ID   PGKB_LEIME              Reviewed;         417 AA.
AC   Q27684;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 86.
DE   RecName: Full=Phosphoglycerate kinase, cytosolic;
DE            EC=2.7.2.3;
DE   AltName: Full=Phosphoglycerate kinase B;
GN   Name=PGKB;
OS   Leishmania mexicana.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MHOM/BZ/84/BEL46;
RX   PubMed=9497040; DOI=10.1016/s0166-6851(97)00152-7;
RA   Adje C.A., Opperdoes F.R., Michels P.A.M.;
RT   "Organization, sequence and stage-specific expression of the
RT   phosphoglycerate kinase genes of Leishmania mexicana mexicana.";
RL   Mol. Biochem. Parasitol. 90:155-168(1997).
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; X98486; CAA67112.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q27684; -.
DR   SMR; Q27684; -.
DR   VEuPathDB; TriTrypDB:LmxM.20.0100; -.
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   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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..417
FT                   /note="Phosphoglycerate kinase, cytosolic"
FT                   /id="PRO_0000145855"
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;  44968 MW;  F79168E2C90C166D CRC64;
     MSLVLKKSID DVALKDKKVL IRVDFNVPVK NGEITNDFRI RSALPTIQKV LKEGGSCILM
     SHLGRPKGAR MSDPKPEKGV RGYEEAATLR PVAARLSELL EEKVAKAPDC LNASIYVSKL
     KRGDVLLLEN VRFYTEEGSK KEEEADAMAK VLASYADLYV SDAFGTAHRD SATMTGIPKV
     LGSGYAGYLM EKEINYFSRV LNNPPRPLVA IVGGAKVSDK IELLDNMLGR INYLVIGGAM
     AYTFQKAQGR KIGISMCEED KLDLAKSLLK KAQERGVQVL LPVDHVCNKE FKAVDSPLVT
     EDVDVPDGYM ALDIGPKTIH MYEEVIGRCK SAIWNGPMGV FEMPCISKGT FAVAKAMGTG
     TQKDGLLSII GGGDTASAAE LSARAKNMSH VSTGGGASLE LLEGKTLPGV AILTDKQ
//