PGK_HYPJE
ID PGK_HYPJE Reviewed; 416 AA.
AC P14228;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk1; Synonyms=pgk;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=2670282; DOI=10.1007/bf00435504;
RA Vanhanen S., Penttilae M., Lehtovaara P., Knowles J.K.C.;
RT "Isolation and characterization of the 3-phosphoglycerate kinase gene (pgk)
RT from the filamentous fungus Trichoderma reesei.";
RL Curr. Genet. 15:181-186(1989).
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; X15764; CAA33770.1; -; Genomic_DNA.
DR PIR; S07803; TVTQGR.
DR AlphaFoldDB; P14228; -.
DR SMR; P14228; -.
DR PRIDE; P14228; -.
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..416
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145890"
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 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 44406 MW; 72195841EAB7A4D7 CRC64;
MSLSNKLSIT DVDLKGKRVL IRVDFNVPLD ENKKITNNQR IVGAIPTIKH ALDNGAKAVV
LMSHLGRPNG AVNPKYSLKP VVPELERLLG KPVTFARDCV GPEVESIVND ADNGAVILLE
NLRFHIEEEG SAKDKDGNKT KADKAKVEEF RKGLTALGDI YINDAFGTAH RAHSSMVGVD
LPQKAAGFLM KKELDYFAKA LESPQRPFLA ILGGAKVSDK IQLIDNLLDK VDTLIVCGGM
AFTFKKVLNN IPIGTSLFDE AGAKTCPSCR EAKAKNVKLV LPVDYITADK FDKDANTGTA
TDESGIPDGW MGLDCGEKSI ELYKEAIADA KTILWNGPAG VFEFDKFANG TKATLDAVVE
GCKNGKIVII GGGDTATVAA KYGVEDKLSH VSTGGGASLE LLEGKELPGV VALSSK