PGKD_TRYBB
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-AUG-2022, entry version 102.
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 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..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