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Database: UniProt
Entry: A0A2D8PA11_9RHOB
LinkDB: A0A2D8PA11_9RHOB
Original site: A0A2D8PA11_9RHOB 
ID   A0A2D8PA11_9RHOB        Unreviewed;       482 AA.
AC   A0A2D8PA11;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:MAM62277.1};
GN   ORFNames=CMH11_12365 {ECO:0000313|EMBL:MAM62277.1};
OS   Maritimibacter sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM62277.1, ECO:0000313|Proteomes:UP000224593};
RN   [1] {ECO:0000313|Proteomes:UP000224593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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}.
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:MAM62277.1}.
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DR   EMBL; NZNT01000020; MAM62277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8PA11; -.
DR   Proteomes; UP000224593; 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   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          3..242
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          252..436
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            7
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   482 AA;  50378 MW;  A9BC039A1B453A03 CRC64;
     MTFLGIDLGT SGLRALLVDD AGQPIGATER HYKVSHPHPG WSEQDPADWI AALEGAVAEL
     AQNHPAFRDL AGIGVAGHMH GATLLDAQGA VLRPCILWND TRSAEEARRL DGMPGVRAAS
     GNIVFPGFTA PKLDWVRDHE PEVFTQVETV LLPAAYLNFF LTGTPVTDMS DAAGTAWLDT
     GARDWSDDLL AAGHMRRDQM PALVEGSDRA GVLRPELLEA WGLTGPVTVA GGAGDNAAAA
     CGIGALNEGQ GFVSLGTSGV LLAARDGYRP APETAVHTFC HAVPGRWYQM GVMLSATDSL
     NWLAGIAGTT PAGLTADLGD ALAAPGTVRF LPYLSGERTP HNDADIRGAF TGLSAATTRD
     DMTRAVLEGV AYGLRDSFEA LKATGAQMDG LMAIGGGAAS RYWLRLIATV LGVPLALPSG
     GEFGAALGAA RLGMAATGRD VQEIMTAPDV GEVIDPVDDL REVYESAYQA FRAAYPAIRS
     IQ
//
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