GLPK_PEDPA
ID GLPK_PEDPA Reviewed; 504 AA.
AC Q03DS8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=PEPE_1623;
OS Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS 183-1w).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=278197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000422; ABJ68644.1; -; Genomic_DNA.
DR RefSeq; WP_002832953.1; NC_008525.1.
DR AlphaFoldDB; Q03DS8; -.
DR SMR; Q03DS8; -.
DR STRING; 278197.PEPE_1623; -.
DR EnsemblBacteria; ABJ68644; ABJ68644; PEPE_1623.
DR GeneID; 33062399; -.
DR KEGG; ppe:PEPE_1623; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_9; -.
DR OMA; VQWMRDQ; -.
DR OrthoDB; 233605at2; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000000773; 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..504
FT /note="Glycerol kinase"
FT /id="PRO_1000020755"
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 504 AA; 55949 MW; 5C8B8024DA2F4931 CRC64;
MADKYILAID EGTTSTRTII FDHAGNKMAD AQREFPQYFP KPGWVEHNAN EIWNAVLSTI
ANAFIESGIK PNQISGIGIT NQRETTVIWD KKTGLPIYNA VVWQSRQTAE IAEQLVKDGY
GDMIHQKTGL VTDAYFSATK IRWILDHVDG AQARAERGEL LFGTIDTWLM WKLTDGDVHV
TDYSNASRTM LYNIHKLEWD KEILALLNIP ASMLPEVKPN STIYGKTKDY HFYGSEVPIS
GMAGDQQAAL FGQLAFEPGM VKNTYGTGAF TVMNTGEKPQ LSDNNLLTTI GYGINGKVYY
ALEGSIFVAG SAIQWLRDGM KLFKKASESE AAAVASQNDN EVYVVPAFTG LGAPYWDPNA
RGSVFGITRG TTREDFIKAT LQSLAYQSRD VIDTMKKDSG IDIPSIRVDG GASNNDYLMQ
FQSDILGIEI DRASDLETTA LGAAFLAGLA VGFWKDLEDL KKEYKPGKVF KPKMSTDERE
DLYTGWQEAV AATRQFKHRP RQSK
