ID   PGK_PENCH               Reviewed;         415 AA.
AC   P09188;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-MAY-2023, entry version 97.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=PGKA; Synonyms=PGK;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GB 533;
RX   PubMed=3145495; DOI=10.1093/nar/16.24.11823;
RA   van Solingen P., Muurling H., Koekman B., van den Berg J.;
RT   "Sequence of the Penicillium chrysogenum phosphoglycerate kinase gene.";
RL   Nucleic Acids Res. 16:11823-11823(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC   STRAIN=ATCC 9480 / CBS 307.48 / NRRL 1951 / GB8 / QM 941;
RX   PubMed=8190080; DOI=10.1007/bf00301062;
RA   Hoskins I.C., Roberts C.F.;
RT   "Expression of the 3-phosphoglycerate kinase gene (pgkA) of Penicillium
RT   chrysogenum.";
RL   Mol. Gen. Genet. 243:270-276(1994).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; X13379; CAA31756.1; -; Genomic_DNA.
DR   EMBL; S71096; AAB30809.1; -; Genomic_DNA.
DR   PIR; S02040; TVPLGC.
DR   AlphaFoldDB; P09188; -.
DR   SMR; P09188; -.
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; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 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..415
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145884"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
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;  44022 MW;  508AC3F76CE35E81 CRC64;
     MSLSNKLPVT DVDLKGKRVL IRVDFNVPLD ENENVTNPQR IVGALPTIKY AIDNGRKAVV
     LMSHLGRPDG KVNPKYSLKP VVPVLEELLG KSVTFTEDCI GPQTEETVNK ASDGQVILLE
     NLRFHAEEEG SSKDAEGKKV KADKADVDRS ASLTALGDVY VNDAFGTAQR AHSSMVGVDL
     PQKAAGFLVK KELEYFAKAL ESPARPFLAI LGGAKVSDKI PVIDNLLPKV NSLIIIGGMA
     LTFKKTLENV KIGNSLFDEA GSKILGEIVE KAKKHNVEIV LPVDYVTADK FSADATVGSA
     TTQRIPDGYM GSDVGPESVK LYQKTIAEAK TILWNGPPGV FELKPSPRPT EATLDAAVKA
     AESGSIVIIG GGDTATVAAK YKAEDKISHV STGGGASLEL LEGKELPGVA ALSSK
//