ID A0A493SYM5_ANAPP Unreviewed; 473 AA.
AC A0A493SYM5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Xylulose kinase {ECO:0000256|ARBA:ARBA00019263, ECO:0000256|RuleBase:RU367058};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU367058};
GN Name=XYLB {ECO:0000313|Ensembl:ENSAPLP00000018646.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000018646.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000018646.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000018646.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Phosphorylates D-xylulose to produce D-xylulose 5-phosphate,
CC a molecule that may play an important role in the regulation of glucose
CC metabolism and lipogenesis. {ECO:0000256|ARBA:ARBA00003260,
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|RuleBase:RU367058};
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU367058}.
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DR AlphaFoldDB; A0A493SYM5; -.
DR Ensembl; ENSAPLT00000026867.1; ENSAPLP00000018646.1; ENSAPLG00000012716.2.
DR GeneTree; ENSGT01000000214434; -.
DR Proteomes; UP000016666; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005997; P:xylulose 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; IPR000577; Carb_kinase_FGGY.
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 PIRSF; PIRSF000538; GlpK; 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:UP000016666};
KW Transferase {ECO:0000256|RuleBase:RU367058};
KW Xylose metabolism {ECO:0000256|RuleBase:RU367058}.
FT DOMAIN 71..223
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 232..415
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 51582 MW; C8DDCB8782E8484C CRC64;
MSESHSLYQG SVKNSSVEQK LGTARQPQLT QVKQHGSVYW KKGSIQTLKN ASPELPLHQL
LKACFAVSNS PIWMDSSTAS QCSNLEKAVG GAQRLAAITG SRAYERFTGN QIAKIYSQNP
EVYTQTERIS LVSSFAASLF LGAYAPIDYS DGSGMNLLQI WEKVWSASCL DACAPGLEEK
LGSPVPSHSV LGSISPYYIQ RYGFSPDCKV VAFTGDNPAS LAGMRLQEGD IAISLGTSDT
LFLWIQEPTP ALEGHILCNP VDSQTFMALL CFKNGSLMRE RIRDDCASGS WDEFSKALSS
TVAGNNGNLG FYFDVMEITP EAVGIHRFNS DNQKVSDFPK EVEIRALIEG QFMAKRIHAE
KLGYKVMPRT RILATGGASH NKKILQVLSD VFNAPVYTID TANSACLGSA YRAIHGLLAE
TNVSLADVVK LAPEPRLAVT PTTGAEELYR PLLKRYAELE QKVIYNPTSC PVK
//
