PGK_OPISI
ID PGK_OPISI Reviewed; 415 AA.
AC P50311;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGK;
OS Opisthorchis sinensis (Clonorchis sinensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=41765;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hong S.J.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; L47982; AAD10200.1; -; mRNA.
DR AlphaFoldDB; P50311; -.
DR SMR; P50311; -.
DR UniPathway; UPA00109; UER00185.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; ISS: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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..415
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145845"
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 415 AA; 44658 MW; 13168A6FB1FB20A0 CRC64;
MGLRKLSIAN VDLKDKRVLM RVDFNVPMKD GKVTNTQRIV GASPTIKYAL DKGAKSIVLM
SHLGGRVGNK VARYSLNPVG EEVSKLLGKP VKFLPDCVGP ETTEGMCQSS AGSVFLLENL
RFHVEEEGKG VSPTGEKIKA TPEQVKAFSE NLTKLGDVYL NDAFGTAHRA HASMVGCRLT
QRACGFLMDK ELTYFSKLLD QPQHPFLAII GGAKVSDKIQ LIKNMLDKVD ELIITGGMAF
TFLKKLHNMK IGKSLYDEPG AAIVDEWMQL AKSKNVKIHL PVDFITGDKF AEDANTGTAT
VEPGIRDTHM GLDGGPKTME EFCKVISRAK TIVWNGPMGV FEMEKFAGGT KAAMDAVVAA
TTKGVTNNNG GGDTATCCPK WKTEAQVSHV STGVGASLEL LEGKQLPGIL ALSDA