ID A0A2N1GIL7_9GAMM Unreviewed; 513 AA. AC A0A2N1GIL7; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-DEC-2020, entry version 11. 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:PKH74250.1}; GN ORFNames=CXF96_09180 {ECO:0000313|EMBL:PKH74250.1}; OS Stenotrophomonas sp. Betaine-02u-21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=2058301 {ECO:0000313|EMBL:PKH74250.1, ECO:0000313|Proteomes:UP000233835}; RN [1] {ECO:0000313|EMBL:PKH74250.1, ECO:0000313|Proteomes:UP000233835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Betaine-02u-21 {ECO:0000313|EMBL:PKH74250.1, RC ECO:0000313|Proteomes:UP000233835}; RA Collins E., Ducluzeau A.-L.; RT "Pharmacopeia of the Arctic Ocean."; RL Submitted (DEC-2017) 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:PKH74250.1}. 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; PJAW01000113; PKH74250.1; -; Genomic_DNA. DR Proteomes; UP000233835; 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 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 Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR SUPFAM; SSF53067; SSF53067; 2. DR TIGRFAMs; TIGR01312; XylB; 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, ECO:0000256|RuleBase:RU364073}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU003733, KW ECO:0000313|EMBL:PKH74250.1}; 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, ECO:0000256|RuleBase:RU364073}. FT DOMAIN 4..248 FT /note="FGGY_N" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 258..440 FT /note="FGGY_C" FT /evidence="ECO:0000259|Pfam:PF02782" FT REGION 79..80 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220" FT ACT_SITE 241 FT /note="Proton acceptor" 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 513 AA; 53572 MW; 8EEBFCDA1D0D41C2 CRC64; MDLVAGIDAG TQSLKVVVYD PAGRNVVASA SALLALASGA DGSREQQPAD WVAALHACFA DIDPALRSRI AALAVSGQQH GFVAVDEAGE VLAPAKLWCD TSSSAECGQI MQAAGGRART IALAGNPVLT GYTASKLPWT KAHRPEAYAR LASILLPHDY LNFVLTGQRF CEYGDASGTG WLDVRTRTWS SELLHATDPE RDLAACLPRI AGPEEVFDID PATATALGLP ATVKVAVGGG DNMMAAIGTG CVVPGRLAMS LGTSGTLFAY SDTPVVDPDG AWAAFCSSTG GWLPLICTMN CTVATEQVAA AFGFSTRDGD AHLRATPPGA DGLVMLPYLN GERTPDLPFG KGMLAGLDTT NMTPAHLYRA AMEGATYSLK YGFDAFVRAG MSFDSIVLTG GGSNSAQWRQ LVADVFGLPV DVPSQPEGAA FGAALQAVWA LGHARGEATS IADIADQHVA LDPLRSARPD PARMQAYATA YARFLRHLDA ITPLYRDGSP STPHPAQRQE DPS //