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GLPK_OCEIH
ID   GLPK_OCEIH              Reviewed;         500 AA.
AC   Q8ENK7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=OB2475;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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: Activated by phosphorylation and inhibited by
CC       fructose 1,6-bisphosphate (FBP). {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).
CC       {ECO:0000255|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: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; BA000028; BAC14431.1; -; Genomic_DNA.
DR   RefSeq; WP_011066868.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENK7; -.
DR   SMR; Q8ENK7; -.
DR   STRING; 221109.22778161; -.
DR   EnsemblBacteria; BAC14431; BAC14431; BAC14431.
DR   KEGG; oih:OB2475; -.
DR   eggNOG; COG0554; Bacteria.
DR   HOGENOM; CLU_009281_2_3_9; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 233605at2; -.
DR   PhylomeDB; Q8ENK7; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
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   HAMAP; MF_00186; Glycerol_kin; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..500
FT                   /note="Glycerol kinase"
FT                   /id="PRO_0000059473"
FT   BINDING         13..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         83..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         245..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         411..415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   MOD_RES         231
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   500 AA;  55668 MW;  D48292EB263764FF CRC64;
     MSEKFILSID QGTTSSRAIL FNHKGEIVES AQKEFEQFFP KPGWVEHDAN EIWTSVLACI
     ADVLRKADIE ANQIEGIGIT NQRETTVVWD KNTGRPIYKA IVWQSRQTEG ICKELKEQGH
     EDTIRHKTGL LIDPYFSGTK VKWILDNVDG AREKAEAGEL SFGTIDSWLI YRLSGGKTHV
     TDYSNASRTL MFNIYDLKWD DELLEILDVP KSMLPEVKPS SEVYANTVSY HFFGEEVPIA
     GVAGDQQAAL FGQACFDQGM AKNTYGTGCF LLMNTGEEPV RSKHGLLTTI AWGVDGKVEY
     ALEGSIFVAG SAIQWLRDGL RLIESSPQSE ALASQVETTD GVYLVPAFVG LGTPYWDSDA
     RGAVFGLTRG TTKEHFVRAT LESLAYQTKD VMDAMLADSD IDLKKLRVDG GAVKNNLLMQ
     FQSDILGVTV ERPVVQETTA LGSAYLAGLA VGFWKDKEEI AKQWLNEKTF ENEMSEEESS
     YLYKGWQKAV EATRSFKFES
 
 
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