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Database: UniProt
Entry: A0A1E3S1B9_9MYCO
LinkDB: A0A1E3S1B9_9MYCO
Original site: A0A1E3S1B9_9MYCO 
ID   A0A1E3S1B9_9MYCO        Unreviewed;       464 AA.
AC   A0A1E3S1B9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=BHQ17_05265 {ECO:0000313|EMBL:ODQ95397.1};
OS   Mycolicibacterium holsaticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=152142 {ECO:0000313|EMBL:ODQ95397.1, ECO:0000313|Proteomes:UP000094243};
RN   [1] {ECO:0000313|Proteomes:UP000094243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M7 {ECO:0000313|Proteomes:UP000094243};
RA   Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL   Submitted (SEP-2016) 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:ODQ95397.1}.
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DR   EMBL; MIGZ01000019; ODQ95397.1; -; Genomic_DNA.
DR   RefSeq; WP_069404176.1; NZ_MIGZ01000019.1.
DR   AlphaFoldDB; A0A1E3S1B9; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000094243; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000094243};
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          4..219
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          244..425
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        227
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         71..72
FT                   /ligand="substrate"
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   464 AA;  47784 MW;  B24B458ACB53B839 CRC64;
     MDLVAGIDSS TQSCKVVICR ADTGEIVRSA SSPHPAGTEV DPRLWWTALQ SAIDEAGGID
     DVAALSVGAQ QHGMVCLDAS GRTVRNALLW NDTRSDTAAD ELVRELGGAQ QWAQRVGVVP
     VAAITASKLR WLADHEPAHA DATAAVCLPH DWLTWRLSGS SDIAALRTDR SDASGTGYYS
     AERDAYQPDL LELAMRGRRP MVPTVLGPRD VAGHLGSGAV LGPGAGDNAA AALGLGAGLG
     DGIVSLGTSG VVSAVSAAAP HDPEGLVAGF ADATGRHLPL VCTLNGAPVL AAVARMLDVD
     FAELDRLALS APAGAQGLTL VPYLEGERSP NLPGAAGALH GVTTRNLLAA NVARAAVEGV
     LASMAYCIEK ICAQGVDVAR LILVGGAMRS EAVRRIAPAV WGAPVDVPAP AEYVALGAAR
     QAAWTLTQQD SPPVWSFGVT TPYTAEPTPQ VLDQYRAAQP LTLR
//
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