ID A0A1B9AFQ2_9BACI Unreviewed; 497 AA.
AC A0A1B9AFQ2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A8L44_13805 {ECO:0000313|EMBL:OCA82656.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA82656.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA82656.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA82656.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-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:RU003733}.
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:OCA82656.1}.
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DR EMBL; MAYV01000017; OCA82656.1; -; Genomic_DNA.
DR RefSeq; WP_066108401.1; NZ_MAYV01000017.1.
DR AlphaFoldDB; A0A1B9AFQ2; -.
DR STRING; 1743146.A8L44_13805; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000092673; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000092673};
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..246
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 256..442
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 239
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 497 AA; 55450 MW; B1446B537998F5CB CRC64;
MAYVLGLDLG TSAIKGLLVN KDGNLVAEAT ATYPLDTPQI GFSEQNPKHW IEAANHVMLE
LLEKVPDMKE LLEGISFSGQ MHSLVLLDEK DKPLRPAILW NDVRTTEQCK EIKEKAGELI
LSHTKNIALE GFTLPKILWV QKHEPEIWSK VKRIQLPKDY LRFWLTNQYH MDFSDAAGTL
MLNQDTKEWD HDILSRFDIP KSILPDVVPS TKVVGFLKPE LQEYYGFSRD VKIITGGADN
ACAAVGAGIL QEGIGMCSIG TSGVFLSYEE DAKKNYQGKL HMFHHAMDDA NYSMGVTLAA
GNSLNWFKQN FAPNQSFGEL LADINSVAIG SDGLLFAPYI VGERTPYSDS QIRGSFIGID
THHQLKHFAR SVLEGITFSL MDSKIIMEEI ADKKFDRIVS VGGGAKNNDW LQMQADIFDT
AVVNLTTEQG PGLGAVMLAA VGCGWFSDLN DCAARFVSYK EEIIPKAENV EKYKEVYARY
RKVYEGTKEI CHSYFGK
//
