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Database: UniProt
Entry: GLPK1_THEMA
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Original site: GLPK1_THEMA 
ID   GLPK1_THEMA             Reviewed;         492 AA.
AC   Q9X049;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Glycerol kinase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase 1 {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK 1 {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK1 {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=TM_0952;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD36033.1; -; Genomic_DNA.
DR   PIR; C72314; C72314.
DR   RefSeq; NP_228760.1; NC_000853.1.
DR   RefSeq; WP_004080610.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X049; -.
DR   SMR; Q9X049; -.
DR   STRING; 243274.TM_0952; -.
DR   PaxDb; 243274-THEMA_09585; -.
DR   EnsemblBacteria; AAD36033; AAD36033; TM_0952.
DR   KEGG; tma:TM0952; -.
DR   eggNOG; COG0554; Bacteria.
DR   InParanoid; Q9X049; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd10427; FGGY_GK_1; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   NCBIfam; TIGR01311; glycerol_kin; 1.
DR   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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..492
FT                   /note="Glycerol kinase 1"
FT                   /id="PRO_0000059513"
FT   BINDING         10
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         10
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         14
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         80
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         80
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         81
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         81
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         132
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         132
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         241
FT                   /ligand="glycerol"
FT                   /ligand_id="ChEBI:CHEBI:17754"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         241
FT                   /ligand="sn-glycerol 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57597"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         263
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         306
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         407
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         407
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         411
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   492 AA;  55091 MW;  7D09C7849FB0221E CRC64;
     MYVLAIDQST SGTKAIIFDE KGGIVHRVTV YHKQYYPKPG WVEHDPEEIF RNTLDACRKV
     IEESGIKPLE IEALAITNQR ETTILWEKKS GKPVYNAVVW QCQRGASLCE EIKKRGLEGK
     IKEKTGLVVD PYFSASKIRW ILDNVEGVKN KAKQGEIAFG TVDSWLIWKL TKGEVHATDF
     SNASRTLLLN IHELRWDEEV LEIFEIPPEI LPELKSSDSV FGYTDLGFLP KKIPIVGVMG
     DSSAALFGQG GFYSGDIKVT YGTGSSTMLN IGEKPNVSDS PIVCSVGWVV KETSSYVLEG
     NIHSAGDTIV WLKEKLGIIS DPSETEKIAL SLENNGGVYL VPAFVGLGAP YWRSDVKAAI
     LGLQRNHGKE HVVRAALESI AYQVRDIFEE MVRISSKEPT EVRADGGITR NRFLMQFQAD
     ILNIPVLVSN IEEVSARGVA FVALLHLGAF SDLEEIRQKI TYREKYEPRM GDELREMYYE
     GWKTAIRKLL TE
//
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