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Database: UniProt
Entry: A8F3M4_PSELT
LinkDB: A8F3M4_PSELT
Original site: A8F3M4_PSELT 
ID   A8F3M4_PSELT            Unreviewed;       507 AA.
AC   A8F3M4;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU364073};
DE            Short=Xylulokinase {ECO:0000256|RuleBase:RU364073};
DE            EC=2.7.1.17 {ECO:0000256|RuleBase:RU364073};
GN   Name=xylB {ECO:0000256|RuleBase:RU364073};
GN   OrderedLocusNames=Tlet_0188 {ECO:0000313|EMBL:ABV32758.1};
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Pseudothermotoga.
OX   NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV32758.1, ECO:0000313|Proteomes:UP000002016};
RN   [1] {ECO:0000313|EMBL:ABV32758.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABV32758.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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|RuleBase:RU364073};
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; CP000812; ABV32758.1; -; Genomic_DNA.
DR   RefSeq; WP_012002239.1; NZ_BSDV01000001.1.
DR   AlphaFoldDB; A8F3M4; -.
DR   STRING; 416591.Tlet_0188; -.
DR   KEGG; tle:Tlet_0188; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_0_0; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000002016; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro.
DR   CDD; cd07805; FGGY_XK_like_2; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364073};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU364073};
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:ABV32758.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002016};
KW   Transferase {ECO:0000256|RuleBase:RU003733};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW   ECO:0000256|RuleBase:RU364073}.
FT   DOMAIN          3..246
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          256..452
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   507 AA;  56254 MW;  38AFBBF453D108B3 CRC64;
     MSYIISYDLG TTGNKATLFK NDGKLLASVF HPYETNYFNI NWVEQDPNDW YESVKISTQK
     LFKLSKINSD DVKVISFSGQ MMGIVPIDRN GNPLRPAIIW ADQRSITQAD RLKKLGDEKV
     YSITGSRITP TYAGPKISWI KDNEPDVYSN AFKFLFAKDF IIYKLTGIAG TDFSDASLSL
     IFDIRKKQWS AELAEILNID IGKLPEVSAS TSIVGTVIPS VASELGLSEK TLVVRGAGDG
     SAATIGAGVF DSCEAYVYLG SSSWISTCTS EPFFDSKART FNFCYPIPDF YCPTGTMQSG
     GGSYQWAKNA LCQFEEKLAK ELNLNVYSIM DDLVDSTNPG AKGLIFLPYL VGERSPHWNV
     NAKGAFIGLS VTHNKNDMLR AVLEGVSFNL KMILDVFEKS GGYNFKKIRL IGGGAKGRNW
     RQIIADVFQK PIAVAKFPEE ATSIGAAIIG GIGTKIITIN DAKNFVKDLC LVEPRSMYFK
     RYEKMYEVFQ KSYYSLLESF DLLAKID
//
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