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Database: UniProt
Entry: A0A2R8B9W7_9RHOB
LinkDB: A0A2R8B9W7_9RHOB
Original site: A0A2R8B9W7_9RHOB 
ID   A0A2R8B9W7_9RHOB        Unreviewed;       483 AA.
AC   A0A2R8B9W7;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
GN   Name=xylB {ECO:0000256|HAMAP-Rule:MF_02220,
GN   ECO:0000256|RuleBase:RU364073, ECO:0000313|EMBL:SPH19832.1};
GN   ORFNames=ASD8599_00572 {ECO:0000313|EMBL:SPH19832.1};
OS   Ascidiaceihabitans donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Ascidiaceihabitans.
OX   NCBI_TaxID=1510460 {ECO:0000313|EMBL:SPH19832.1, ECO:0000313|Proteomes:UP000244880};
RN   [1] {ECO:0000313|EMBL:SPH19832.1, ECO:0000313|Proteomes:UP000244880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8599 {ECO:0000313|EMBL:SPH19832.1,
RC   ECO:0000313|Proteomes:UP000244880};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_02220}.
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|HAMAP-Rule:MF_02220,
CC         ECO:0000256|RuleBase:RU364073};
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_02220, ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; OMOR01000001; SPH19832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8B9W7; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000244880; 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-KW.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07808; FGGY_D-XK_EcXK-like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02220; XylB; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR006000; Xylulokinase.
DR   NCBIfam; TIGR01312; XylB; 1.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF6; 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.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02220};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU003733};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244880};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU003733};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_02220}.
FT   DOMAIN          1..242
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          252..434
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         79..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            6
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   483 AA;  50905 MW;  87A0CF4B4388A3E5 CRC64;
     MFIGLDLGTS GLRALLVDAA GRTIGDANAN YSVSHPHSGW SEQNPKDWTD SCIAVMAALK
     ASYPSDFAKV QGIGMSGHMH GATTLDAEGL VLRPCILWND TRSHSQAARL DSNPVFRKVT
     GNIVFPGFTA PKLVWMAQHE PALFEQVDKV LLPKDYMNFW LTGVAASDMS DSAGTAWLDV
     GARDWSDTLL DATGMRRDQM PMLYEGTEGI GTVKPDIAAL LGLPEDVQVV AGGGDNAVAA
     CGVGAMEDGD GFVSLGTSGV VLTARDGFAP MAETAVHSFC HAVPAQWYQM GVVLAATDSM
     NWLSGITGVT PSELTQALGA TPEPPNDLLF LPYLSGERTP HNDSAVRGGF LGLDIAHTRN
     DMTRAVMEGV CYALRDSLEA LRATGAAPKR LLAIGGGTQS DHWVAMLASI LDLPLDVPAQ
     GEFGAALGAA RLAICGVTGA DPATIMTKPT LARTVHPDPS LVEPYAQGYA RYCKGYSAMK
     ALQ
//
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