ID   PGK1_TRYCO              Reviewed;         420 AA.
AC   P41760; P41761;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-MAY-2023, entry version 82.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
GN   Name=C1PGK;
GN   and
GN   Name=C2PGK;
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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; L37337; AAC37222.1; -; Genomic_DNA.
DR   EMBL; L37337; AAC37223.1; -; Genomic_DNA.
DR   EMBL; L37336; AAC37224.1; -; Genomic_DNA.
DR   EMBL; L37336; AAC37225.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41760; -.
DR   SMR; P41760; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000275200; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000275300; -.
DR   VEuPathDB; TriTrypDB:TcIL3000_1_220; -.
DR   OMA; VNEMITG; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PIRSF; PIRSF500126; Pgk_euglenozoa; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..420
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145867"
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         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         375..378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  44897 MW;  0FE519E5EC184061 CRC64;
     MTLNEKKSIN ECDLKGKKTL VRVDFNVPVK GGVITNDYRI RSALPTIQKV LNEGGSCILM
     SHLGRPKGIS ISEAAAVRSA GKVPGYEEAA TLRPVAQRLG ELLSKPVVFA PDCLDAADVV
     KKMSPGDVVL LENVRFYREE GSKKEEEREA MAKVLASYGD IFVSDAFGTA HRDSATMTGI
     PKVLGHGAAG YLMEKEISYF SKVLGNPPRP LVAIVGGSKV SDKIQLLDNM LQRIDYLLIG
     GAMAYTFLKA QGHRIGTSMC EEDRLDLARS LLKKAEDRKV QVLLPVDHVC HTEFKAVDTP
     VVTADADIPD GHMALDIGPK TIANYVETIG KCKSAIWNGP MGVFEMTPYS KGTFAVAKAM
     GDCTQKNGLM SIIGGGDSAS AAEQSGEATR MSHVSTGGGA SLELLEGKTL PGVAILDEKV
//