ID N1QH82_SPHMS Unreviewed; 595 AA.
AC N1QH82;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN ORFNames=SEPMUDRAFT_160018 {ECO:0000313|EMBL:EMF16581.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF16581.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF16581.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF16581.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB456260; EMF16581.1; -; Genomic_DNA.
DR RefSeq; XP_016764702.1; XM_016907873.1.
DR AlphaFoldDB; N1QH82; -.
DR STRING; 692275.N1QH82; -.
DR GeneID; 27905010; -.
DR eggNOG; KOG2531; Eukaryota.
DR HOGENOM; CLU_016149_5_0_1; -.
DR OMA; STHFFNH; -.
DR OrthoDB; 1704034at2759; -.
DR Proteomes; UP000016931; 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:UP000016931};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 136..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"
FT REGION 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 64829 MW; 23CDC3B71002B1AA CRC64;
MASHGPLYMG FDLSTQQLKG IVVESNLKLI HEAKVDFDAD LSTYGIEKGV LTNPAEGEVF
APPAMWLDAI DLVLSRLREA GLDFNRVKGL SGAGMQHGTV FWSRDASALL SNLDSGKSLK
EQLETGAFAH DMSPNWQDAS TQKQCDAFDA ELGDAETLAE VTGSKAHHRF SGPQILRYRE
KYPEHYEATE RISLVSSFLA SVFLGGFAPI DIADVTGMNL WNIKKGAWDE RLLALAAGGK
HGVEELKKKL GDVPEDGGKA FGCISDYFVG RYGFPKDCQI IPTTGDNPST ILALPLRASD
AMVSLGTSTT FLMSTPQYKP DPAYHFMNHP TTSGLYMFML CYKNGGLARE QIRDQLSSSK
DWDQFNSAAT STPPLSQKSP SDPQRLGLYF PRPEIVPNLP AGQWRYTYNP HSHNLTATAS
SSDFITDDAR TIIESQFLSL RLRSQPLVHS AKDPQTGQLL PPQPRRVYLV GGGSANPAIA
QIAGQVLGGV EGVFKLDIGG NACALGAAYK AVWGCERKSD GGGYQTFEDL IGERWDEDGF
VKRVAEGYTK GVFEQYGEAV EGFREMERVV LEEQGRTAKE AAATQSVRDG NGTAR
//
