GLPK_DELAS
ID GLPK_DELAS Reviewed; 498 AA.
AC A9BRV2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Daci_1023;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX33669.1; -; Genomic_DNA.
DR RefSeq; WP_012202955.1; NC_010002.1.
DR AlphaFoldDB; A9BRV2; -.
DR SMR; A9BRV2; -.
DR STRING; 398578.Daci_1023; -.
DR PRIDE; A9BRV2; -.
DR EnsemblBacteria; ABX33669; ABX33669; Daci_1023.
DR GeneID; 60685585; -.
DR KEGG; dac:Daci_1023; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_4; -.
DR OMA; FMLMNIG; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000000784; 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 Reference proteome; Transferase.
FT CHAIN 1..498
FT /note="Glycerol kinase"
FT /id="PRO_1000098728"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 81..82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 242..243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 412..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ SEQUENCE 498 AA; 53089 MW; 342D8AACE5FEC5FD CRC64;
MTYLLALDQG TSSSRSIVFD TQGRIVASAQ LELPQIYPRP GWVEHDPREI WRTQLATARE
ALAKAGLAAA DIRALGITNQ RETTVVWNRA TGQPIHHAIV WQDRRAEPLC AQLREAGHAD
TIQRKTGLLI DAYFSGTKLR WILDNVNGAR AAAERGELAF GTVDSWLIWQ LTGGRRHVTD
VSNASRTMLF NVHTNQWDDD LLALLEIPRA LMPEVLPSAA DFGRTAAEVL GGEIAIGGVA
GDQQSALFGQ ACFSAGMAKN TYGTGCFMLM HTGGVFQTSA NGLLTTAAAQ PTAAPAYALE
GSVFVGGAVV QWLRDGLRAI EHSGQVQQLA ESVPDSGGVM MVPAFTGLGA PYWKPDARGT
ITGLTRGTTI AHIARAALES IAFQSAALLL AMSRDAVASG GAPVSELRVD GGACVNNLLM
QFQADLLGIP VVRPACVETT ALGAAYLAGL SSGVYQSTEE LSALWKAERR FVPTLDKHRA
DELMARWEHA VAQTALAA
