ID X0PP68_9LACO Unreviewed; 504 AA.
AC X0PP68;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=FC83_GL002047 {ECO:0000313|EMBL:KRM34907.1};
OS Agrilactobacillus composti DSM 18527 = JCM 14202.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Agrilactobacillus.
OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM34907.1, ECO:0000313|Proteomes:UP000051236};
RN [1] {ECO:0000313|EMBL:KRM34907.1, ECO:0000313|Proteomes:UP000051236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM34907.1,
RC ECO:0000313|Proteomes:UP000051236};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM34907.1}.
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DR EMBL; AZGA01000020; KRM34907.1; -; Genomic_DNA.
DR RefSeq; WP_035451233.1; NZ_BAMK01000003.1.
DR AlphaFoldDB; X0PP68; -.
DR STRING; 1423734.FC83_GL002047; -.
DR PATRIC; fig|1423734.3.peg.2070; -.
DR eggNOG; COG1070; Bacteria.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000051236; 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:UP000051236};
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; 54685 MW; 809EBE4ECB7010BF CRC64;
MTACVLGVDL GTSSVKVSAV TKTGAIIAQE SADFPLRQPQ PGYAEQDPED WVSATTIAIV
RLILTDKLKP ADIKGISYSG QMHGLVLLDA ANQVLRPAML WNDTRSTKQR AAIMAKMGQR
FIEITHNQPL EGFTLPKLLW VKENQPDIFA QAKTMLLPKD YLRFRMTGKL AMDYSDATGT
VMLDVQQQQW SQEILDAFDI PKSLCPPLVR SIDDTGSISA WYAAYSGLAT TTRTFAGGAD
NACGAVGAGI DSPTKVLSSI GTSGVILKYE PAKNTNYQGV LQFEDHAIPD AFYSMGVTLA
AGFSLNWFKQ TFAADEDFTA VVKSAGKSTV GANGLLFAPY IVGERAPYAD ADIRGSFIGI
DGIHQRHDFV RAVLEGIIFS FQDLLAQYVA QGSQFETVVS IGGGAKSALW QQIQADIFNT
KVVSLANEQG PGLGAAMLAA VGLGWFETVS ECTKVFVHFK DVFLPKPENV AKYQKLHALY
QQIYPSTKAI THGLVAYRRE NNAQ
//
