VDLVLSRLRE AGAPLDRIRG ISGAGQQHGS VFWNKAGEET LSKLDAKKTL
     VEQLKGGFAC ETSPNWQDAS TQNECDAFDK VLGSEDALAK LTGSKAHHRF TGPQIMKFKK
     NNPDVYEKTS KISLVSSFLA SVFLGSVAPI DISDVCGMNL WNIVEGAWEW DLLTLAAGSK
     EDGEILRRKL GDVRSDGGGS MGAISDYYVQ RYGFSKECQI APFTGDNPST ILSLPLRAGD
     AMVSLGTSTT FLMSTPHFVA DPAVHFFNHP TTSGLYMFML CYKNGGLARE KTRDSLIKSS
     DGNTWSTFEK TVLESPPLGK NTPLDPAKLG LYFPLPEIVP NVRAGTWRFS LANGALTESA
     EGWKIPEDDA RAIVESQALS LRLRSKNLVV SPAAGLPAQP KRIYLVGGGS LSPAIARVMG
     DVLGGVEGVY KLDVGGNACA LGGAYKAVWA VERKGTETFE ELIGARWNES EAVEKVDIGY
     KPQVWQAYGD VLPAFEEAEK QVLASENRAA
//
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