PGK_PENCI
ID PGK_PENCI Reviewed; 417 AA.
AC P33161;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=PGKA; Synonyms=PGK;
OS Penicillium citrinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5077;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8431954; DOI=10.1007/bf00352012;
RA Nara F., Watanabe I., Serizawa N.;
RT "Cloning and sequencing of the 3-phosphoglycerate kinase (PGK) gene from
RT Penicillium citrinum and its application to heterologous gene expression.";
RL Curr. Genet. 23:134-140(1993).
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:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; S54965; AAB25344.1; -; Genomic_DNA.
DR PIR; S28922; S28922.
DR AlphaFoldDB; P33161; -.
DR SMR; P33161; -.
DR PRIDE; P33161; -.
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..417
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145885"
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 171
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 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 44074 MW; 6944E3D9C1082B0F CRC64;
MSLSNKLPVT DVDLKGKRVL IRVDFNVPLD ENKNVTNPQR IVGALPTIKY AIDNGAKAVV
LMSHLGRPDG KVNPKYSLKP VVPVLEKLLG KSVTFAEDCV GPQTEETVNK ASDGQVILLE
NLRFHAEEEG SSKDAEGKKV KADKADVDAF RKGLTALGDV YVNDAFGTAH RAHSSMVGVD
LPQKAAGFLV KKELEYFAKA LESPARPFLA ILGGAKVSDK IQLIDNLLPK VNSLIITGGM
AFTFKKTLEN VKIGNSLFDE AGSKIVGEIV EKAKKYNVEI VLPVDYVTAD KFSADATVGA
ATDATGIPDG YMGLDVGPES VKLYQKTIAE AKTILWNGPP GVFELKPFAS ATEATLDAAV
KAAESGSIVI IGGGDTATVA AKYKVEDKIS HVSTGGGASL ELLEGKELPG VAALSSK