ID Q8IDI4_PLAF7 Unreviewed; 501 AA.
AC Q8IDI4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=glycerol kinase {ECO:0000256|ARBA:ARBA00012099};
DE EC=2.7.1.30 {ECO:0000256|ARBA:ARBA00012099};
DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|ARBA:ARBA00043149};
GN ORFNames=PF3D7_1351600 {ECO:0000313|EMBL:CAD52637.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD52637.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.,
RA Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corto C., Cronin A., Davies R.,
RA Davies P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James D.,
RA Johnson D., Kerhornou A., Knight A., Kontfortov B., Keyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., McLean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M-A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0007829|PDB:2W40, ECO:0007829|PDB:2W41}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=19040641; DOI=10.1111/j.1365-2958.2008.06544.x;
RA Schnick C., Polley S.D., Fivelman Q.L., Ranford-Cartwright L.C.,
RA Wilkinson S.R., Brannigan J.A., Wilkinson A.J., Baker D.A.;
RT "Structure and non-essential function of glycerol kinase in Plasmodium
RT falciparum blood stages.";
RL Mol. Microbiol. 71:533-545(2009).
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005190}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family.
CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|RuleBase:RU003733}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL844509; CAD52637.1; -; Genomic_DNA.
DR RefSeq; XP_001350228.1; XM_001350192.1.
DR PDB; 2W40; X-ray; 1.49 A; A/B/C/D=1-501.
DR PDB; 2W41; X-ray; 2.41 A; A/B=1-501.
DR PDBsum; 2W40; -.
DR PDBsum; 2W41; -.
DR AlphaFoldDB; Q8IDI4; -.
DR SMR; Q8IDI4; -.
DR STRING; 36329.Q8IDI4; -.
DR PaxDb; 5833-PF13_0269; -.
DR EnsemblProtists; CAD52637; CAD52637; PF3D7_1351600.
DR GeneID; 814234; -.
DR KEGG; pfa:PF3D7_1351600; -.
DR VEuPathDB; PlasmoDB:PF3D7_1351600; -.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; Q8IDI4; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 2734344at2759; -.
DR PhylomeDB; Q8IDI4; -.
DR BRENDA; 2.7.1.30; 4889.
DR Reactome; R-PFA-75109; Triglyceride biosynthesis.
DR SABIO-RK; Q8IDI4; -.
DR UniPathway; UPA00618; UER00672.
DR EvolutionaryTrace; Q8IDI4; -.
DR Proteomes; UP000001450; Chromosome 13.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:GeneDB.
DR GO; GO:0004370; F:glycerol kinase activity; ISS:GeneDB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; ISS:GeneDB.
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 CDD; cd07769; FGGY_GK; 1.
DR Gene3D; 3.30.420.40; -; 2.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2W40, ECO:0007829|PDB:2W41};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:CAD52637.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0007829|PDB:2W41};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW Transferase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:CAD52637.1}.
FT DOMAIN 3..253
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 262..451
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT BINDING 268
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:2W41"
FT BINDING 313
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:2W41"
FT BINDING 332
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:2W41"
FT BINDING 414
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:2W41"
SQ SEQUENCE 501 AA; 56653 MW; 6713C232D6F99D20 CRC64;
MNVILSIDQS TQSTKVFFYD EELNIVHSNN LNHEQKCLKP GWYEHDPIEI MTNLYNLMNE
GIKVLKDKYT SVIIKCIGIT NQRETVIIWD RITGKPLYNA IVWLDTRVEE LVTEFSAKYN
NNDIQKKTGT YFNTYFSAFK ILWLIQNNPE IKQKIDDGTA VIGNINTWLI FNLTKGNCYT
DVTNASRTLL MDINTLQWDE KMCKIFNITN MSVLPEIKSN CSNFGLVKSE HVPDYLNIPI
TGCIGDQQSA CIGQAIFDEG EAKCTYGTGV FLLINTGEKV VYSTCGLITT ICYKFNDNDK
PKYALEGSIG TAGSGVSWLL KNKLIDDPSE ASDIMEKCEN TTGVIFVPAF SGLYAPRWRS
DARASIYGMT FNTERSHIVR ALLEGIAFQL NEIVDSLTSD MGIEMLHVLR CDGGMTKNKP
FMQFNSDIIN TKIEVSKYKE VTSLGAAVLA GLEVKIWDSL DSVKSLLRRS DAVFHSKMDD
KKRKKKTSEW NKAVERTLIQ L
//
