ID D4TZF0_9ACTO Unreviewed; 456 AA.
AC D4TZF0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ECO:0000313|EMBL:EFF79697.1};
GN ORFNames=HMPREF0970_01331 {ECO:0000313|EMBL:EFF79697.1};
OS Schaalia odontolytica F0309.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=649742 {ECO:0000313|EMBL:EFF79697.1, ECO:0000313|Proteomes:UP000003150};
RN [1] {ECO:0000313|EMBL:EFF79697.1, ECO:0000313|Proteomes:UP000003150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0309 {ECO:0000313|EMBL:EFF79697.1,
RC ECO:0000313|Proteomes:UP000003150};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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, 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:EFF79697.1}.
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DR EMBL; ACYT02000038; EFF79697.1; -; Genomic_DNA.
DR RefSeq; WP_004565340.1; NZ_GG753640.1.
DR AlphaFoldDB; D4TZF0; -.
DR PATRIC; fig|649742.3.peg.1400; -.
DR HOGENOM; CLU_009281_12_0_11; -.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000003150; 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; IPR018483; Carb_kinase_FGGY_CS.
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; 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 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 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 8..254
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 262..443
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 11
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 456 AA; 47257 MW; 22BEED7C4B7B81E8 CRC64;
MGERPFVAGV DSSTQSCKVV VWDPVSGEVV REGRAPHPEG TEVDPRAWWD ALNEAVAAAG
GLDDVRALSV GAQQHGMVVL DERGEVIRPA LLWNDTRSAG AARDLIAERE GDSTGEAWWA
DATGSVPVAS LTVTKLRWLA DHEPEAAQRV AAVCLPHDYL TWRIAGGFER LGLEGLATDR
SDASGTGYVD RSGSAYRRDI LAQALRCDEE RAEHIVLPRI AEPYEVVAHG DEARGWGEIA
LGPGAGDNAA AALGVDLGPG AAMLSLGTSG VVAAVSESAV SDPSGLVTGF SDASGRWLPL
ACTLNASRII DAMRRVTGLG YEEFDEAALS VPDAGGLRLI PYFEGERTPN LPDATATLEG
MTLANCDPAH VARAAVEGLL TLMRGALDAV RAQGVPIERV VMVGGGARSR AVRALASGIL
GAEVEVPSPA EYVALGAAKQ AAALNVADPG AGGSDV
//
