ID   PGKB_TRYBB              Reviewed;         421 AA.
AC   P07377;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
DE   AltName: Full=PGK B allele 2;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3004970; DOI=10.1002/j.1460-2075.1985.tb04152.x;
RA   Osinga K.A., Swinkels B.W., Gibson W.C., Borst P., Veeneman G.H.,
RA   van Boom J.H., Michels P.A.M., Opperdoes F.R.;
RT   "Topogenesis of microbody enzymes: a sequence comparison of the genes for
RT   the glycosomal (microbody) and cytosolic phosphoglycerate kinases of
RT   Trypanosoma brucei.";
RL   EMBO J. 4:3811-3817(1985).
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; X03370; CAA27068.1; -; Genomic_DNA.
DR   EMBL; X05889; CAA29317.1; -; Genomic_DNA.
DR   PIR; A25119; KIUTGC.
DR   AlphaFoldDB; P07377; -.
DR   SMR; P07377; -.
DR   BRENDA; 2.7.2.3; 6520.
DR   SABIO-RK; P07377; -.
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..421
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145864"
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         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         376..379
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  45154 MW;  33AE32B02B51D1C5 CRC64;
     MSLKERKSIN ECDLKGKKVL IRVDFNVPLD DGNITNDYRI RSALPAVQKV LTEGGSCVLM
     SHLGRPKGVS MAEGKELGSA GGIPGFEQKA TLKPVAKALS ELLSRPVTFA PDCLNAADVV
     SKMSPGDVVL LENVRFYKEE GSKKSTEERE AMAKILSSYG DVYISDAFGT AHRDSATMTG
     IPKILGNGAA GYLMEKEISY FAKVLGNPPR PLVAIVGGAK VSDKIQLLDN MLQRIDYLLI
     GGAMAYTFLK AQGYSIGISM CEESKLEFAR SLLKKAEDRK VQIILPIDHV CHTEFKAVDS
     PLITEDQNIP EGHMALDIGP KTIEKYVQTI GKCKSAIWNG PMGVFEMVPY SKGTFAIAKA
     MGRGTHEHGL MSIIGGGDSA SAAELSGEAK RMSHVSTGGG ASLELLEGKT LPGVTVLDDK
     E