ID   PGKD_TRYBB              Reviewed;         508 AA.
AC   P08892;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-MAY-2023, entry version 105.
DE   RecName: Full=Phosphoglycerate kinase A;
DE            EC=2.7.2.3;
DE   AltName: Full=PGK A allele 4;
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   -!- 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; CAA29319.1; -; Genomic_DNA.
DR   PIR; S02233; TVUT4B.
DR   AlphaFoldDB; P08892; -.
DR   SMR; P08892; -.
DR   UniPathway; UPA00109; UER00185.
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; 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; 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; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..508
FT                   /note="Phosphoglycerate kinase A"
FT                   /id="PRO_0000145863"
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   508 AA;  55668 MW;  D6C96922FDEC498A CRC64;
     MSTAPNAKNN ISLKKSVGDV FRLTAKRVLM RVDFNVPMQN GHITNDYRIR AAIPTIRRVI
     DQGGICILLS HLGRPRGVSM VAGVRDIRRR YHEAQFHDNK GKTAFFSVLP GEEKVKILAK
     SSAREEATHI SPEVKSGKTM LFARLPEDEK KSLLMQYLNE NKDSALPQMS VSAGYEEQYS
     LRPVAVRLAE LLGQHVYFAH DCLDARVEVS RLKRGNVMLL ENVRFYSEEN GENAEEREAM
     AKILASYGDV YISDAFGAAH RDSATMTGIP KILGHGAAGY LMEKEISYFA KVLGNPPRPL
     VAIVGGAKVS EKIQLLDNML QRIDYLLIGG AMAYTFLKAQ GYSIGKSKCE ESKLEFARSL
     LKKAEDRKVQ IILPIDHVCH TEFKAVDSPL ITEDQNIPEG HMALDIGPKT IEKYVQTIGK
     CKSAIWNGPM GVFEMVPYSK GTFAIAKAMG RGTQKRGLMS IIGGGESAGA AELCGKLSIS
     HVSTGGGASL ELLEGKTLPG VAVLDDKE
//