ID U4LBI6_PYROM Unreviewed; 562 AA.
AC U4LBI6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=PCON_11114 {ECO:0000313|EMBL:CCX11520.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX11520.1};
RN [1] {ECO:0000313|EMBL:CCX11520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX11520.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX11520.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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; HF935626; CCX11520.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LBI6; -.
DR STRING; 1076935.U4LBI6; -.
DR eggNOG; KOG2531; Eukaryota.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000018144; 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 PANTHER; PTHR10196; SUGAR KINASE; 1.
DR PANTHER; PTHR10196:SF57; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 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:CCX11520.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU367058};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 300..505
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 562 AA; 61412 MW; 2E84C31255071CEE CRC64;
MSATYLGFDL SSSGLKCLAV TPDLKAVHEE SITFDQDLPS YGVSGGVLKN ETENEVYAPV
AMWIEALDLL LQRMKDNGFD FSTVKGMSGA GQQHGSVYWS DKAEDLLKSL DPTKTLVDQL
SPSAFTHPFS PNWQDHSTQP ECEQFETTSC SGDSLAHTTG SRAHHRFTGP QIKRFLRLRP
EIYESTPRIS LVSSFLCSLF LGKIAPLDIS DVCGMNLWSI PTNSWDETLL ALTAEGSKDG
AAGLKTKLGE VSQHPGENLG AISQFFVSRY GFTPSCIITP FTGDNPSTIL ALPLRPMDAI
LSLGTSTTLL MVTETYKTSV EYHMFNHPTT RGLYMFMLCY CNGALAREEL KDTLNNGKGG
DWSAFNQAAL SSPIAGKSTP SAPAKLGIYF PLPENIPNVR AGTWRFTYDG QSIKETSEGW
NIPHDDARSI LESQALSMRL RSDPLLEEAG DKRQPRRLYV VGGGSKNEAI VEVMAQVLGA
KEGVYRLDVG SNACALGAAY LAAWGGEAEG AAFEDWVQER WDESSMVKKI AEGYREGVWE
TYGELVEGLR LVEKSIVGRA SN
//