ID A0A087CG08_9BIFI Unreviewed; 496 AA.
AC A0A087CG08;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220};
DE Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220};
DE EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220};
GN Name=xylB {ECO:0000256|HAMAP-Rule:MF_02220};
GN ORFNames=BPSY_1057 {ECO:0000313|EMBL:KFI82208.1};
OS Bifidobacterium psychraerophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=218140 {ECO:0000313|EMBL:KFI82208.1, ECO:0000313|Proteomes:UP000029050};
RN [1] {ECO:0000313|EMBL:KFI82208.1, ECO:0000313|Proteomes:UP000029050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21775 {ECO:0000313|EMBL:KFI82208.1,
RC ECO:0000313|Proteomes:UP000029050};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_02220}.
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:KFI82208.1}.
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DR EMBL; JGZI01000009; KFI82208.1; -; Genomic_DNA.
DR RefSeq; WP_033494791.1; NZ_JGZI01000009.1.
DR AlphaFoldDB; A0A087CG08; -.
DR STRING; 218140.BPSY_1057; -.
DR eggNOG; COG1070; Bacteria.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000029050; 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 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; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF5; XYLULOSE KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 2.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02220};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02220};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000313|EMBL:KFI82208.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220};
KW Reference proteome {ECO:0000313|Proteomes:UP000029050};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000313|EMBL:KFI82208.1};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 6..107
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 143..270
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 279..461
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 10
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 496 AA; 52018 MW; 65E97A291B218C9A CRC64;
MAQVLVAGID TSTQSTKVRV TDAATGTMVR FGQAKHPDGT SVDPECWWKA FLEASEQAGG
LDDVSALSVG GQQHGMVLLD AHGEVVRDAL LWNDTRSASN AEDLIARLGA ADRNADEEEL
DDDPQMRGRQ RWVKAVGSSP VASLTITKIA WVAANEPENA AKVAAVCLPH DWLSWRIAGF
GPNGEGDAHL DELFTDRSDA SGTGYFDSAG NDYRMDLFRM AFNRDDVILP RVAAPAEAAA
TADPSIAGRN VPGGCIIAAG GGDNAMASLG LNMTVGDVSI SLGTSGVAAA ISPVPAYDMT
AAVTGFADST GHWLPLACTI NGSRIIDAGR AALGADYEEL TDLALNAEAG AGGLTLIPYF
DGERTPNRPD ATADLHGMTL RNVSRENIAR SFVEGLLCSQ RDCLELIKGL GVSVNRMLLI
GGGARSRAVR ALAPAILGSD VSLPAADEYV AIGAARQAAW ALAQSPEAPI WPLDIEETLS
APATEQVYEQ YARYRG
//
