ID   PGKC_LEIMA              Reviewed;         479 AA.
AC   P50312;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Phosphoglycerate kinase, glycosomal;
DE            EC=2.7.2.3;
DE   AltName: Full=Phosphoglycerate kinase C;
DE   AltName: Full=gPGK;
GN   Name=PGKC;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=9497041; DOI=10.1016/s0166-6851(97)00172-2;
RA   McKoy G.E.M., Badal M., Prescott Q., Lux H., Hart D.T.;
RT   "Characterisation of phosphoglycerate kinase genes in Leishmania major and
RT   evidence for the absence of a third closely related gene or isoenzyme.";
RL   Mol. Biochem. Parasitol. 90:169-181(1997).
RN   [2]
RP   ERRATUM OF PUBMED:9497041.
RA   McKoy G.E.M., Badal M., Prescott Q., Lux H., Hart D.T.;
RL   Mol. Biochem. Parasitol. 93:161-161(1998).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Glycosome.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; L25121; AAC12659.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50312; -.
DR   SMR; P50312; -.
DR   STRING; 5664.LmjF.20.0100; -.
DR   VEuPathDB; TriTrypDB:LmjF.20.0100; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_200006000; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_300041800; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   BRENDA; 2.7.2.3; 2950.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR027250; Pgk_euglenozoa.
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   PIRSF; PIRSF500126; Pgk_euglenozoa; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Glycosome; Kinase; Nucleotide-binding; Peroxisome;
KW   Transferase.
FT   CHAIN           1..479
FT                   /note="Phosphoglycerate kinase, glycosomal"
FT                   /id="PRO_0000145854"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  51576 MW;  ADEAC5489E9F8393 CRC64;
     MSLVLKKSID DATVRDKKVL IRVDFNVPVK NGKITNDFRI RSALPTIQKV LKEGGSCILM
     SHLGRPKGAR MSDPSPEKGV RGYEEAATLR PVAARISELL GQKVEFAPDC LDAASYASKL
     KNADVLLLEN VRFYAEEGSK KEEERDAMAK VLASYGDVYV SDAFGTAHRD SATMTGIPKV
     LGAGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM
     AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERNVQVF LPVDHVCNKE FKAADSPLVT
     ESVDVPDGYM ALDIGPRTIH MYEEVIGRCK SAIWNGPMGV FEMPCYSKGT FAVAKAMGTG
     TQKNGLMSII GGGDSASAAE LSGEAKNMSH VSTGGGASLE LLEGKTLPGV AILTDKDVKE
     RGASCKFAFG VGSPSREACP LRCGHIFGGA SIVREIVKIV VALLIGIFIG RRMSTKLIR