ID G9ZKL0_9LACO Unreviewed; 504 AA.
AC G9ZKL0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HMPREF9103_00258 {ECO:0000313|EMBL:EHM01139.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHM01139.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHM01139.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHM01139.1,
RC ECO:0000313|Proteomes:UP000004625};
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., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHM01139.1}.
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DR EMBL; AGEY01000012; EHM01139.1; -; Genomic_DNA.
DR RefSeq; WP_008210585.1; NZ_JH414910.1.
DR AlphaFoldDB; G9ZKL0; -.
DR STRING; 797515.HMPREF9103_00258; -.
DR PATRIC; fig|797515.3.peg.238; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_0_9; -.
DR Proteomes; UP000004625; 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 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 5..247
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 258..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 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 9
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 504 AA; 55447 MW; 7F9E11E2C3C518A9 CRC64;
MTDCVLGVDL GTSAVKVSAV TKAGEIIAQE GMDFPLRQPK PGYAEQDPED WVSATTVAIV
RLILNDQLKP EQIKGISYSG QMHGLVLLDA DNQVLRPAML WNDTRSTKQR EEIMAKMGDR
FIEITHNQPL EGFTLPKLLW VKENQPEIFA KAKTMLLPKD YLRFRMTGNL AIDYSDATGT
VMLDVDKQVW SQEILDAFDI PASLCPPLVR SIDNTGNIDD WYAQYSGLST ETVTFGGGAD
NACGAVGAGI DSPTKVLSSI GTSGVILKYE PQKETNYNGV LQYEDHAIPD AFYSMGVTLA
AGFSLSWFKK TFAADEDFTA VVESAAQSTV GANGLLFAPY IVGERAPYAD ADIRGSFIGI
DGIHQRHDFV RAVLEGIIFS FRDLMDEYEA KGSRFDTVVS IGGGAKSPLW QQIQANIFNT
KVVSLKNEQG PGLGAAMLAA VGLGWFKSVS ECTKVFVKFK DVFLPRANDV AKYRKLHDIY
KQIYPSTKEI THELVAYRRE NGEE
//
