ID   PGKA_CRIFA              Reviewed;         505 AA.
AC   P25055;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphoglycerate kinase, glycosomal;
DE            Short=Phosphoglycerate kinase A;
DE            EC=2.7.2.3;
GN   Name=PGKA; Synonyms=PGK-A;
OS   Crithidia fasciculata.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX   NCBI_TaxID=5656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1542317; DOI=10.1016/0166-6851(92)90245-f;
RA   Swinkels B.W., Loiseau A., Opperdoes F.R., Borst P.A.;
RT   "A phosphoglycerate kinase-related gene conserved between Trypanosoma
RT   brucei and Crithidia fasciculata.";
RL   Mol. Biochem. Parasitol. 50:69-78(1992).
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: Glycosome.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X17251; CAA35114.1; -; Genomic_DNA.
DR   PIR; S14463; KICRGF.
DR   AlphaFoldDB; P25055; -.
DR   SMR; P25055; -.
DR   PRIDE; P25055; -.
DR   VEuPathDB; TriTrypDB:CFAC1_180007100; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0020015; C:glycosome; 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; -; 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; Glycosome; Kinase; Nucleotide-binding; Peroxisome;
KW   Transferase.
FT   CHAIN           1..505
FT                   /note="Phosphoglycerate kinase, glycosomal"
FT                   /id="PRO_0000145848"
FT   BINDING         30..32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         460..463
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   505 AA;  54758 MW;  E184277AAB86D355 CRC64;
     MLLSTQSIPI KKSVDDIWPV AGKRVLIRVD FNVPTSSGGI DDDFRIRSAI PTIRRIVDQG
     GICILISHLG RPTGVDYDTA HAEQEKRQTP VQLPNSRGKT AFFSGLRGDA KATILAWSSQ
     REKAATLSNP YGSGKTAVFA RLPEEEKRRL LLRFMSEHKE ELFPQLGSAG YEKEFSLEPV
     AVKLAELLDQ HVYFGHDCLG AQADIAKLRC GEVMLLENLR FYTNENSSDE RKRMLMARIL
     ASYADVYIND AFGTAHRDSA SLTGIPRVLQ QGAAGYLMEK EISYFSKVLN NPPRPLLAII
     GGAKLSDKMQ VLENLLDCVD SLFIGGGLAY TFLRSQGYSI GTSHFEEAFV PFAQALPLAG
     SGRQVRVVLP EDHVCHAHTR PAEAPLTTTS ANIPDGYAGL DIGPLTIQSI THLVRQCSSV
     IWNGPLGMFE MPYYAFGTFS IARVVSQSSA AKGTTSIVGG GDTASAMMKS GEAAHISHIS
     TGGNASLELL EGKVLAAVAV LDNKE