ID A0A1L6HT90_9BURK Unreviewed; 495 AA.
AC A0A1L6HT90;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BTO02_03730 {ECO:0000313|EMBL:APR34682.1};
OS Paraburkholderia sp. SOS3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR34682.1, ECO:0000313|Proteomes:UP000184708};
RN [1] {ECO:0000313|EMBL:APR34682.1, ECO:0000313|Proteomes:UP000184708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SOS3 {ECO:0000313|EMBL:APR34682.1,
RC ECO:0000313|Proteomes:UP000184708};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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:RU364073}.
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DR EMBL; CP018811; APR34682.1; -; Genomic_DNA.
DR RefSeq; WP_075155895.1; NZ_CP018811.1.
DR AlphaFoldDB; A0A1L6HT90; -.
DR STRING; 1926494.BTO02_03730; -.
DR KEGG; para:BTO02_03730; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000184708; Chromosome 1.
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|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
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..439
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 495 AA; 52972 MW; 041EBF44A6D67D6F CRC64;
MYLGIDLGTS EVKVLLLASD GRVIGTAGSP FTVSRPHPRW SEQNPVDWWE GTRAALFALR
ERHPGEFAQI RGIGLSGQMH GAVLLDAQDR VLRPAILWND MRSVEECAEL TERAPELHRV
AGNLAMPGFT APKLLWVARH EPEIFRQTAC VLLPKDYLRL QLTGGKVSDP SDAAGTLWLD
VAKRDWSDSL LAACNLSRAH MPALAEGSAP SGMLKPELAR ELGLREPVVV AAGGGDNATS
AIGIGATQPG DGFVSLGTSG VLCVIGDSFR PNPESAVHAF CHAIPHRWHQ MSVVLSAASC
LRWVCKLTGT NETSLLPEIE ALPEAALTHA PIFLPYLSGE RTPHNDPYAQ GVFFGMTHAT
DRALLGYAVL EGVTLALTDG LDALKAAGTE ANALSLLGGG ARSNYWGQLL ADALNTNTRK
HGGGETGAAL GAARLGWLAA GGDPAQVLTK PPVEIEFTPN PQRHAVLRRR LEHYRALYRQ
LKPLFAQTAT SDPQA
//
