PGK_PENCH
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-AUG-2022, entry version 94.
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 PRIDE; 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 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 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