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Entry: W7DTK0_9LIST
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ID   W7DTK0_9LIST            Unreviewed;       497 AA.
AC   W7DTK0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Glycerol kinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000256|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000256|HAMAP-Rule:MF_00186,
GN   ECO:0000313|EMBL:EUJ58525.1};
GN   ORFNames=MCOL2_07941 {ECO:0000313|EMBL:EUJ58525.1};
OS   Listeria fleischmannii FSL S10-1203.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1265822 {ECO:0000313|EMBL:EUJ58525.1, ECO:0000313|Proteomes:UP000019241};
RN   [1] {ECO:0000313|EMBL:EUJ58525.1, ECO:0000313|Proteomes:UP000019241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL S10-1203 {ECO:0000313|EMBL:EUJ58525.1,
RC   ECO:0000313|Proteomes:UP000019241};
RA   den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Novel taxa of Listeriaceae from agricultural environments in the United
RT   States.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC       glycerol 3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000256|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation and inhibited by
CC       fructose 1,6-bisphosphate (FBP). {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium).
CC       {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system
CC       (PTS), including enzyme I, and histidine-containing protein (HPr) are
CC       required for the phosphorylation, which leads to the activation of the
CC       enzyme. {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|HAMAP-Rule:MF_00186,
CC       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:EUJ58525.1}.
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DR   EMBL; AODM01000025; EUJ58525.1; -; Genomic_DNA.
DR   RefSeq; WP_007544027.1; NZ_AODM01000025.1.
DR   AlphaFoldDB; W7DTK0; -.
DR   PATRIC; fig|1265822.4.peg.1620; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000019241; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07786; FGGY_EcGK_like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00186; Glycerol_kin; 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; IPR005999; Glycerol_kin.
DR   NCBIfam; TIGR01311; glycerol_kin; 1.
DR   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00186};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798, ECO:0000256|HAMAP-
KW   Rule:MF_00186};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00186}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00186};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00186}.
FT   DOMAIN          5..252
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          262..450
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   BINDING         13..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         83..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         245..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   BINDING         411..415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
FT   MOD_RES         231
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   497 AA;  55257 MW;  FDE644D0C7DD0FF1 CRC64;
     MEKKYILALD QGTTSSRAMI IDSDGEVIGV EQEEFEQIFP KPGWVEHNAN EIWASILAVI
     AGVLLKTNIS SKQIAGIGIT NQRETAVVWD KETGNPIYNA IVWQSRQTAD ICKELKEAGK
     EEMVREKTGL LIDAYFSGTK VRWILDNVDG AQERAEAGEL LFGTIDSWLV WKLTGGKAHV
     TDYSNASRTL LYNIYDLKWD DDLLEMLNIP KSMLPEVRQS SEVYETTVPY HFFGEEVPVA
     GIAGDQQSAL FGQGCFESGM AKNTYGTGCF LLMNTGEKAV RSENGLLTTL AWGIDGKVEY
     ALEGSIFVAG SAIQWLRDGL RMLRQSSDSE GYAEKIESSD GVYVVPAFVG LGAPYWDSDV
     RGAVFGLTRG TEKEQFVRAT LESLAYQTRD VLHAMEEDSK IKLKALRVDG GASANDFLMQ
     FQADILNVPV ERPDNLETTV LGAAYLAGLA VGVWEDKNEI VKRWKLDKKF DVKMKEDERE
     TLYDGWHKAV KAAQSFK
//
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