PGKA_TRYBB
ID PGKA_TRYBB Reviewed; 505 AA.
AC P08891;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphoglycerate kinase A;
DE EC=2.7.2.3;
DE AltName: Full=PGK A allele 2;
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; X05889; CAA29316.1; -; Genomic_DNA.
DR PIR; S00748; TVUT2B.
DR AlphaFoldDB; P08891; -.
DR SMR; P08891; -.
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 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; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..505
FT /note="Phosphoglycerate kinase A"
FT /id="PRO_0000145862"
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 505 AA; 55376 MW; DAECFD31CC0CF2FE CRC64;
MSTAPNAKNN ISLKKSVGDV WPLTAKRVLM 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
EAIVGGAKVS EKIQLLDNMK QRIDYLLIGG AMAYTFLKAQ GYSIGKSKCE ESKLEFARSL
LKKAEDRKVQ VILPIDHVCH TEFKAVDSPL ITEDQNIPEG HMALDIGPKT IEKYVQTIGK
CKSAIWNGPM GVFEMVPYSK GTFAIAKAMG RGTQKRGLMS IIGGGESAGA AEAARISHVS
TGGGASLELL EGKTLPGVAV LDDKE