ID   GLPK_PSETO              Reviewed;         503 AA.
AC   O87924;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
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};
OS   Pseudomonas tolaasii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=29442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PT814;
RA   Murata H.;
RT   "GlpK of Pseudomonas tolaasii.";
RL   Submitted (JUL-1998) 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: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {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   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
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DR   EMBL; AB015974; BAA31995.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87924; -.
DR   SMR; O87924; -.
DR   UniPathway; UPA00618; UER00672.
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; Transferase.
FT   CHAIN           1..503
FT                   /note="Glycerol kinase"
FT                   /id="PRO_0000059480"
FT   BINDING         17..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         87..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         141
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"
SQ   SEQUENCE   503 AA;  55768 MW;  928BEFCC5462C8CE CRC64;
     MTDIQNKNYI IALDQGTTSS RAIIFDRDAN VVCTAQREFT QHYPQAGWVE HDPMEIFATQ
     SAVMVEALAQ AGLHHDQVAA IGITNQRETT VVWDKVTGRP IYNAIVWQCR RSTEIQICQQ
     LKRDGHEQYI NDTTGLVTDP YFSGTKLKWI LDNVEGSRER ARNGELLFGT IDSWLIWKFT
     GGKTHVTDYT NASRTMLFNI HTLEWDAKML EILDVPREML PEVKSSSEIY GRTKVASPSA
     AIAGDQQAAL FGQMCVRGGQ AKNTYGTGCF LLMNTGDKAV KSKHGMLTTI ACGPRGEVAY
     ALEGAVFNGG STVQWLRDEL KIIADATDTE YFAGKVKDSN GVYLVPAFTG LGAPYWDPYA
     RGALFGLTRG VRVDHIIRAA LESIAYQTRD VLDAMQQDSG ERLKALRVDG GAVANNFLMQ
     FQADILGTQV ERPQMRETTA LGAAYLAGLA CGFWGSLEEL RGKAVIEREF EPQLDEAAKE
     KLYAGWQKAV SRTRDWEPHE GAE