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Database: UniProt
Entry: F7JL18_9FIRM
LinkDB: F7JL18_9FIRM
Original site: F7JL18_9FIRM 
ID   F7JL18_9FIRM            Unreviewed;       489 AA.
AC   F7JL18;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
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};
GN   ORFNames=HMPREF0988_01022 {ECO:0000313|EMBL:EGN30370.1};
OS   Lachnospiraceae bacterium 1_4_56FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658655 {ECO:0000313|EMBL:EGN30370.1, ECO:0000313|Proteomes:UP000004289};
RN   [1] {ECO:0000313|EMBL:EGN30370.1, ECO:0000313|Proteomes:UP000004289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_4_56FAA {ECO:0000313|EMBL:EGN30370.1,
RC   ECO:0000313|Proteomes:UP000004289};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 1_4_56FAA.";
RL   Submitted (MAY-2011) 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:EGN30370.1}.
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DR   EMBL; ACTN01000009; EGN30370.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7JL18; -.
DR   STRING; 658655.HMPREF0988_01022; -.
DR   PATRIC; fig|658655.3.peg.1032; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_0_9; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000004289; 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; 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; 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|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
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:UP000004289};
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          2..244
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          254..436
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         78..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            7
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   489 AA;  53852 MW;  C7086943F78CD761 CRC64;
     MLYIGVDLGT SAVKLLLMDE TGKIHNIVSK EYPLYFPHPG WSEQDPKDWF TQSMEGIREL
     TAECDKSQVA GISFGGQMHG LVALDKNDEV IRPAILWNDG RTEKETDYLN QVIGKEKLSE
     YTANIAFAGF TAPKILWMKE NEPENFARIA KIMLPKDYLA YRLSGVHCTD YSDASGMLLL
     DVKNKCWSKE MMEICSVTEE QLPKLYESYE VVGTLKPEIA AELGLSENVK VVAGAGDNAA
     AAVGTGTVGD GMCNISLGTS GTIFISSKTF GVDEHNALHS FDHADGYYHL MGCMLSAASC
     NKWWMDEILK TAEYSKEQEA ITKLGENNVF YLPYLMGERS PHNDPKARAA FIGMSMDTTR
     EEMTQAVLEG VAFGLRDSLE VAKSLGIRIE RTKICGGGAK SPLWKKIIAN VMNLKVDVIE
     SEEGPGYGGA ILAAVGCGEF ASVEEAAQKL VKVVDTVEPD AELAAKYEER YQKFRKIYPA
     VKGLFRELA
//
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