ID A0A0T6BJU9_9BACI Unreviewed; 499 AA.
AC A0A0T6BJU9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ATH93667.1};
GN ORFNames=AB447_206135 {ECO:0000313|EMBL:KRT90157.1}, COP00_14390
GN {ECO:0000313|EMBL:ATH93667.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT90157.1, ECO:0000313|Proteomes:UP000036168};
RN [1] {ECO:0000313|EMBL:KRT90157.1, ECO:0000313|Proteomes:UP000036168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT90157.1,
RC ECO:0000313|Proteomes:UP000036168};
RX PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT paste.";
RL Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN [2] {ECO:0000313|EMBL:KRT90157.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT90157.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATH93667.1, ECO:0000313|Proteomes:UP000218414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH93667.1,
RC ECO:0000313|Proteomes:UP000218414};
RA Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
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}.
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DR EMBL; CP023481; ATH93667.1; -; Genomic_DNA.
DR EMBL; LECW02000045; KRT90157.1; -; Genomic_DNA.
DR RefSeq; WP_048352748.1; NZ_LECW02000045.1.
DR AlphaFoldDB; A0A0T6BJU9; -.
DR STRING; 1664069.BGLY_4444; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000036168; Unassembled WGS sequence.
DR Proteomes; UP000218414; 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 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: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.
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..247
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 257..442
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 8
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 499 AA; 55050 MW; C5D3954A3FE9597D CRC64;
MEYCIGVDLG TSAVKAILVN RHGGICGEAS KPFSIIEPHA GYSEQDPREW AEKTKEAIKE
LVGGHRGGAD EIKGISFSGQ MHGLVLLDGK GEVLRNAILW NDTRTTEQCR LINEVIGKAR
LLELVKNPAL EGFTLPKLLW IKEHEQEVFQ KAAVFLLPKD YVRYTMTGRI HSEYSDAAGT
LLLDVKHKTW SSEMCRRLGI PEAMCPELVE SGSFVGCLTS KFAEETGLTP EVKVFAGGAD
NACGAVGAGI LQEGTALCSI GTSGVVLSYE KDPDQQFRGN IHLFNHAAPD AYYSMGVTLS
AGRSFSWFKD VFAKDEAFDS LIGEVEESRP GSRGLLFTPY LSGERTPHAD AEIRASFIGM
DSGHRRADVV RSVIEGITFS LHESIEQFRA RGKNISRVIS IGGGAKSEEW LQIQADIFNA
EIIRLKSEQG PAFGAAMIAA VGCGWFPTLE ACAERFVHIK ETFQPRPEYS GQYQHIFPVY
RDVYRYTKPL NERLAFLRE
//
