GLPK_TRYBB
ID GLPK_TRYBB Reviewed; 512 AA.
AC Q9NJP9; Q95PL3;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glycerol kinase, glycosomal;
DE Short=GK;
DE Short=Glycerokinase;
DE EC=2.7.1.30 {ECO:0000269|PubMed:10759857, ECO:0000269|PubMed:11154065};
DE AltName: Full=ATP:glycerol 3-phosphotransferase;
GN Name=GK; Synonyms=GLK1;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702 {ECO:0000312|EMBL:AAF61320.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF ALA-141, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=427;
RX PubMed=10759857; DOI=10.1046/j.1432-1327.2000.01238.x;
RA Kralova I., Rigden D.J., Opperdoes F.R., Michels P.A.M.;
RT "Glycerol kinase of Trypanosoma brucei. Cloning, molecular characterization
RT and mutagenesis.";
RL Eur. J. Biochem. 267:2323-2333(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-3, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=MITat 1.2;
RX PubMed=11154065; DOI=10.1515/bc.2000.132;
RA Steinborn K., Szallies A., Mecke D., Duszenko M.;
RT "Cloning, heterologous expression and kinetic analysis of glycerol kinase
RT (TbGLK1) from Trypanosoma brucei.";
RL Biol. Chem. 381:1071-1077(2000).
CC -!- FUNCTION: Catalyzes the phosphorylation of glycerol using ATP
CC (PubMed:10759857, PubMed:11154065). Under anoxic conditions, when
CC glycerol 3-phosphate accumulates in the glycosome, it catalyzes the
CC reverse reaction, maintaining the ATP balance (PubMed:10759857,
CC PubMed:11154065). Key enzyme for the survival of bloodstream forms
CC under anoxic conditions (PubMed:11154065).
CC {ECO:0000269|PubMed:10759857, ECO:0000269|PubMed:11154065,
CC ECO:0000303|PubMed:11154065}.
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:0000269|PubMed:10759857,
CC ECO:0000269|PubMed:11154065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21645;
CC Evidence={ECO:0000269|PubMed:10759857, ECO:0000269|PubMed:11154065};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21646;
CC Evidence={ECO:0000269|PubMed:10759857, ECO:0000269|PubMed:11154065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for ATP {ECO:0000269|PubMed:10759857};
CC KM=0.246 mM for ATP {ECO:0000269|PubMed:11154065};
CC KM=0.56 mM for ADP {ECO:0000269|PubMed:10759857};
CC KM=3.29 mM for ADP {ECO:0000269|PubMed:11154065};
CC KM=0.44 mM for glycerol {ECO:0000269|PubMed:10759857};
CC KM=0.169 mM for glycerol {ECO:0000269|PubMed:11154065};
CC KM=3.83 mM for sn-glycerol 3-phosphate {ECO:0000269|PubMed:10759857};
CC KM=12.56 mM for sn-glycerol 3-phosphate
CC {ECO:0000269|PubMed:11154065};
CC pH dependence:
CC Optimum pH is 8.0 (PubMed:10759857). Optimum pH is 8.5 for glycerol
CC phosphorylation and 7.0 for ATP formation (PubMed:11154065).
CC {ECO:0000269|PubMed:10759857, ECO:0000269|PubMed:11154065};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000305|PubMed:10759857, ECO:0000305|PubMed:11154065}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000269|PubMed:11154065}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; AF132295; AAF61320.1; -; Genomic_DNA.
DR EMBL; AJ319055; CAC67800.1; -; mRNA.
DR AlphaFoldDB; Q9NJP9; -.
DR SMR; Q9NJP9; -.
DR BRENDA; 2.7.1.30; 6520.
DR SABIO-RK; Q9NJP9; -.
DR UniPathway; UPA00618; UER00672.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IDA:GeneDB.
DR GO; GO:0004370; F:glycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; NAS:UniProtKB.
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; PS00445; FGGY_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycerol metabolism; Glycolysis; Glycosome; Kinase;
KW Nucleotide-binding; Peroxisome; Transferase.
FT CHAIN 1..512
FT /note="Glycerol kinase, glycosomal"
FT /id="PRO_0000059541"
FT MOTIF 510..512
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
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 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 422..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 3
FT /note="Y -> I"
FT /evidence="ECO:0000269|PubMed:11154065"
FT MUTAGEN 141
FT /note="A->S: Increased affinity for glycerol and glycerol
FT 3-phosphate."
FT /evidence="ECO:0000269|PubMed:10759857"
FT CONFLICT 508..509
FT /note="KW -> SG (in Ref. 2; CAC67800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56366 MW; A4A642AA0C572DB0 CRC64;
MKYVGSIDQG TTSTRFIIFD ERQRPVSVHQ VPHTQHTPHP GWLEHDPMEI FRSACKCMSV
AIAKLRQKDA SFRKIEAIGI TNQRETTVAW DRVTKEPLCY APVWNDLRTY DITKKVTAEL
GGGDSMFASK ITGLPVSTYF AAFKMRWMLE NVPAVADACR RGTLCFGTID TWLMYKLSGG
KAFVTDVTNA SRTFLMDLRT RKWSPELCEK LKIPMETLPE IRSNSELFGY VETDECGVAA
ALNERTPIMG SIGDQQSALF GNMCFEKGEA KNTYGTGCFL LMNVGEEARF SKHGLLSTVG
FQVGRDGPCY YALEGAIACA GATVEWMRRN MNLFSHITEC EKLARSVPGT QGIVFVPAFS
GLLAPYWDPS ARGTIVGMTL KTTRAHVIRA ALQAIALQLN DVVGSMKRDA GLNLSSLRVD
GGLSKNGLLM EIQASLLGVD ILVPSMHETT ALGAALCAGL AAGVWTSLEE VKAVSRRENS
WKTVSPSGSA MEREAMIAEW REALKRTKWA KL
