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Database: UniProt
Entry: A1RAY1_PAEAT
LinkDB: A1RAY1_PAEAT
Original site: A1RAY1_PAEAT 
ID   A1RAY1_PAEAT            Unreviewed;       476 AA.
AC   A1RAY1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 114.
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   ECO:0000313|EMBL:ABM06428.1};
GN   OrderedLocusNames=AAur_3707 {ECO:0000313|EMBL:ABM06428.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM06428.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM06428.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM06428.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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}.
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DR   EMBL; CP000474; ABM06428.1; -; Genomic_DNA.
DR   RefSeq; WP_011776319.1; NC_008711.1.
DR   AlphaFoldDB; A1RAY1; -.
DR   STRING; 290340.AAur_3707; -.
DR   KEGG; aau:AAur_3707; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_12_0_11; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000000637; Chromosome.
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; 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   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   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..229
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          254..434
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        238
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   476 AA;  48360 MW;  1726C7D7B5BCD307 CRC64;
     MPLVAGIDSS TQSCKVVIRD SVTGALVRQG RASHPEGTEV HPDHWWSALQ EAIAQAGGLE
     DVDAVSVGGQ QHGMVCLDES GDVVRPALLW NDTRSATDAE ELILEAGNGD ATAGASYWAS
     RTGTVPVASL TATKLRWLAR NEPGNAQRTA AVCLPHDWLS WRLAGHGPGS GPASLDLLRT
     DRSDASGTGY FSASSGEYLP EVLNSTLGHV PVLPVVVGPL EAAGKTPGGA LIGPGAGDNA
     AAGLGVSAAV GDVVISIGTS GTVFAVSDVP AQDESGLVAG FADATGNYLP LACTLNATRI
     FDATAALLGV TLTELGDLAL SAPEGAEGLT LVPYFEGERT PNLPEATGSL HGITVSNYTP
     ANMARAAVEG VLCSLADGLA ALQAQGGSAQ RIILVGGGAQ STAVQQIAAA AFGLPVFVPA
     PGEYVADGAA RQAAGILTGK LPEWPLEGTE VCHRKTTGNP EFLTRYRHYA AKVAKG
//
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