ID A0A1X1D8P7_9GAMM Unreviewed; 489 AA.
AC A0A1X1D8P7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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};
GN ORFNames=HA48_11960 {ECO:0000313|EMBL:ORM72997.1};
OS Pantoea wallisii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1076551 {ECO:0000313|EMBL:ORM72997.1, ECO:0000313|Proteomes:UP000193104};
RN [1] {ECO:0000313|EMBL:ORM72997.1, ECO:0000313|Proteomes:UP000193104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26277 {ECO:0000313|EMBL:ORM72997.1,
RC ECO:0000313|Proteomes:UP000193104};
RX PubMed=28255640;
RA Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT "Phylogenomic resolution of the bacterial genus Pantoea and its
RT relationship with Erwinia and Tatumella.";
RL Antonie Van Leeuwenhoek 0:0-0(2017).
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:RU364073}.
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:ORM72997.1}.
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DR EMBL; MLFS01000030; ORM72997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1D8P7; -.
DR STRING; 1076551.HA48_11960; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000193104; 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.
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:RU364073};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02220};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 1..243
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 253..438
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 236
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 489 AA; 52722 MW; 77FB85A1A9D2F831 CRC64;
MYLGIDIGTS ELKALIVDAQ GDIVATQHAT LTVQRPHPHW AEQDPTLWWQ ACNQVMAGLR
QQVPEAWAAI RGIGLSGQMH GAVLLDAAGN VLRPCILWND TRSAAQCEAL RTQHPEMMQI
SANMIMPGFT APKLQWVAEN EPEVFRRIDK VLLPKDYLRW RLTGRFVSEP SDAAGTLWLD
VAQRDWSDTL LAITGLTRAQ MPMLVEGSAV SGTLKAELAS EWGLSTTVSV AGGGGDNAAS
AVGVGAVNPG DAFISLGTSG VIFVVNDRLQ ADPHAGVHAF CHALPGRWHQ MSVMLSAASC
LRWLCNLLSV TESQLMEEMA QLSESRLRAA PLFLPYLSGE RTPHNDPDAS GAFFNLRHET
PRALLGYAVI EGVAFGLADG LAVLGDAQHQ ITQCSLTGGG ARSALWAQLI ADVLQLPIVT
HPASASGALG AARLAWLAEG GAEREVCRKP PVQARYLPDT ARGAVLQQRL RLFRELYVQQ
QQARTLLPA
//
