ID   PGK_HYPRU               Reviewed;         417 AA.
AC   P24590;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-MAY-2023, entry version 96.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk1; Synonyms=pgk;
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T9 BR47;
RX   PubMed=2251146; DOI=10.1093/nar/18.22.6717;
RA   Goldman G.H., Villarroel R., van Montagu M., Herrera-Estrella A.;
RT   "Sequence of the Trichoderma viride phosphoglycerate kinase gene.";
RL   Nucleic Acids Res. 18:6717-6717(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T9 BR47;
RX   PubMed=1588821; DOI=10.1111/j.1365-2958.1992.tb01562.x;
RA   Goldman G.H., Geremia R.A., Caplan A.B., Vila S.B., Villarroel R.,
RA   van Montagu M., Herrera-Estrella A.;
RT   "Molecular characterization and regulation of the phosphoglycerate kinase
RT   gene from Trichoderma viride.";
RL   Mol. Microbiol. 6:1231-1242(1992).
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; X54284; CAA38181.1; -; Genomic_DNA.
DR   PIR; S13596; S13596.
DR   PIR; S25381; S25381.
DR   AlphaFoldDB; P24590; -.
DR   SMR; P24590; -.
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..417
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145891"
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"
FT   CONFLICT        24..29
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  44381 MW;  99B7B75838C1805D CRC64;
     MSLSNKLSIT DVDVKGKRVL IRVDFNVPLD ENKNITNPQR IAGAIPTIKH ALDNGAKAVI
     LMSHLGRPNG AVNAKYSLKP VVPKLEELLG KPVTFAPDCV GPEVEAIVNK ADNGAVILLE
     NLRFHIEEEG SSKDKEGNKT KADKAKVEEF RKGLTALGDV YVNDAFGTAH RAHSSMVGVD
     LPQKAAGFLM KKELDYFAKA LESPQRPFLA ILGGAKVSDK IQLIDNLLDK VNTLIICGGM
     AFTFKKVLDN LAIGDSLFDK AGAETVPKLV EKAKAKNVKI VLPTDFITAD KFDKDANTGL
     ATDKDGIPDG WMGLDCGDES IKLYKEAIDE AKTILWNGPA GVFEFEKFAG GTKATLDAVV
     EGCKNGKIVI IGGGDTATVA AKYGVEDKLS HVSTGGGASL ELLEGKELPG VTALSSK
//