ID   GLPK_CAEEL              Reviewed;         502 AA.
AC   Q21944;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable glycerol kinase;
DE            Short=GK;
DE            Short=Glycerokinase;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
GN   ORFNames=R11F4.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; FO081682; CCD73301.1; -; Genomic_DNA.
DR   PIR; T16716; T16716.
DR   RefSeq; NP_494721.1; NM_062320.4.
DR   AlphaFoldDB; Q21944; -.
DR   SMR; Q21944; -.
DR   BioGRID; 39103; 1.
DR   DIP; DIP-26828N; -.
DR   STRING; 6239.R11F4.1.2; -.
DR   EPD; Q21944; -.
DR   PaxDb; Q21944; -.
DR   PeptideAtlas; Q21944; -.
DR   EnsemblMetazoa; R11F4.1.1; R11F4.1.1; WBGene00020007.
DR   GeneID; 173747; -.
DR   KEGG; cel:CELE_R11F4.1; -.
DR   UCSC; R11F4.1.1; c. elegans.
DR   CTD; 173747; -.
DR   WormBase; R11F4.1; CE04828; WBGene00020007; -.
DR   eggNOG; KOG2517; Eukaryota.
DR   GeneTree; ENSGT01000000214434; -.
DR   HOGENOM; CLU_009281_2_2_1; -.
DR   InParanoid; Q21944; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 519426at2759; -.
DR   PhylomeDB; Q21944; -.
DR   Reactome; R-CEL-75109; Triglyceride biosynthesis.
DR   UniPathway; UPA00618; UER00672.
DR   PRO; PR:Q21944; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00020007; Expressed in larva and 3 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IBA:GO_Central.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..502
FT                   /note="Probable glycerol kinase"
FT                   /id="PRO_0000059540"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         416..420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  55165 MW;  F0438E95F1A1B189 CRC64;
     MVLLAAIDQG TSSSRFLVFE ADTGELVTSH QIEVRQLFPH GGWVEMDPME LYDTVVSCIS
     KTIEKLENLG ISADEIKSVG VANQRETSIV WDKETGKPLY NAIVWLDTRT SSLADEAISR
     TASKSKDEFR AKTGLPIHPY FSALKLKWLF QNVPEVKKAY ADGNLMFGTV DTWLIWKLTG
     AYVTDVSNAS RTLLLDLHKR KWSTQLCEFF DLPIEILPEI RSSAEVYGHF DKGPLEGVPL
     SGCLGDQQAA MVGHQCLNAG QTKNTYGTGT FMLCNIGTRP IISKNGLLTT VGFQFGADSP
     VVYALEGSGS IGGNVVRFLR DNFKFISDAK EMEGLCRSVE DTSGAYFVPS FTGLYTPYWD
     STARGTILGL TQVTQREHIC LAALRAVAFQ SAEMIAAVEQ DLEGGTKVTT LKVDGGMIAN
     KLFNEIQADI MGRDIVTPKI TEISGWGAAV AGGIGAQQIS LDEFLQQSSE DNRYTPQKDD
     NWRSAELARW KEAVKRSCGW AQ