ID   PGKE_TRYBB              Reviewed;         420 AA.
AC   P08893;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
DE   AltName: Full=PGK B allele 4;
DE   AltName: Full=Phosphoglycerate kinase B;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3267227; DOI=10.1016/0022-2836(88)90534-7;
RA   le Blancq S.M., Swinkels B.W., Gibson W.C., Borst P.;
RT   "Evidence for gene conversion between the phosphoglycerate kinase genes of
RT   Trypanosoma brucei.";
RL   J. Mol. Biol. 200:439-447(1988).
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   -!- MISCELLANEOUS: In T.brucei, three genes code for phosphoglycerate
CC       kinase isozymes, which are transported to different cell compartments.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X05890; CAA29320.1; -; Genomic_DNA.
DR   PIR; S02234; TVUTG4.
DR   AlphaFoldDB; P08893; -.
DR   SMR; P08893; -.
DR   SABIO-RK; P08893; -.
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   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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..420
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145865"
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;  45087 MW;  98AFF47BEB156D7A CRC64;
     MSLKERKSIN ECDLKGKKVL IRVDFNVPLD DGNITNDYRI RSALPAVQKV LTEGGSCVLM
     SHLGRPKGVS MAEGKELRST GGIPGFEQKA TLKPVAKALS ELLSRPVTFA PDCLNAADVV
     SKMSPGDVVL LENVRFYKEE GSKSTEEREA MAKILASYGD VYISDAFGTA HRDSATMTGI
     PKILGHGAAG YLMEKEISYF AKVLGNPPRP LVAIVGGAKV SDKIQLLDNM LQRIDYLLIG
     GAMAYTFLKA QGYSIGISMC EESKLEFARS LLKKAEDRKV QVILPIDHVC HTEFKAVDSP
     LITEDQNIPE GHMALDIGPK TIEKYVQTIG KCKSAIWNGP MGVFEMVPYS KGTFAIAKAM
     GRGTHEHGLM SIIGGGESAG AAELCGEAAR ISHVSTGGGA SLELLEGKTL PGVTVLDEKE