GLPK_THETH
ID GLPK_THETH Reviewed; 496 AA.
AC O66131;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, FUNCTION, AND
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX PubMed=9540790; DOI=10.1016/s0167-4838(97)00206-9;
RA Huang H.-S., Kabashima T., Ito K., Yin C.-H., Nishiya Y., Kawamura Y.,
RA Yoshimoto T.;
RT "Thermostable glycerol kinase from Thermus flavus: cloning, sequencing, and
RT expression of the enzyme gene.";
RL Biochim. Biophys. Acta 1382:186-190(1998).
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 ECO:0000269|PubMed:9540790}.
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 and p-
CC chloromercuribenzoate (PCMB). {ECO:0000269|PubMed:9540790}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
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 -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase system
CC (PTS), including enzyme I, and histidine-containing protein (HPr) are
CC required for the phosphorylation of, which leads to the activation of
CC the enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; AB004569; BAA28283.1; -; Genomic_DNA.
DR AlphaFoldDB; O66131; -.
DR SMR; O66131; -.
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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Glycerol metabolism; Kinase;
KW Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..496
FT /note="Glycerol kinase"
FT /id="PRO_0000059516"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="substrate"
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 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 244..245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 410..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT MOD_RES 230
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 496 AA; 54836 MW; 359B64124493F51B CRC64;
MNQYMLAIDQ GTTSSRAILF NQKGEIVHMA QKEFTQYFPQ PGWVEHNANE IWGSVLAVIA
SVLSEAQVKP EQVAGIGITN QRETTVVWEK DTGNPIYNAI VWQSRQTAGI CDELKAKGYD
PLFRKKTGLL IDAYFSGTKV KWILDHVDGA RERAERGELL FGTIDTWLIW KLSGGRVHVT
DYSNASRTLM FNIHTLEWDD ELLDILGVPK AMLPEVRPSS EVYAKTAPYH FFGVEVPIAG
AAGDQQAALF GQACFTEGMA KNTYGTGCFM LMNTGEKAVA SKHGLLTTIA WGIDGKVEYA
LEGSIFVAGS AIQWLRDGLR MIKTAADSET YAEKVESTDG VYVVPAFIGL GTPYWDSEVR
GAVFGLTRGT TKEHFIRATL ESLAYQTKDV LAVMEADSGI SLTTLRVDGG AVKNNFLMQF
QSDLLAVPVE RPVVNETTAL GAAYLAGLAV GYWNSRDDIA AQWQLERRFE PKMDDDKRTM
LYDGWKKAVR AAMAFK
