ID   PGKG_TRYCO              Reviewed;         509 AA.
AC   P41762;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Phosphoglycerate kinase, glycosomal;
DE            EC=2.7.2.3;
GN   Name=56PGK;
OS   Trypanosoma congolense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=5692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IL3000;
RX   PubMed=7770090; DOI=10.1016/0166-6851(94)00208-5;
RA   Parker H.L., Hill T., Alexander K.A., Murphy N.B., Fish W.R., Parsons M.;
RT   "Three genes and two isozymes: gene conversion and the compartmentalization
RT   and expression of the phosphoglycerate kinases of Trypanosoma (Nannomonas)
RT   congolense.";
RL   Mol. Biochem. Parasitol. 69:269-279(1995).
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.
CC   -!- SUBCELLULAR LOCATION: Glycosome.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; L37337; AAC37221.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41762; -.
DR   SMR; P41762; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000275400; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_1_240; -.
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; -; 3.
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..509
FT                   /note="Phosphoglycerate kinase, glycosomal"
FT                   /id="PRO_0000145868"
FT   BINDING         33..35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         434
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         464..467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  55963 MW;  EA3FFD44B9426B3A CRC64;
     MSHVTGVTSN IRIKKTIDDI WPLTAKRVLV RVDFNVPIQN GHITNDYRIR ATIPTIQRII
     DQGGICILLS HLGRPAGISM TTAVRDVRRR YHEAHFHDNK GKTAFFSVLP PEEKIKILAQ
     SSLREEATHI MPGVKSGKTI LFARLPEDEK KQLLMQYLDE KKDNGLPQLS VSAGYEEQYS
     LRPVAVRLAE LLGQHVYFAH DCMDAKMELS RLKRGNVMLL ENVRFYREED SKKEEEREAM
     AKVLASYGDI FVSDAFGTAH RDSATMTGIP KVLGHGAAGY LMEKEISYFS KVLGNPPRPL
     VAIVGGSKVS DKIQLLDNML QRIDYLLIGG AMAYTFLKAQ GHRIGTSMCE EDRLDLARSL
     LKKAEDRKVQ VLLPVDHVCH TEFKAVDTPV VTADADIPDG HMALDIGPKT IANYVETIGK
     CKSAIWNGPM GVFEMTPYSK GTFAVAKAMG DCTQKNGLMS IIGGGDSASA AEQSGEATRM
     SHVSTGGGAS LELLEGKTLP GVAILDDKE