PGK_PLAF7
ID PGK_PLAF7 Reviewed; 416 AA.
AC P27362;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK; ORFNames=PFI1105w;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2055463; DOI=10.1016/0378-1119(91)90357-h;
RA Hicks K.E., Read M., Holloway S.P., Sims P.F.G., Hyde J.E.;
RT "Glycolytic pathway of the human malaria parasite Plasmodium falciparum:
RT primary sequence analysis of the gene encoding 3-phosphoglycerate kinase
RT and chromosomal mapping studies.";
RL Gene 100:123-129(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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.D.,
RA Eisen J.A., Rutherford K.M., 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.A.,
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.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., 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., Corton C., Cronin A., Davies R.M.,
RA Davis 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 K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes 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.R.,
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 [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-416 IN COMPLEX WITH AMP.
RX PubMed=15158737; DOI=10.1016/j.bbapap.2004.01.003;
RA Pal B., Pybus B., Muccio D.D., Chattopadhyay D.;
RT "Biochemical characterization and crystallization of recombinant 3-
RT phosphoglycerate kinase of Plasmodium falciparum.";
RL Biochim. Biophys. Acta 1699:277-280(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15158737}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; M59249; AAA29727.1; -; Genomic_DNA.
DR EMBL; AL844508; CAD51907.1; -; Genomic_DNA.
DR PIR; JU0475; JU0475.
DR RefSeq; XP_001352096.1; XM_001352060.1.
DR PDB; 1LTK; X-ray; 3.00 A; A/B/C=2-416.
DR PDB; 3OZ7; X-ray; 2.70 A; A/B=2-415.
DR PDB; 3OZA; X-ray; 3.00 A; A/B/C=2-416.
DR PDBsum; 1LTK; -.
DR PDBsum; 3OZ7; -.
DR PDBsum; 3OZA; -.
DR AlphaFoldDB; P27362; -.
DR SMR; P27362; -.
DR BioGRID; 1208777; 3.
DR IntAct; P27362; 3.
DR STRING; 5833.PFI1105w; -.
DR SwissPalm; P27362; -.
DR PRIDE; P27362; -.
DR EnsemblProtists; CAD51907; CAD51907; PF3D7_0922500.
DR GeneID; 813501; -.
DR KEGG; pfa:PF3D7_0922500; -.
DR VEuPathDB; PlasmoDB:PF3D7_0922500; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; P27362; -.
DR OMA; YVNDAYS; -.
DR PhylomeDB; P27362; -.
DR BRENDA; 2.7.2.3; 4889.
DR Reactome; R-PFA-70171; Glycolysis.
DR Reactome; R-PFA-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P27362; -.
DR Proteomes; UP000001450; Chromosome 9.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..416
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145859"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1LTK"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3OZ7"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1LTK"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:3OZ7"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 262..274
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1LTK"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3OZ7"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:3OZ7"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:3OZ7"
SQ SEQUENCE 416 AA; 45427 MW; 91105E552AE944CF CRC64;
MLGNKLSISD LKDIKNKKVL VRVDFNVPIE NGIIKDTNRI TATLPTINHL KKEGASKIIL
ISHCGRPDGL RNEKYTLKPV AETLKGLLGE EVLFLNDCVG KEVEDKINAA KENSVILLEN
LRFHIEEEGK GVDANGNKVK ANKEDVEKFQ NDLTKLADVF INDAFGTAHR AHSSMVGVKL
NVKASGFLMK KELEYFSKAL ENPQRPLLAI LGGAKVSDKI QLIKNLLDKV DRMIIGGGMA
YTFKKVLNNM KIGTSLFDEA GSKIVGEIME KAKAKNVQIF LPVDFKIADN FDNNANTKFV
TDEEGIPDNW MGLDAGPKSI ENYKDVILTS KTVIWNGPQG VFEMPNFAKG SIECLNLVVE
VTKKGAITIV GGGDTASLVE QQNKKNEISH VSTGGGASLE LLEGKELPGV LALSNK
