ID   PGKB_LEIMA              Reviewed;         417 AA.
AC   Q27683;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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;
DE   AltName: Full=cPGK;
GN   Name=PGKB;
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin;
RX   PubMed=9497041; DOI=10.1016/s0166-6851(97)00172-2;
RA   McKoy G.E.M., Badal M., Prescott Q., Lux H., Hart D.T.;
RT   "Characterisation of phosphoglycerate kinase genes in Leishmania major and
RT   evidence for the absence of a third closely related gene or isoenzyme.";
RL   Mol. Biochem. Parasitol. 90:169-181(1997).
RN   [2]
RP   ERRATUM OF PUBMED:9497041.
RA   McKoy G.E.M., Badal M., Prescott Q., Lux H., Hart D.T.;
RL   Mol. Biochem. Parasitol. 93:161-161(1998).
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. {ECO:0000250}.
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; L25120; AAC12658.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27683; -.
DR   SMR; Q27683; -.
DR   STRING; 5664.LmjF.20.0110; -.
DR   VEuPathDB; TriTrypDB:LmjF.20.0110; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_000016100; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_300041800; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   BRENDA; 2.7.2.3; 2950.
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_0000145853"
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;  44963 MW;  9EB46B3375FED6D6 CRC64;
     MSLVLKKSID DATVRDKKVL IRVDFNVPVK NGKITNDFRI RSALPTIQKV LKEGGSCILM
     SHLGRPKGAR MSDPSPEKGV RGYEEAATLR PVAARISELL GQKVEFAPDC LDAASYASKL
     KNADVLLLEN VRFYAEEGSK KEEERDAMAK VLASYGDVYV SDAFGTAHRD SATMTGIPKV
     LGAGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IQLLDNMLGR INYLVIGGAM
     AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERNVQVF LPVDHVCNKE FKAADSPLVT
     ESVDVPDGYM ALDIGPRTIH MYEEVIGRCK SAIWNGPMGV FEMPCYSKGT FAVAKAMGTG
     TQKNGLMSII GGGDSASAAE LSGEAKNMSH VSTGGGASLE LLEGKTLPGV AILTDRE