GLPK_DICDI
ID GLPK_DICDI Reviewed; 539 AA.
AC Q54VT8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Name=gk; ORFNames=DDB_G0280371;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000035; EAL67412.1; -; Genomic_DNA.
DR RefSeq; XP_641267.1; XM_636175.1.
DR AlphaFoldDB; Q54VT8; -.
DR SMR; Q54VT8; -.
DR STRING; 44689.DDB0218222; -.
DR PaxDb; Q54VT8; -.
DR EnsemblProtists; EAL67412; EAL67412; DDB_G0280371.
DR GeneID; 8622399; -.
DR KEGG; ddi:DDB_G0280371; -.
DR dictyBase; DDB_G0280371; -.
DR eggNOG; KOG2517; Eukaryota.
DR HOGENOM; CLU_009281_2_3_1; -.
DR InParanoid; Q54VT8; -.
DR OMA; FMLMNIG; -.
DR PhylomeDB; Q54VT8; -.
DR Reactome; R-DDI-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00618; UER00672.
DR PRO; PR:Q54VT8; -.
DR Proteomes; UP000002195; Chromosome 3.
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 Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 2.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 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..539
FT /note="Probable glycerol kinase"
FT /id="PRO_0000343679"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 453..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 60005 MW; 613594EE51F8503B CRC64;
MKPYIGAIDQ GTSSTRFILF DKNGDIVLSH QILLTQHHPH PGWVEHDGNE ILESVNKCIQ
VVMKQYYENN FGTKEDIKAI GITNQRETTI VWDKKTSKPL NNAIVWCDTR TKDLVNYFNN
KAKKLIDDNN IIDNNSKSTT VVDGAQGECK LESKNYLREK CGLPLSSYFS GLKLKWLFDN
CESVREAYGR GDCLMGTIDS WLVWNLTGGK CHITDVTNAS RTMLMNLKTL SWDKELCDFL
EVPIEILPNI HSSSEIYGHV TMGDDEQQQQ QHPLHGIPIA GVLGDQQAAM VGQMCFEKGQ
AKNTYGTGCF LLYNTGNDIV HSRNGLLTTV CYQFGKDSPP IYALEGGVAV AGSGVRWLID
NMGIAESSQE IEDLAKSVQD TGGMYFVPAF SGLFAPYWRD DARGVMVGLT HHTNRCHIAR
SVLESTCLQT FEVLDAMQKD SGNKLVELRV DGGMAKNNLL LQIQSDLLGL PVVKPISLET
TCFGAAFAAG IATGVWKETM QFKIGGKFTP QLDENHKTQK LKEWKKAISK SLDWIDTKN
