ID   PGKC_CRIFA              Reviewed;         455 AA.
AC   P08967;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-MAY-2023, entry version 98.
DE   RecName: Full=Phosphoglycerate kinase, glycosomal;
DE            Short=Phosphoglycerate kinase C;
DE            EC=2.7.2.3;
GN   Name=PGKC; Synonyms=PGK-C;
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=3402434; DOI=10.1002/j.1460-2075.1988.tb02926.x;
RA   Swinkels B.W., Evers R., Borst P.;
RT   "The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase
RT   of Crithidia fasciculata resides in a carboxy-terminal extension.";
RL   EMBO J. 7:1159-1165(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   -!- SUBCELLULAR LOCATION: Glycosome.
CC   -!- DOMAIN: This glycosomal PGK has a C-terminal extension of 38 AA which
CC       is not present in the cytosolic isoenzyme. This domain most likely
CC       serves as topogenic signal to direct the glycosomal PKG to the
CC       glycosome.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X07459; CAA30342.1; -; Genomic_DNA.
DR   PIR; S00487; TVCRGG.
DR   AlphaFoldDB; P08967; -.
DR   SMR; P08967; -.
DR   VEuPathDB; TriTrypDB:CFAC1_180006900; -.
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   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; 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; 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; Glycosome; Kinase; Nucleotide-binding; Peroxisome;
KW   Transferase.
FT   CHAIN           1..455
FT                   /note="Phosphoglycerate kinase, glycosomal"
FT                   /id="PRO_0000145850"
FT   REGION          417..455
FT                   /note="Topogenic signal"
FT                   /evidence="ECO:0000255"
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         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  47843 MW;  D8BF53AE5A0E1BFE CRC64;
     MSLVPKKSID DAVVKGKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM
     SHLGRPKGAK MSDPKPAKSV RGYEEAATLR PVAARLSELL GQKVEFAPDC LDAASYAAKL
     KGGDVLLLEN VRFYAEEGSK KEEERDAMAK VLAAYGDVYV SDAFGTAHRD SADMTGIPKV
     LGAGYAGYLM EKEINYFAQV LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM
     AYTFQKAQGH AIGISMCEED KLDLAKSLLK KAQERNVEVL LPVDHVCNKE FQGVDAPLVT
     KDVEIPEGYM ALDIGPKTIK IYEDVIAKCK STIWNGPMGV FEMPCYSKGT FAVAKAMGNG
     TQKNGLMSII GGGDTASAAE LSGEAKNMSH VSTGGGASLE LLEGKSLPGV TVLTNKDAKA
     PAAAAAAGGD CPCGSGCAAV PAAATATVSM VLASP
//