ID A0A2J8GQI1_VIBDI Unreviewed; 483 AA. AC A0A2J8GQI1; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 03-MAY-2023, entry version 20. 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:PNH88256.1}; GN ORFNames=C1M56_10580 {ECO:0000313|EMBL:PNH88256.1}; OS Vibrio diazotrophicus. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=685 {ECO:0000313|EMBL:PNH88256.1, ECO:0000313|Proteomes:UP000236330}; RN [1] {ECO:0000313|Proteomes:UP000236330} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=60.6B {ECO:0000313|Proteomes:UP000236330}; RA Castillo D., Vandieken V., Chang O., Middelboe M.; RT "Draft genome sequences of six Vibrio diazotrophicus strains isolated from RT deep-sea sediments of the Baltic Sea."; RL Submitted (JAN-2018) 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:PNH88256.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; POSH01000008; PNH88256.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2J8GQI1; -. DR STRING; 1348635.BBJY01000006_gene492; -. DR EnsemblBacteria; PNH88256; PNH88256; C1M56_10580. DR Proteomes; UP000236330; 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; IPR018485; Carb_kinase_FGGY_C. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018484; Carb_kinase_FGGY_N. DR InterPro; IPR006000; Xylulokinase. DR PANTHER; PTHR43095; SUGAR KINASE; 1. DR PANTHER; PTHR43095:SF6; 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 TIGRFAMs; TIGR01312; XylB; 1. 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:UP000236330}; 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 1..240 FT /note="Carbohydrate kinase FGGY N-terminal" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 249..432 FT /note="Carbohydrate kinase FGGY C-terminal" FT /evidence="ECO:0000259|Pfam:PF02782" FT ACT_SITE 233 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220" FT BINDING 77..78 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220" FT SITE 6 FT /note="Important for activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220" SQ SEQUENCE 483 AA; 52455 MW; 07D4865CD3AEE51C CRC64; MYMGIDLGTS GVKIILLDEN DKIVASKTKS LTVSRPHELW SEQNPEDWWT ATESIIGELK DEFALSQVRA IGLSGQMHGA TLLDQNGKVL RPAILWNDGR CFEECIELEQ LVPNSREITG NLMMPGFTAP KLKWVQKHEP DVFSKVEKVL LPKDYLRFKL SGDYASDMSD SAGTMWLDVD KRDWSDELLK ATGLGREQMP KLFEGTEVTG QLKKELAELW GMSCVPIVAG AGDNAAGAVG VGITEPGQAM LSLGTSGVYF AVSDGFIANP ESALHSFCHA LPKTWHTMSV ILSAASCLDW VANLTGQADV GTMLKDVEQH ADPKSKVIFL PYLSGERTPH NDPNAKGVFF GMTHSTTKAD LALAVLEGVS FALADGLDAQ HSVSSEPNEI SLIGGGAKSG YWRQMLADIS GMKLVYRSGG EVGPALGAAR LARLGTEVGV TVQDVCPVPE LVQTHLPDES KKELYQAKRK VFQALYTQVK DLF //