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GLPK_LACDB
ID   GLPK_LACDB              Reviewed;         502 AA.
AC   Q047N5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=LBUL_1941;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
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   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
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DR   EMBL; CP000412; ABJ59337.1; -; Genomic_DNA.
DR   RefSeq; WP_003620463.1; NC_008529.1.
DR   AlphaFoldDB; Q047N5; -.
DR   SMR; Q047N5; -.
DR   KEGG; lbu:LBUL_1941; -.
DR   HOGENOM; CLU_009281_2_3_9; -.
DR   OMA; FMLMNIG; -.
DR   BioCyc; LDEL321956:LBUL_RS09175-MON; -.
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..502
FT                   /note="Glycerol kinase"
FT                   /id="PRO_1000020740"
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"
SQ   SEQUENCE   502 AA;  55620 MW;  555986D66742DF9E CRC64;
     MSEQYILAID EGTTSTREII FNYAGQQVAS VAREFTQYFP KPGWVEHQAE EIWNAVQITT
     STALINSAIR PDQLAVIGIT NQRETTVVWD KETGRPIYPA IVWQSRQTSD IAEKLVKDSY
     SEMIRQKTGL VIAPYFSATK IRWILDHLEG AQERAEKGEL LFGTIDTWLV WKLTRGKVHV
     TDCTNASRTM LFNIHDLTWD QEILDLLKIP RTMLPEVKSN SEVYGETDPY QFFGGRVPIA
     GMAGDQQAAL FGQLAVKPGM VKNTYETGSF IVMNTGEEPI ESKNNLLTTI GYKLGDQVNY
     ALEGSVFVAG SAIQWLRDSV KLLNSAPESE QAALESKDAN EVYVVPAFTG LGAPYWDSEA
     RGAIFGLTRG SSDKDLIKAT LQSLAYQTRD VVDTMQKDSG IEIPVLRVDG GASNNNYLLQ
     FQADLLGKKI ERAADLETTG LGAAFLAGLA VGYWQDLDSL KEIAKTGAAF APKMEEAERD
     RLYAGWQRAV LATRVFAHGK DF
 
 
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