ID A0A087VTG1_9BIFI Unreviewed; 501 AA.
AC A0A087VTG1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=BINDI_0409 {ECO:0000313|EMBL:AIC91690.1};
OS Bifidobacterium indicum LMG 11587 = DSM 20214.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341694 {ECO:0000313|EMBL:AIC91690.1, ECO:0000313|Proteomes:UP000028569};
RN [1] {ECO:0000313|EMBL:AIC91690.1, ECO:0000313|Proteomes:UP000028569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11587 {ECO:0000313|EMBL:AIC91690.1,
RC ECO:0000313|Proteomes:UP000028569};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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; CP006018; AIC91690.1; -; Genomic_DNA.
DR RefSeq; WP_033489843.1; NZ_JDUE01000001.1.
DR AlphaFoldDB; A0A087VTG1; -.
DR KEGG; bii:BINDI_0409; -.
DR HOGENOM; CLU_009281_12_0_11; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000028569; Chromosome.
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 NCBIfam; TIGR01312; XylB; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF5; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
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 Reference proteome {ECO:0000313|Proteomes:UP000028569};
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 7..275
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 284..465
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 268
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 501 AA; 53357 MW; 236E253AED32E6AD CRC64;
MNEILVAGID TSTQSCKVRI TEARTGRMVR FGKAPHPDGT SIDPQAWWEA FQEAARQAGG
LDDVSAISVG GQQHGMVLLD DSGQVIRDAL LWNDTRSAPE ADDLIARLGR PPRRADEGDL
DADTMMRGRE RWVRAVGSSP VASLTITKVA WVSRNEPDKA RSIAAICLPH DWLSWAIAGH
GPAAQGNGNA GLESLFTDRS DASGTGYFDS ATDTYRRDLL AMALPEGMAD TVMLPHVLAP
HEIGAKADPR IAGKNVPGGC IIAPGGGDNA MTALGLSMQI GDVSISLGTS GVTAAISPVP
AYDMTASVTG FADATGHWLP LACTINASRI LDAGRTALGV DYDELADLAD QSEPGAAGIT
LIPYFDGERT PNRPDAKASI HGLTLGNTTK ANLARAFVEG LLCSQRDCLE LLKRLGTETR
RILLVGGGAK SRAVRAYAPQ ILGKDVELPK LDEYVAIGAA RQAAWVLSGD NQPPEWSIEV
KETLTGEPEE ETYRQYRSWR K
//
