ID   PGKB_CRIFA              Reviewed;         417 AA.
AC   P08966;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
DE   AltName: Full=Phosphoglycerate kinase B;
GN   Name=PGKB; Synonyms=PGK-B;
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: Cytoplasm.
CC   -!- DOMAIN: This cytosolic PGK lacks a C-terminal extension of 38 AA which
CC       is present in the glycosomal isoenzyme.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X07458; CAA30341.1; -; Genomic_DNA.
DR   PIR; S00486; TVCRGC.
DR   AlphaFoldDB; P08966; -.
DR   SMR; P08966; -.
DR   VEuPathDB; TriTrypDB:CFAC1_180006900; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; 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; -; 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; 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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..417
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145849"
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   417 AA;  44603 MW;  7D7C2D3625E05DB6 CRC64;
     MSLAPKKTID 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 TVLTNKE