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Database: UniProt
Entry: GLPK_SALAR
LinkDB: GLPK_SALAR
Original site: GLPK_SALAR 
ID   GLPK_SALAR              Reviewed;         502 AA.
AC   A9MI40;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=SARI_03571;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Activity of this regulatory enzyme is affected by
CC       several metabolites. Allosterically and non-competitively inhibited by
CC       fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier
CC       protein EIIA-Glc (III-Glc), an integral component of the bacterial
CC       phosphotransferase (PTS) system. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium). Heterodimer with
CC       EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc
CC       ion is important for dimerization. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
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DR   EMBL; CP000880; ABX23386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MI40; -.
DR   SMR; A9MI40; -.
DR   STRING; 41514.SARI_03571; -.
DR   KEGG; ses:SARI_03571; -.
DR   HOGENOM; CLU_009281_2_3_6; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
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   Allosteric enzyme; ATP-binding; Glycerol metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..502
FT                   /note="Glycerol kinase"
FT                   /id="PRO_1000077426"
FT   BINDING         14
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         14
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         18
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         84
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         84
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         85
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         85
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         136
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         136
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         246
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         246
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         247
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         268
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         412
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         416
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   502 AA;  56065 MW;  993B20BE36234BC1 CRC64;
     MTEKKYIVAL DQGTTSSRAV VMDHDANIVS VSQREFEQIY PKPGWVEHDP MEIWASQSST
     LVEVLAKADI SSDQIAAIGI TNQRETAIVW ERETGKPIYN AIVWQCRRTA DICEQLKRNG
     LEDYIRDNTG LVVDPYFSGT KVKWILDHVE GSRERAKRGE LLFGTVDTWL IWKMTQGRVH
     VTDYTNASRT MLFNIHDLDW DEKMLDVLDI PRAMLPQVRK SSEVYGQTNI GGKGGTRIPI
     AGIAGDQQAA LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPSGEVN
     YALEGAVFMA GASIQWLRDE MKLISDAFDS EYFATKVKDT NGVYVVPAFT GLGAPYWDPY
     ARGAIFGLTR GVNSNHIIRA TLESIAYQTR DVLEAMQADS GIRLHALRVD GGAVANNFLM
     QFQSDILGTR VERPEVREVT ALGAAYLAGL AVGYWQNLDE LQEKAVIERE FRPGIETTER
     NYRYSGWKKA VQRAMAWEEH DK
//
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