ID   PGK_SCHMA               Reviewed;         416 AA.
AC   P41759;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000303|PubMed:7477104};
DE            Short=PGK {ECO:0000303|PubMed:7477104};
DE            EC=2.7.2.3 {ECO:0000269|PubMed:7477104};
GN   Name=PGK;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NMRI;
RX   PubMed=7477104; DOI=10.1016/0166-6851(95)91598-o;
RA   Lee K.W., Shalaby K.A., Thakur A., Medhat A.M., Karim A.M., Loverde P.T.;
RT   "Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni
RT   and characterization of its gene product.";
RL   Mol. Biochem. Parasitol. 71:221-231(1995).
CC   -!- FUNCTION: Involved in the seventh step in glycolysis (PubMed:7477104).
CC       Catalyzes the conversion of 1,3-bisphosphoglycerate ((2R)-3-phospho-
CC       glyceroyl phosphate) to 3-phosphoglycerate ((2R)-3-phosphoglycerate)
CC       and results in the formation of ATP (PubMed:7477104). Associated with
CC       the tegument to provide the energy needed for the tegumental repair
CC       resulting from immune damage (PubMed:7477104).
CC       {ECO:0000269|PubMed:7477104, ECO:0000303|PubMed:7477104}.
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         Evidence={ECO:0000269|PubMed:7477104};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14803;
CC         Evidence={ECO:0000305|PubMed:7477104};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Expressed in all cells of the worm (at protein
CC       level), higher expression in the cells associated with the tubercles
CC       (tegumental modifications), the muscle and along the tegument.
CC       {ECO:0000269|PubMed:7477104}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; L36833; AAA93516.1; -; mRNA.
DR   AlphaFoldDB; P41759; -.
DR   SMR; P41759; -.
DR   STRING; 6183.Smp_018890.1; -.
DR   EnsemblMetazoa; Smp_214060.1; Smp_214060.1; Smp_214060.
DR   EnsemblMetazoa; Smp_307440.1; Smp_307440.1; Smp_307440.
DR   WBParaSite; Smp_214060.1; Smp_214060.1; Smp_214060.
DR   WBParaSite; Smp_307440.1; Smp_307440.1; Smp_307440.
DR   eggNOG; KOG1367; Eukaryota.
DR   HOGENOM; CLU_025427_1_0_1; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   ExpressionAtlas; P41759; baseline.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; NAS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 3.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
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   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glycolysis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..416
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145846"
FT   BINDING         23..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
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         371..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  44508 MW;  28DB11837F7EF9CB CRC64;
     MGLSKLSISD VDLKGKRVLI RVDFNVPMKD GKVTNTQRIA AAIPTIKYAL DKGAKSVVLM
     SHLGRPDGHK VDKYSLKPVC PEVSKLLGKE VTFLNDCVGP DVVNACANPA PGSVFLLENL
     RFHVEEEGKG VSPTGEKTKA TADQIKAFSE SLTKLGDVYV NDAFGTAHRA HASMVGCQLP
     QKACGFLMNK ELTYFAKALE NPERPFLAIL GGAKVSDKIQ LINNMLDKVN ELIIGGGMAY
     TFLKQIHNMH IGNSLFDAPG AEIVHKVMET AKAKNVAIHL PVDFVTADKF ADDANTEIRT
     IQSGIADGWM GLDIGPKTIE EFSKVISRAK TIVWNGPMGV FEMDKFATGT KAAMDEVVKA
     TKNGATTIIG GGDTATCCAK WDTEDKVSHV STGGGASLEL LEGKQLPGVV ALTDAH